MXPA01003461A - Hypersensitive response elicitor fragments which are active but do not elicit a hypersensitive response. - Google Patents

Abstract

The present invention is directed to isolated active fragments of a hypersensitive response elicitor protein or polypeptide which fragment does not elicit a hypersensitive response in plants. Also disclosed are isolated DNA molecules which encode such fragments. Isolated fragments of hypersensitive response elicitor proteins or polypeptides in accordance with the present invention and the isolated DNA molecules that encode them have the following activities: imparting disease resistance to plants, enhancing plant growth, and/or controlling insects on plants. This can be achieved by applying the fragments of a hypersensitive response elicitor in a non-infectious form to plants or plant seeds under conditions effective to impart disease resistance, to enhance plant growth, and/or to control insects on plants or plants grown from the plant seeds. Alternatively, transgenic plants or plant seeds transformed with a DNA molecule encoding the fragment can be provided and the transgenic plants or plants resulting from the transgenic plant seeds are grown under conditions effective to impart disease resistance, to enhance plant growth, and/or to control insects on plants or plants grown from the plant seeds.

Description

FRAI3MENT0S OF THE PROMOTER OF L? HYPERSENSITIVE RESPONSE THAT ARE ACTIVE, BUT NOT PROMOTE AN ANSWER HYPERSENSITIVE The present invention relates to the active fragments of a hypersensitive response promoter, which do not promote a hypersensitive response.

BACKGROUND OF THE INVENTION 10 The interactions between bacterial pathogens and their host or plant hosts are generally in two categories: (1) compatible (host-pathogen), which leads to intercellular bacterial development, development 15 of symptoms, and development of the disease in the host plant; and (2) incompatible (pathogen-non-host), resulting in the hypersensitive response, a particular type of incompatible interaction that occurs, with no symptoms of progressive disease. During the 20 compatible interactions on host plants, bacterial populations increase rapidly and progressive symptoms occur. During incompatible interactions, bacterial populations do not increase, and progressive symptoms do not occur.

REF: 128463 - ----- "" - The hypersensitive response is a rapid localized necrosis that is associated with the active defense of plants against many pathogens (Kiraly, Z., "Defenses Triggered by the Invader: Hypersensitivity", 5 pages 201- 224 in: Plant disease: An Advanced Treatise, Vol. 5, JG Horsfall &EB Cowling, Academic Press New York (1980), Klement, Z. "Hipersensibity", pages 149-177 in: Phytopathogenic Prokaryotes)), Vol. 2, MS Mount & G.H. Lacy, ed Academic Press, New York (1982)). The hypersensitive 0 response promoted by bacteria is easily observed as a tissue collapse if high concentrations (> 107 cells / ml) of a limited range of host pathogen, such as Pseudomonas syringae or Erwin ia amylovora are infiltrated in the leaves of plants 5 host (necrosis occurs only in isolated plant cells at lower inoculum levels) (Klement Z., "Rapid Detection of Pathogenicity of Phytopathogenic Pseudomonas", Nature 199: 299-300, Klement et al., "Hypersensibity Reaction Induced by Phytopathogenic 0 Bacteria in the Tobacco Leaf ", Phytopathology 54: 474-477 (1963); Turner et al.," The Quantitative Relation Between Plant and Bacterial Cells Involved in the Hypersensitive Reaction ", Phytopathology 64-885-890 (1974): Klement. Z. "Hypersensibity" pages 149-177 in 5 Phytopathogenic Prokaryotes, Vol. 2, MS Mount and GH "» "* '-"' - - -.-> Lacy, ed. Academic Press, New York (1982).) The abilities to promote the hypersensitive response in a non-host and to be pathogenic in a host, seem to be As noted by Klement Z. "Hypersensivity" 5 pages 149-177 in Phytopathogenic Prokaryotes, Vol 2, MS Mount and GH Lacy, ed., Academic Press New York, these pathogens also cause physiologically similar, albeit retarded, necrosis in their interactions with compatible guests, and the ability to produce The hypersensitive response or pathogenesis is dependent on a common group of genes, denoted hrp (Lindgren, PB and collaborators "Gene Cluster of Pseudomonas syringae pv. 'Phaseolicola' Controls Pathogenicity of Bean Plants and Hypersensitivity on Nonhost Plants" J. Bacteriol. 168-512-22 15 (1986); Willis, D. K. et al, "hrp Genes of Phytopathogenic Bacteria" Mol. Plant-Microbe Interact 4: 132-138 (1991)). Consequently, the hypersensitive response can hold the keys to the nature of the defense of the plant and the basis for the 20 bacterial pathogenicity. The hrp genes are very widespread in Gram-negative plant pathogens, where they accumulate, and are conserved and in some cases interchangeable (Willis, D. K. et al., "Hrp Genes of Phytopathogenic 25 Bacteria ", Mol Plant-Microbe Interact 4: 132-138 (1991); ^ gj ^ ggg Bones, U, "hrp Genes of Phytopathogenic Bacteria," pages 79-98 in: Current Topics in Microbiology and Immunology; Bacterial Pathogenesis of Plants and Animáis - Molecular and Cellular Mechanisms, J. L. Dangl, ed. Springer Verlag, Berlin (1994)). Several hrp genes code for the components of a protein secretion pathway, similar to one used by Yersinia, Shigella, and Salmonella spp., To secrete essential proteins in animal diseases (Van Gijsegem et al., "Evolution Conservation of Pathogenicity Determinants Among Plant and Animal Pathogenic Bacteria ", Trends Microbiol 1: 175-180 (1993)). In E. amylovora, P. syringae, and P. solana cearum, hrp genes have been shown to control the production and suppression of glycine-rich protein promoters of the hypersensitive response (He, SY et al., "Pseudomonas Syringae pv. Syringae HarpirPss: a Protein that is Secreted via the Hrp Pathway and Elicits the Hypersensitive Response in Plants ", Cell 73: 1255-1266 (1993), Wei, Z, H., and collaborators," Hrpl of Erwinia amylovora Functions in Secretion of Harpin and is a Member of a New Protein Family ", J. Bacteriol 175-7958-7967 (1993); Arlat M. and collaborators" PopAl, a protein Which Induces a Hypersensitive-like Response on Specific Petunia Genotypes, is Secretd via the Hrp Pathway of Pseudomonas solanacearum "EMBO J. 13: 543-553 (1994)).

The first of these proteins was discovered in E. amylovora Ea321, a bacterium that causes the fire rust of pink plants, and was designated harpin (Wei ZM, and collaborators, Harpin Elicitor of the Hypersensitive Response Produced by the Plant Pathogen Erwinia amylovora "Science 257: 85-88 (1992)). Mutations in the hrpN coding gene revealed that harpin is required for E. Amylovora, to promote a hypersensitive response in non-host tobacco leaves and incite disease symptoms in highly susceptible pears. The PopAl protein of P. Solanacearum GMI1000 has similar physical properties and also promotes hypersensitive response in leaves of tobacco, which is not a host of that strain (Arlat et al. "PopAl, a Protein Which Induces a Hypersensitive-like Response on Specific Petunia Genotypes ís Secreted via the Hrp Pathawy of Pseudomonas solana cearum "EMBO J. 13: 543-53 (1994)). However, the mutants of P. Solanacearum PoPAl GMI1000 also promote the hypersensitive response in tobacco and promote the disease in tomato. Thus, the role of these glycine-rich hypersensitive response promoters can vary widely in Gram negative plant pathogens. Other hypersensitive response promoters, plant pathogens, have been isolated, cloned and r-1-iitírr. sequenced These include: Erwinia chrysanthemi (Bauer et al. * Erwinia chrysanthemi HarpinECh 'Soft-Rot Pathogenesis', MPM I 8 (4): 484-91 (1995)), Erwinia carotovora (Cui, and collaborators xThe RsmA "Mutants of Erwinia carotovora subsp carotovora Strain Ecc71 Overexpress hrpNcc and Elicit a Hypersensitive Reaction-like Response in Tobacco Leaves ", MPMI9 (7): 565-73 (1996)); Erwinia stewartii (Ahmad et al, wHarpin is not necessary for the Pathogenicity of Erwinia stewartii on Maize "8 ^ Int." Cong. Molec. Plant-Microb, inter, July 14-19, 1996 and Ahmad, et al, 'Harpin is not Neccesary for the Pathogenicity of Erwinia stewartii on Maize "Ann. Mt. Am. Phytopath Soc. Julio 27-31, 1996) and Pseudomonas syringae pv. Syringae (WO 94/26782 to Cornell Research Foundation, Inc.) The present invention seeks to identify fragments of protein or polypeptide promoter of the hypersensitive response, which do not promote a hypersensitive response but that are active when or being used together with plants.

BRIEF DESCRIPTION OF THE I-NVENTION The present invention is directed to isolated fragments of a hypersensitive response-enhancing polypeptide or protein from Erwinia, whose fragments do not promote a hypersensitive response in plants but are otherwise active when used in conjunction with plants. . Also isolated are DNA molecules encoding such fragments. Fragments of the hypersensitive response promoters according to the present invention have the following activity when used in conjunction with plants: imparting disease resistance to plants, improving the development of the plant and / or controlling the insects. This involves the application of 10 the fragments in a non-infectious way to the plants or the seeds of the plants, under conditions effective to impart resistance against the disease, to increase the development of the plants, and / or to control the insects on the plants, or the plants developed 15 from the seeds of plants. As an alternative to applying the fragments to the plants or to the seeds of plants in order to impart resistance to the disease, to increase the development of the plant, and / or to control the insects 20 about plants, transgenic plants or plant seeds can be used. When transgenic plants are used, this involves the provision of a transgenic plant transformed with a DNA molecule that codes for a fragment of a polypeptide or protein. 25 hypersensitive response promoter, according to the present invention, and the development of the plant under conditions effee to impart resistance against the disease, to improve plant development, and / or to control insects in plants, or plants developed from the seeds of the plant. Alternatively, a transgenic plant seed transformed with the DNA molecule encoding such a fragment can be provided and seeded in the soil. A plant is then propagated under effee conditions 10 to impart resistance against the disease, to increase the development of the plant and / or to control insects on plants or plants developed from plant seeds. 15 BRIEF DESCRIPTION OF THE DRAWINGS Figure 1 shows the truncated proteins of the polypeptide or hypersensitive response promoter protein. Figure 2 shows a list of oligonucleotide primers synthesized for the construn of truncated harpin proteins. N represents the N-terminus (5 'region), and C represents the C-terminus (3' region). The primers correspond to the identification numbers of Sequences indicated, for the present application: NI (SEQ.

M ^ ggl ID No. 1), N76 (SEQ ID No. 2), N99 (SEQ ID No. 3), N105 (SEQ, ID No. 4), N110 (SEQ ID No. 5), N137 (SEQ ID No. 6), N150 (SEQ ID No. 7), N169 (SEQ ID No. 8), N210 (SEQ D. No. 9), N267 (SEQ ID No. 10), N343 (SEQ ID No. 11), C75 (SEQ ID No. 12), C104 (SEQ ID No. 13), C168 (SEQ ID No. 14), C180 ( SEQ ID No. 15), C204 (SEQ ID No. 16), C209 (SEQ ID No. 17), C266 (SEQ ID No. 18), C342 (SEQ ID No. 19) , and C403 (SEQ ID No. 20).

DETAILED DESCRIPTION OF THE INVENTION The present invention is directed to the fragments isolated to a hypersensitive response promoter or polypeptide protein, where the fragments do not promote a hypersensitive response but have other aity in the plants. Also described are DNA molecules that code for various fragments, as well as expression systems, host cells, and plants that contain such molecules. The uses of the fragments themselves and of the DNA molecules that encode them are also described. The fragments of the polypeptides or proteins that promote the hypersensitive response, according to the present invention, are derivatives of the polypeptides or proteins that promote the hypersensitive response of a wide variety of fungal and bacterial pathogens. Such polypeptides or proteins are capable of promoting local necrosis in the plant tissue contacted by the promoter. Examples of bacterial suitable sources 5 of the polypeptide or protein promoters include Erwinia, Pseudomonas, and Xanthomonas species (for example, the following bacteria: Erwinia amylovora, Erwinia chrysanthemi, Erwinia stewartii, Erwinia carotovora, Pseudomonas syringae, Pseudomonas solancearum, Xanthomonas 10 campestris, and mixtures thereof). An example of a fungal source of a protein or polypeptide promoting the hypersensitive response is Phytophthora. Suitable species include Phytophthora Phytophthora parasitica, Phytophthora cryptogea, Phytophthora cinnamomi 15, Phytophthora ici caps, Phytophthora megasperma, and Phytophthora citrophthora. The polypeptide or protein promoter of the hypersensitive response of Erwinia chrysanthemi has an amino acid sequence corresponding to SEQ. ID. No. 20 21 as follows: i? r? rtwnrÉIBMÉlnt? r • • • - • - - - - - - "....... m. ' - TNSS ut Met Gln lie Thr He Lys Ala His He Gly Gly Asp Leu Gly Val Ser 1 May 10 15 Gly Leu Gly Ala Gln Gly Leu Lys Gly Leu Asn Ser Ala Ala Ser Ser 20 25 30 Leu Gly Ser Ser Val Asp Lys Leu Be Ser Thr He Asp Lys Leu Thr 35 40 45 Ser Ala Leu Thr Ser Met Met Phe Gly Gly Ala Leu Ala Gln Leu Gly Gly 50 55 60 Ala Ser Ser Leu Gly Lys Gly Met Ser Asn Gln Leu Gly Gln Ser 65 70 75 80 Ph Gly Asn Gly Wing Gln Gly Wing Being Asn Leu Leu Being Val Pro Lys 85 90 95 Asp Wing Leu Ser Lys Met Phe Asp Lys Wing Leu Asp Asp 100 105 110 Leu Leu Gly His Asp Thr Val Thr Lys Leu Thr Asn Gln Ser Asn Gln 115 120 125 Leu Wing Asn Being Met Leu Asn Wing Being Gln Met Thr Gln Gly Asn Met 130 135 140 Asn Ala Phe Gly Ser Gly Val Asn Asn Ala Leu Ser Ser He Leu Gly 14Í. 150 155 160 Like »Gly Leu Gly Gln Being Met Being Gly Phe Being Gln Pro Being Leu Gly 165 170 175 Wing Gly Gly Leu Gln Gly Leu Gly Wing Wing Gly Wing Phe Asn Gln Leu 180 185 190 Gly Asn Wing He Gly Met Gly Val Gly Gln Asn Wing Wing Leu Wing 195 200 205 - Leu Ser Asn Val Ser Thr His Val Asp Gly Asn Asn Arg His Phe Val 210 215 220 Asp Lys Glu Asp Arg Gly Met Wing Lys Glu He Gly Gln Phe Met Asp 225 230 235 240 Glr. Tyr Pro Glu He Phe Gly Lys Pro Glu Tyr Gln Lys Asp Gly Trp 245 250 255 Ser Ser Pro Lys Thr Asp Asp Lys Ser Trp Ala Lys Ala Leu Ser Lys 260 265 270 Prc Asp Asp Asp Gly Met Thr Gly Ala Ser Met Asp Lys Phe Arg Gln 275 280 285 Wing Met Gly Met He Lys Ser Wing Val Wing Gly Asp Thr Gly Asn Thr 290 295 300 Asn Leu Asn Leu Arg Gly Wing Gly Gly Wing Being Leu Gly He Asp Wing 305 310 315 320 Wing Val Val Gly Asp Lys He Ala Asn Met Ser Leu Gly Lys Leu Ala 325 330 335 Asn Ala This polypeptide or hypersensitive response promoter protein has a molecular weight of 34 kDa, is heat stable, has a glycine content greater than 16%, and does not substantially contain cysteine. The hypersensitive response polypeptide or protein of Erwinia chrysan themi is encoded by a DNA molecule having a nucleotide sequence corresponding to SEQ. ID. No. 22 as follows: CGATTTTACC CGGGTGAACG TGCTATGACC GACAGCATCA CGGTATTCGA CACCGTTACG 60 GCGTTTATGG CCGCGATGAA CCGGCATCAG GCGGCGCGCT GGTCGCCGCA ATCCGGCGTC 120 GATCTOGTAT TTCAGTTTGG GGACACCGGG CGTGAACTCA TGATGCAGAT TCAGCCGGGG 1T0 CAGCATATC CCGGCATGTT GCGCACGCTG CTCGCTCGTC GTTATCAGCA GGCGGCAGAG 240 TGCGATGGCT GCCATCTGTG CCTGAACGGC AGCGATGTAT TGATCCTCTG GTGGCCGCTG 300 CCGTCGGATC CCOGCAGTTA TCCGCAGGTG ATCGAACGTT TGTTGAACT GGCGGGAATG 360 ACGTTGCCGT CGCTATCCAT AGCACCGACG GCGCGTCCGC AGACAGGGAA CGGACGCGCC 420 CGATCATTAA GATAAAGGCG GCTTTTTTTA TTGCAAAACG GTAACGGTGA GGAACCsTTT 480 CACCGTCGGC GTCACTCAGT AACAAOTATC CATCATGATG CCTACATCGG GATCGGCGTG 540 GGCATCCGTT GCAGATACTT TTGCGAACAC CTGACATGAA TGAGGAAACG AAATTATGCA 600 AÍTTACGATC AAAGCGCACA TCGC-CGGTGA TTTGGGCGTC TCCGGTCTGG GGCTGGGTGC 660 TCAGGGACTG AAAGGACTGA ATTCCGCGGC TTCATCGCTG GGTTCCAGCG TGGATAAACT 720 GÍGCAGCACC ATCGATAAGT TGACCTCCGC GCTGACTTCG ATGATGTTTG GCGGCGCGCT 780 GCCGCAGGGG CTGGGCGCCA GCTCGAAGGG GCTGGGGATG AGCAATCAAC TGGGCCAGTC 840 TTTCGGCAAT GGCsCGCAGG GTGCGAGCAA CCTGC7ATCC GTACCGAAAT CCGGCGGCGA 900 TGCGTTGTCA AAAATGTTTG ATAAAGCGCT GGACGATCTG CTGGGTCATG ACACCGTGAC 960 C? AGCTGACT AACCAGAGCA ACCAACTGGC TAATTCAATG CTGAACGCCA GCCAGATGAC 1020 CCAGGGTAAT ATGAATGCGT TCGGCAGCGG TGTGAACAAC GCACTGTCGT CCATTCTCGG 1080 CA ^ CGGTCTC GGCCAGTCGA TGAGTGGCTT CTCTCAGCCT TCTCTGGGGG CAGGCGGCTT 1140 GC AGGGCCTG AGCGGCGCGG GTGCATTCAA CCAGTTGGGT AATGCCATCG GCATGGGCGT 1200 GGGGCAGAAT GCTGCGCTGA GTGCGTTGAG TAACGTCAGC ACCCACGTAG ACGGTAACAA 1260 CCGCCACTTT GTAGATAAAG AAGATCGCGG CATGGCGAAA GAGATCGGCC AGTTTATGGA 1320 TC? GTATCCG GAAATATTCG GTAAACCGGA ATACCAGAAA GATGGCTGGA GTTCGCCGAA 1380 GACGGACGAC AAATCCTGGG CTAAAGCGCT GAGTAAACCG GATGATGACG GTATGACCGG 1440 CGCCAGCATG GACAAATTCC GTCAGGCGAT GGGTATGATC AAAAGCGCGG TGGCGGGTGA 1500 TA CGGCAAT ACCAACCTGA ACCTGCGTGG CGCGGGCGGT GCATCGCTGG ? GTATCGATGC 1560 GGCTGTCGTC GGCGATAAAA TAGCCAACAT GTCGCTGGsT AAsCTGGCCA ACGCCTGATA 1620 ATCTGTGCTG GCCTGATAAA GCGGAAACGA AAAAAGAGAC GGGGAAGCCT GTCTCTTTTC 1680 TT TTATGCG GTTTATGCGG TTACCTGGAC CGGTTAATCA TCGTCATCGA TCTGGTACAA 1740 ACGCACATTT TCCCGTTCAT TCGCGTCGTT ACGCGCCACA ATCGCGATGG CATCTTCCTC 1800 GTC: GCTCAGA TTGCGCGGCT GATGGGGAAC GCCGGGTGGA ATATAGAGAA ACTCGCCGGC 1860 CAOATGGAGA CACGTCTGCG ATAAATCTGT GCCGTAACGT GTTTCTATCC GCCCCTTTAG_1920_CACiATAGATT GCGGTTTCGT AATCAACATG GTAATGCGGT TCCGCCTGTG CGCCGGCCG G 1980 GATCACCACA ATATTCATAG AAAGCTGTCT TGCACCTACC GTATCGCGGG AGATACCGAC 2040 AAÍATAGGGC AGTTTTTTGCG TGGTATCCGT GGGGTGTTCC GGCCTGACAA TCTTGAGTTG 2100 GTTCGTCATC ATCTTTCTCC ATCTGGGCGA CCTGATCGGT T 2141 ^ aifeAal ^ * > - - - - .. L. ,. . * -. . ,. -. .-. . rii ^ - The polypeptide or hypersensitive response promoter protein derived from Erwinia amylovora has an amino acid sequence corresponding to SEQ. ID No. 23 as follows: M «t Ser Leu Asn Thr Ser Gly Leu Gly Wing Being Thr Met Gln He Ser 1 5 10 15 He Gly Gly Wing Gly Gly Asn Asn Gly Leu Leu Gly Thr Being Arg Gln 20 25 30 Asn Wing Gly Leu Gly Gly Asn Wing Leu Gly Leu Gly Gly Gly Asn 35 40 45 Gln Asn Asp Thr Val Asn Gln Leu Wing Gly Leu Leu Thr Gly Met Met 50 55 60 Met Met Met Met Met Met Gly Gly Gly Gly Leu Met Gly Gly Gly Leu 65 70 75 80 G2 .and Gly Gly Leu Gly Asn Gly Leu Gly Gly Ser Gly Gly Leu Gly Glu 85 90 95 G] and Leu Ser Asn Ala Leu Asn Asp Met Leu Gly Gly Ser Leu Asn Thr 100 105 110 Le u Gly Ser Lys Gly Gly Asn Asn Thr Thr Ser Thr Thr Asn Ser Pro 115 120 125 Leu Asp Gln Wing Leu Gly He Asn Ser Thr Ser Gln Asn Asp Asp Ser 130 135 140 Thr Ser Gly Thr Asp Ser Thr Ser Asp Ser Ser Asp Pro Met Gln Gln 145 150 155 160 Leu Leu Lys Met Phe Ser Glu He Met Gln Ser Leu Phe Gly Asp Gly 165 170 175 Gln Asp Gly Thr Gln Gly Being Ser Gly Gly Lys Gln Pro Thr Glu 180 185 190 Gl and Glu Gln Asn Ala Tyr Lys Lys Gly Val Thr Asp Ala Leu Ser Gly 195 200 205 Leu Met Gly Asn Gly Leu Ser Gln Leu Leu Gly Asn Gly Gly Leu Gly 210 215 220 Gly Gly Gln Gly Gly Asn Wing Gly Thr Gly Leu Asp Gly Ser Ser Leu 225 230 235 240 Gly Gly Lys Gly Leu Gln Asn Leu Ser Gly Pro Val Asp Tyr Gln Gln 245 250 255 Le > u Gly Asn Wing Val Gly Thr Gly He Gly Met Lys Wing Gly He Gln 260 265 270 AJ.a Leu Asn Asp He Gly Thr His Arg His Being Ser Thr Arg Ser Phe 275 280 285 Val Asn Lys Gly Asp Arg Ala Met Ala Lys Glu He Gly Gln Phe Met 290 295 300 Asp Gln Tyr Pro Glu Val Phe Gly Lys Pro Gln Tyr Gln Lys Gly Pro 305 310 315 320 G and Gln Glu Val Lys Thr Asp Asp Lys Ser Trp Ala Lys Ala Leu Ser 325 330 335 Lys Pro Asp Asp Asp Gly Met Thr Pro Wing Being Met Glu Gln Phe Asn 340 345 350 Lys Wing Lys Gly Met He Lys Arg Pro Met Wing Gly Asp Thr Gly Asn 355 360 365 Gly Asn Leu Gln Wing Arg Gly Wing Gly Gly Being Ser Leu Gly He Asp 370 375 380 AJ.a Met Met Wing Gly Asp Wing He Asn Asn Met Wing Leu Gly Lys Leu 3 £ I5 390 395 400 Gly Ala Wing This polypeptide or hypersensitive response promoter protein has a molecular weight of about 39 kDa, has a pl of about 4.3, and is heat stable at 100 ° C for at least 10 minutes. This polypeptide or response-promoting protein ^^^^ or hypersensitive has substantially no cysteine. The polypeptide or hypersensitive response promoter protein derived from Erwinia amylovora is more fully described in Wei, Z. -M, R.J. Laby, C.H. Zumoff, D.W. Bauer, S.-Y., He, A. Collmer, and S.V. Beer, "Harpin, Elicitor of the Hypersensitive Response Produced by tha Plant Pa thogen Erwinia amylovora", Science 257: 85-88 (1992), which is incorporated by reference herein. The DNA molecule encoding this polypeptide or protein has a nucleotide sequence corresponding to SEQ. ID No. 24 as follows: AAGC TCGGC ATGGCACGTT TGACCGTTGG GTCGGCAGGG TACGTTTGAA TTATTCATAA 60 GAGGAATACG TTATGAGTCT GAATACAAGT GGGCTGGGAG CGTCAACGAT GCAAATTTCT 120 ATCGGCGGTG CGGGCGGAAA TAACGGGTTG CTGGGTACCA GTCGCCAGAA TGCTGGGTTG 180 GGTGGCAATT CTGCACTGGG GCTGGGCGGC GGTAATCAAA ATGATACCGT CAATCAGCTG 240 GCTGGCTTAC TCACCGGCAT GATGATGATG ATGAGCATGA TGGGCGGTGG TGGGCTGATG 300 GGCGGTGGCT TAGGCGGTGG CTTAGGTAAT GGCTTGGGTG GCTCAGGTGG CCTGGGCGAA 360 GGACTGTCGA ACGCGCTGAA CGATATGTTA GGCGGTTCGC TGAACACGCT GGGCTCGAAA 420 GGCGGCAACA ATACCACTTC AACAACAAAT TCCCCGCTGG ACCAGGCGCT GGGTATTAAC 460 TCAACGTCCC AAAACGACGA TTCCACCTCC GGCACAGATT CCACCTCAGA CTCCAGCGAC 540 CCGATGCAGC AGCTGCTGAA GATGTTCAGC GAGATAATGC AAAGCCTGTT TGGTGATGGG 600 CAAGATGGCA CCCAGGGCAG TTCCTCTGGG GGCAAGCAGC CGACCGAAGG CGAGCAGAAC 660 GCCTATAAAA AAGGAGTCAC TGATGCGCTG TCGGGCCTGA TGGGTAATGG TCTGAGCCAG 720 CTCCTTGGCA ACGGGGGACT GGGAGGTGGT CAGGGCGGTA ATGCTGGCAC GGGTCTTGAC 780 GGTTCGTCGC TGGGCsGCAA AGGGCTGCAA AACCTGAGCG GGCCGGTGGA CTACCAGCAG 840 TTAGGTAACG CCGTGGGTAC CGGTATCGGT ATGAAAGCGG GCATTCAGGC GCTGAATGAT 900 ATCGGTACGC ACAGGCACAG TTCAACCCGT TCTTTCGTCA ATAAAGGCGA TCGGGCGATG 960 GCGAAGGAAA TCGGTCAGTT CATGGACCAG TATCCTGAGG TGTTTGGCAA GCCGCAGTAC 1020 CAGAAAGGCC CGGGTCAGGA GGTGAAAACC GATGACAAAT CATGGGCAAA AGCACTGAGC 1080 5 AAGCCAGATG ACGACGGAAT GACACCAGCC AGTATGGAGC AGTTCAACAA AGCCAAGGGC 114 0 ATGATCAAAA GGCCCATGGC GGGTGATACC GGCAACGGCA ACCTGCAGGC ACGCGGTGCC 1200 G3TGGTTCTT CGCTGGGTAT TGATGCCATG ATGGCCGGTG ATGCCATTAA CAATATGGCA 1260 CGTGGCAAGC TGGsCGCGsC TTAAGCTG 1288 Another potentially suitable hypersensitive response promoter from Erwinia amylovora is described in U.S. Patent Application Serial No. 09 / 120,927 which is incorporated by reference herein. The protein is encoded by a DNA molecule that is a nucleic acid sequence of the SEQ. ID. 15 NO. 25 as follows: ATGTCAATTC TTACGCTTAA CAACAATACC TCGTCCTCGC CGGGTCTGTT CCAGTCCGGG 60 GGG3ACAACG GGCTTGGTGG TCATAATGCA AATTCTGCGT TGGGGCAACA ACCCATCGAT 120 CGGCAAACCA TTGAGCAAAT GGCTCAATTA TTGGCGGAAC TGTTAAAGTC ACTGCTATCG 180 CCACAATCAG GTAATGCGGC AACCGGAGCC GGTGGCAATG ACCAGACTAC AGGAGTTGGT 24 0 2 0 AAC CTGGCG GCCTGAACGG ACGAAAAGGC ACAGCAGGAA CCACTCCGCA GTCTGACAGT 300 CAGAACATGC TGAGTGAGAT GGGCAACAAC GGGCTGGATC AGGCCATCAC GCCCGATGGC 360 CAGGGCGGCG GGCAGATCGG CGATAATCCT TTACTGAAAG CCATGCTGAA GCTTATTGCA 420 and CGCATGATGG ACGGCCAAAG CGATCAGTTT GGCCAACCTG GTACGGGCAA CAACAGTGCC 480 TCTTCCGGTA CGTCTTCATC TGGCGGTTCC CCTTTTAACG ATCTATCAGG GGGGAAGGCC 540 CCTGCCGGCA ACTCCCCTTC CsGCAACTAC TCTCCCGTCA GTACCTTCTC ACCCCCATCC 600c ACGCCAACGT CCCCTACCTC ACCGCTTGAT TTCCCTTCTT CTCCCACCAA AGCAGCCGGG 660 O J ~ - * *** - - -a GGCAGCACGC CGGTAACCGA TCATCCTGAC CCTGTTGGTA GCGCGGGCAT CGGGGCCGGA 720 ÍATTCGGTGG CCTTCACCAG CGCCGGCGCT AATCAGACGG TGCTGCATGA CACCATTACC 780 GTGAAAGCGG GTCAGGTGTT TGATGGCAAA GGACAAACCT TCACCGCCGG TTCAGAATTA 840 GGCGATGGCG GCCAGTCTGA AAACCAGAAA CCGCTGTTTA TACTGGAAGA CGGTGCCAGC 900 CTGAAAAACG TCACCATGGG CGACGACGGG GCGGATGGTA TTCATCTTTA CGGTGATGCC 960 ÍAAATAGACA ATCTGCACGT CACCAACGTG GGTGAGGACG CGATTACCGT TAAGCCAAAC 1020 AGCGCGGGCA AAAAATCCCA CGTTGAAATC ACTAACAGTT CCTTCGAGCA CGCCTCTGAC 1080 AAGATCCTGC AGCTGAATGC CGATACTAAC CTGAGCGTTG ACAACGTGAA GGCCAAAGAC 1140 TTGGGTACTT TTGTACGCAC TAACGGCGGT CAACAGGGTA ACTGGGATCT GAATCTGAGC 1200 C TATCAGCG CAGAAGACGG TAAGTTCTCG TTCGTTAAAA GCGATAGCGA GGGGCTAAAC 1260 10 G: CAATACCA GTGATATCTC ACTGGGTGAT GTTGAAAACC ACTACAAAGT GCCGATGTCC 1320 GCCAACCTGA AGGTGGCTGA ATGA 1344 See GenBank Access No. U94513. The isolated DNA molecule of the present invention encodes a 15 protein or hypersensitive response promoter polypeptide having an amino acid sequence of SEQ. ID. No. 26 as follows: Met Ser He Leu Thu Leu Asn Asn Asn Thr Ser Ser Being Pro Gly Leu 1 5 10 15 20 Phe Gln Ser Gly Gly Asp Asn Gly Leu Gly Gly His Asn Wing Asn Being 20 25 30 Wing Leu Gly Gln Gln Pro He Asp Arg Gln Thr He Glu Gln Met Wing 35 40 45 G n Leu Leu Wing Glu Leu Leu Lys Ser Leu Leu Ser Pro Gln Ser Gly 50 55 60 Asn Wing Wing Thr Gly Wing Gly Gly Asn Asp Gln Thr Thr Gly Val Gly 65 7 ° 75 80 25 «*" ¡^ * ^^ - i- * • - * - Asn Wing Gly Gly Leu Asn Gly Arg Lys Gly Thr Wing Gly Thr Thr Pro 85 90 95 Gln Ser Asp Ser Gln Asn Met Leu Ser Glu Met Gly Asn Asn Gly Leu 100 105 110 Asp Gln Wing He Thr Pro Asp Gly Gln Gly Gly Gly Gln Gly Asp 115 120 125 Asn Pro Leu Leu Lys Wing Met Leu Lys Leu He Wing Arg Met Met Asp 130 135 140 Gly Gln Ser Aep Gln Phe Gly Gln Pro Gly Thr Gly Asn Asn Ser Wing 145 150 155 160 Ser Ser Gly Thr Ser Ser Ser Gly Gly Ser Pro Phe Asn Asp Leu Ser 165 170 175 Gly Gly Lys Wing Pro Gly Asn Ser Pro Gly Asn Tyr Ser Pro 180 185 190 Val Ser Thr Phe Ser Pro Pro Ser Thr Pro Thr Ser Pro Thr Ser Pro 195 200 205 Leu Asp Phe Pro Ser Ser Thr Pro Lys Wing Ala Gly Gly Ser Thr Pro 210 215 220 Val Thr Asp His Pro Asp Pro Val Gly Ser Ala Gly He Gly Ala Gly 225 230 235 240 Asn Ser Val Ala Phe Thr Ser Ala Gly Ala Asn Gln Thr Val Leu His 245 250 255 Asp Thr He Thr Val Lys Wing Gly Gln Val Phe Asp Gly Lys Gly Gln 260 265 270 Thr Phe Thr Wing Gly Ser Glu Leu Gly Asp Gly Gly Gln Ser Glu Asn 275 280 285 - Gln Lys Pro Leu Phe He Leu Glu Asp Gly Wing Ser Leu Lys Asn Val 290 295 300 Thr Met Gly Asp Asp Gly Wing Asp Gly He His Leu Tyr Gly Asp Wing 305 310 315 320 Lys He Asp Asn Leu His Val Thr Asn Val Gly Glu Asp Ala He Thr 325 330 335 Val Lys Pro Asn Ser Wing Gly Lys Lys Ser His Val Glu He Thr Asn 340 345 350 * * • * fl Being Ser Phe Glu His Wing Being Asp Lys He Leu Gln Leu Asn Wing Asp 355 360 365 Thr Asn Leu Ser Val Asp Aen Val Lys Wing Lys Asp Phe Gly Thr Phe 370 375 380 Val Arg Thr Asn Gly Gly Gln Gln Gly Asn Trp Asp Leu Asn Leu Ser 385 390 395 400 H: .s He Ser Wing Glu Asp Gly Lys Phe Ser Phe Val Lys Ser Asp Ser 405 410 415 G ^ .u Gly Leu Asn Val Asn Thr Ser Asp He Ser Leu Gly Asp Val Glu 420 425 430 Asn His Tyr Lys Val Pro Met Ser Ala Asn Leu Lys Val Ala Glu 435 440 445 This protein or polypeptide is acid, rich in glycine and serine, and lacks cysteine. It is also stable to heat, sensitive to protease, and suppressed by inhibitors of plant metabolism. The protein or polypeptide of the present invention has a predicted molecular weight of about 4. 5 kDa. Another hypersensitive response promoter, potentially suitable for Erwinia amylovora, is described in United States Patent Application No. of Series 09/120, 663 which is incorporated by reference herein. The protein is encoded by a DNA molecule having a nucleic acid sequence of the SEQ.

ID. Do not . 27 as follows: _ -_.

ATGGAATTAA AATCACTGGG AACTGAACAC AAGGCGGCAG TACACACAGC GGCGCACAAC 60 CCGGTGGGGC ATGGTGTTGC C TACAGCAG GGCAGCAGCA GCAGCAGCCC GCAAAATGCC 120 GCRGCATCAT TGGCGGCAGA AGGCAAAAAT CGTGGGAAAA TGCCGAGAAT TCACCAGCCA 180 TCGACTGCGG CTGATGGTAT CAGCGCTOCT CACCAGCAAA AGAAATCCTT CAGTCTCAGG 240 GGCTGTTTGG GGACGAAAAA ATTTTCCAGA TCGGCACCGC AGGGCCAGCC AGGTACCACC 300 CACAGCAAAG GGGCAACATT GCGCGATCTG CTGGCGCGGG ACGACGGCGA AACGCAGCAT 360 GAC5GCGGCCG CGCCAGATGC GGCGCGTTTG ACCCGTTCGG GCGGCGTCAA ACGCCGCAAT 420 ATGGACGACA TGGCCGGGCG GCCAATGGTG AAAGGTGGCA GCGGCGAAGA TAAGGTACCA 480 ACGCAGCAAA AACGGCATCA GCTGAACAAT TTTGGCCAGA TGCGCCAAAC GATGTTGAGC 540 AA? ATGGCTC ACCCGGCTTC AGCCAACGCC GGCGATCGCC TGCAGCATTC ACCGCCGCAC 600 ATC'CCGGGTA GCCACCACGA AATCAAGGAA GAACCGGTTG GCTCCACCAG CAAGGCAACA 660 ACGGCCCACG CAGACAGAGT GGAAATCGCT CAGGAAGATG ACGACAGCGA ATTCCAGCAA 720 CTGCATCAAC AGCGGCTGGC GCGCGAACGG GAAAATCCAC CGCAGCCGCC CAAACTCGGC 780 GTTGCCACAC CGATTAGCGC CAGGTTTCAG CCCAAACTGA CTGCGGTTGC GGAAAGCGTC 840 CTTGAGGGGA CAGATACCAC GCAGTCACCC CTTAAGCCGC AATCAATGCT GAAAGGAAGT 900 GGA3CCGGGG TAACGCCGCT GGCGGTAACG CTGGATAAAG GCAAGTTGCA GCTGGCACCG 960 GAT ^ ATCCAC CCGCGCTCAA TACGTTGTTG AAGCAGACAT TGGGTAAAGA CACCCAGCAC 1020 TATCTGGCGC ACCATGCCAG CAGCGACGGT AGCCAGCATC TGCTGCTGGA CAACAAAGGC 1080 CACCTGTTTG ATATCAAAAG CACCGCCACC AGCTATAGCG TGCTGCACAA CAGCCACCCC 1140 GGTGAGATAA AGGGCAAGCT GGCGCAGGCG GGTACTGGCT CCGTCAGCGT AGACGGTAAA 1200 AGCGGCAAGA TCTCGCTGGG GAGCGGTACG CAAAGTCACA ACAAAACAAT GCTAAGCCAA 1260 CCGC? GGGAAG CGCACCGTTC CTTATTAACC GGCATTTGGC AGCATCCTGC TGGCGCAGCG 1320 CGGOCGCAGG GCGAGTCAAT CCGCCTGCAT GACGACAAAA TTCATATCCT GCATCCGGAG 1380 CTGCIGCGTAT GGCAATCTGC GGATAAAGAT ACCCACAGCC AGCTGTCTCG CCAGGCAGAC 1440 GGTÍAGCTCT ATGCGCTGAA AGACAACCGT ACCCTGCAAA ACCTCTCCGA TAATAAATCC 1500 TCAGAAAAGC TGGTCGATAA AATCAAATCG TATTCCGTTG ATCAGCGGGG GCAGGTGGCG 1560 ATCCTGACGG ATACTCCCGG CCGCCATAAG ATGAGTATTA TGCCCTCGCT GGATGCTTCC 1620 CCGGAGAGCC ATATTTCCCT CAGCCTGCAT TTTGCCGATG CCCACCAGGG GTTATTGCAC 1680 GGGAAGTCGG AGCTTGAGGC ACAATCTGTC GCGATCAGCC ATGGGCGACT GGTTGTGGCC 1740 GATAGCGAAG GCAAGCTGTT TAGCGCCGCC ATTCCGAAGC AAGGGGATGG AAACGAACTG 1800 AAAAGGAAAG CCATGCCTCA GCATGCGCTC GATGAACATT TTGGTCATGA CCACCAGATT 1860 TCTGGATTTT TCCATGACGA CCACGGCCAG CTTAATGCGC TGGTGAAAAA TAACTTCAGG 1920 CAGCAGCATG CCTGCCCGTT GGGTAACGAT CATCAGTTTC ACCCCGGCTG GAACCTGACT 1980 GATGCGCTGG TTATCGACAA TCAGCTGGGG CTGCATCATA CCAATCCTGA ACCGCATGAG 2040 ATTCTTGATA TGGGGCATTT AGGCAGCCTG GCGTTACAGG AGGGCAAGCT TCACTATTTT 2100 GACCAGCTGA CCAAAGGGTG GACTGGCGCG GAGTCAGATT GTAAGCAGCT GAAAAAAGGC 2160 CTGGATGGAG CAGCTTATCT ACTGAAAGAC GGTGAAGTGA AACGCCTGAA TATTAATCAG 2220 AGCACCTCCT CTATCAAGCA CGGAACGGAA AACGTTTTTT CGCTGCCGCA TGTGCGCAAT 2280. ^ AACCGGAGC CGGGAGATGC CCTGCAAGGG CTGAATAAAG ACGATAAGGC CCAGGCCATG 2340 GCGGTGATTG GGGTAAATAA ATACCTGGCG CTGACGGAAA AAGGGGACAT TCGCTCCTTC 2400 i-? GATAAAAC CCGGCACCCA GCAGTTGGAG CGGCCGGCAC AAACTCTCAG CCGCGAAGGT 2460 ATCAGCGGCG AACTGAAAGA CATTCATGTC GACCACAAGC AGAACCTGTA TGCCTTGACC 2520 iZACGAGGGAG AGGTGTTTCA TCAGCCGCGT GAAGCCTGGC AGAATGGTGC CGAAAGCAÜC 2580 AGCTGGCACA AACTGGCGTT GCCACAGAGT GAAAGTAAGC TAAAAAGTCT GGACATGAGC 2640 CATGAGCACA AACCGATTGC CACCTTTGAA GACGGTAGCC AGCATCAGCT GAAGGCTGGC 2700 GGCTGGCACG CCTATGCGGC ACCTGAACGC GGGC CGCTGG CGGTGGGTAC CAGCGGTTCA 2760 CAAACCGTCT TTAACCGACT AATGCAGGGG GTGAAAGGCA AGGTGATCCC AGGCAGCGGG 2820 TTGACGGTTA AGCTCTCGGC TCAGACGGGG GGAATGACCG GCGCCGAAGG GCGCAAGGTC 2880 AGCAGTAAAT TTTCCGAAAG GATCCGCGCC TATGCGTTCA ACCCAACAAT GTCCACGCCG 2940 CGACCGATTA AAAATGCTGC TTATGCCACA CAGCACGGCT GGCAGGGGCG TGAGGGGTTG 3000 .AAGCCGTTGT ACGAGATGCA GGGAGCGCTG ATTAAACAAC TGGATGCGCA TAACGTTCGT 3060 CATAACGCGC CACAGCCAGA TTTGCAGAGC AAACTGGAAA CTCTGGATTT AGGCGAACAT 3120 3GCGCAGAAT TGCTTAACGA CATGAAGCGC TTCCGCGACG AACTGGAGCA GAGTGCAACC 3180 CGTTCGGTGA CCGTTTTAGG TCAACATCAG GGAGTGCTAA AAAGCAACGG TGAAATCAAT 3240 AGCGAATTTA AGCCATCGCC CGGCAAGGCG TTGGTCCAGA GCTTTAACGT CAATCGCTCT 3300 3GTCAGGATC TAAGCAAGTC ACTGCAACAG GCAGTACATG CCACGCCGCC ATCCGCAGAG 3360 AGTAAACTGC AATCCATGCT GGGGCACTTT GTCAGTGCCG GGGTGGATAT GAGTCATCAG 3420 AAGGGCGAGA TCCCGCTGGG CCGCCAGCGC GATCCGAATG ATAAAACCGC ACTGACCAAA 3480 TCGCGTTTAA TTTTAGATAC CGTGACCATC GGTGAACTGC ATGAACTGGC CGATAAGGCG 3540 AAACTGGTAT CTGACCATAA ACCCGATGC C GATCAGATAA AACAGCTGCG CCAGCAGTTC 3600 GATACGCTGC OTGAAAAGCG GTATGAGAGC AATCCGGTGA AGCATTACAC CGATATGGGC 3660 TTCACCCATA ATAAGGCGCT GGAAGCAAAC TATGATGCGG TCAAAGCCTT TATCAATGCC 3720 TTTAAGAAAG AGCACCACGG CGTCAATCTG ACCACGCGTA CCGTACTGGA ATCACAGGGC 3780 AGTGCGGAGC TGCCGAAGAA GCTCAAGAAT ACGCTGTTGT CCCTGGACAG TGGTGAAAGT 3840 ATGAGCTTCA GCCGGTCATA TGGCGGGGGC GTCAGCACTG TCTTTGTGCC TACCCTTAGC 3900 L., ... -.-- », -..-- - -. . *. . ^ - ^ - a- AJIGAAGGTGC CAGTTCCGGT GATCCCCGGA GCCGGCATCA CGCTGGATCG CGCCTATAAC 3960 C GAGCTTCA GTCGTACCAG CGGCGGATTG AACGTCAGTT TTGGCCGCGA CGGCGGGGTG 4020 AOTGGTAACA TCATGGTCGC TACCGGCCAT GATGTGATGC CCTATATGAC CGGTAAGAAA 4080 ACCAGTGCAG GTAACGCCAG TGACTGGTTG AGCGCAAAAC ATAAAATCAG CCCGGACTTG 4140 CCITATCGGCG CTGCTGTGAG TGGCACCCTG CAAGGAACGC TACAAAACAG CCTGAAGTTT 4200 10 AAGCTGACAG AGGATGAGCT GCCTGsCTTT ATCCATGGCT TGACGCATGG CACGTTGACC 4260 COGGCAGAAC TGTTGCAAAA GGGGATCGAA CATCAGATGA AGCAGGGCAG CAAACTGACG 4320 15 TTTAGCGTCG ATACCTCGGC AAATCTGGAT CTGCGTsCCs GTATCAATCT GAACGAAGAC 4380 GG CAGTAAAC CAAATGGTOT CACTGCCCGT GTTTCTGCCG GGCTAAGTGC ATCGGCAAAC 4440 CTGGCCGCCG GCTCGCGTGA ACGCAGCACC ACCTCTGGCC AGTTTGGCAG CACGACTTCG 4500 20 GCCAGCAATA ACCGCCCAAC CTTCCTCAAC GGGGTCGGCG CGGGTGCTAA CCTGACGGCT 4560 GCTTTAGGGG TTGCCCATTC ATCTACGCAT GAAGGGAAAC CGGTCGGGAT CTTCCCGGCA 4620 25 TTTACCTCGA CCAATGTTTC GGCAGCGCTG GCGCTGGATA ACCGTACCTC ACAGAGTATC 4680 AGCCTGGAAT TGAAGCGCGC GGAGCCGGTG ACC AGCAACG ATATCAGCGA GTTGACCTCC 4740 ACGCTGGGAA AACACTTTAA GGATAGCGCC ACAACGAAGA TGCTTGCCGC TCTCAAAGAG 4800 30 TTAGATGACG CTAAGCCCGC TGAACAACTG CATATTTTAC AGCAGCATTT CAGTGCAAAA 4860 GATGTCGTCG GTGATGAACG CTACGAGGCG GTGCGCAACC TGAAAAAACT GGTGATACGT 4920 35 CAACAGGCTG CGGACAGCCA CAGCATGGAA TTAGGATCTG CCAGTCACAG CACGACCTAC 4980 AATAATCTGT CGAGAATAAA TAATGACsGC ATTGTCGAGC TGCTACACAA ACATTTCGAT 5040 GC3GCATTAC CAGCAAGCAG TGCCAAACGT CTTGGTGAAA TGATGAATAA CGATCCGGCA 5100 40 CT3AAAGATA TTATTAAGCA GCTGCAAAGT ACGCCGTTCA GCAGCGCCAG CGTGTCGATG 5160 ^ GAGCTGAAAG ATGGTCTGCG TGAGCAGACG GAAAAAGCAA TACTGGACGG TAAGGTCGGT 5220 45 CGTGAAGAAG TGGGAGTACT TTTCCAGGAT CGTAACAACT TGCGTGTTAA ATCGGTCAGC 5280 GT AGTCAGT CCGTCAsCAA AAGCGAAGGC TTCAATACCC CAGCGCTGTT ACTGGGGACG 5340 AGi? AACAGCG CTGCTATGAG CATGGAGCGC AACATCGGAA CCATTAATTT TAAATACGGC 5400 50 CA GATCAGA ACACCCCACG GCGATTTACC CTGGAGGGTG GAATAGCTCA GGCTAATCCG 5460 CAGGTCGCAT CTGCGCTTAC TGATTTGAAG AAGGAAGGGC TGGAAATGAA GAGCTAA 5517 ^^^^^^ 5 '- "^" ^ M ^ This DNA molecule is known as the dspE gene for Erwinia amylovora, this isolated DNA molecule of the present invention encoded for a protein or polypeptide that promotes a hypersensitive response. to the plant pathogen, having an amino acid sequence of SEQ ID No. 28 as follows: Met Glu Leu Lys Ser Leu Gly Thr Glu His Lys Ala Ala Val His Thr 1 5 10 15 Ala Ala His Asn Pro Val Gly HIS Gly Val Ala Leu Gln Gln Gly Ser 20 25 30 10 Ser Ser Ser Pro Gln Asn Ala Ala Ala Be Leu Wing Wing Glu Gly 35 40 45 Lys Asn Arg Gly Lys Met Pro Arg He His Gln Pro Ser Thr Wing Wing 50 55 60 Asp Gly He Wing Ala Wing Gln Gln Lys Lys Ser Phe Ser Leu Arg 65 70 75 80 Gly Cys Leu Gly Thr Lys Lys Phe Ser Arg Ser Wing Pro Gln Gly Gln 85 90 95 15 Pro Gly Thr Thr His Ser Lys Gly Wing Thr Leu Arg Asp Leu Leu Wing 100 105 110 Arg Asp Asp Gly Glu Thr Gln His Glu Wing Wing Ala Pro Asp Ala Ala 115 120 125 Arg Leu Thr Arg Ser Gly Gly Val Lys Arg Arg Asn Met Asp Asp Met 130 135 140 Wing Gly Arg Pro Met Val Lys Gly Gly Ser Gly Glu Asp Lys Val Pro 145 150 155 160 Thr Gln Gln Lys Arg His Gln Leu Asn Asn Phe Gly Gln Met Arg Gln 20 165 170 175 Thr Met Leu Ser Lys Met Wing His Pro Wing Wing Wing Asn Wing Gly Asp 180 185 190 Arg Leu Gln His Ser Pro Pro HIS He Pro Gly Ser His His Glu He 19 5 200 205 Lys Glu Glu Pro Val Gly Ser Thr Ser Lys Wing Thr Thr Wing His Wing 210 215 220 Asp Arg Val Glu He Wing Gln Glu Asp Asp Asp Ser Glu Phe Gln Gln 25 2 S 230 235 240 ' Leu Hxs Gln Gln Arg Leu Wing Arg Glu Arg Glu Asn Pro Pro Gln Pro 245 250 255 Pro Lys Leu Gly Val Wing Thr Pro He Wing Wing Arg Phe Gln Pro Lys 260 265 270 Leu Thr Ala Val Ala Glu Ser Val Leu Glu Gly Thr Asp Thr Thr Gln 275 280 285 Ser Pro Leu Lys Pro Gln Ser Met Leu Lys Gly Ser Gly Wing Gly Val 290 295 300 Thr Pro Leu Wing Val Thr Leu Asp Lys Gly Lys Leu Gln Leu Wing Pro 305 310 315 320 Asp Asn Pro Pro Ala Leu Asn Thr Leu Leu Lys Gln Thr Leu Gly Lys 325 330 335 Asp Thr Gln His Tyr Leu Wing His His Wing Being Ser Asp Gly Ser Gln 34C 345 350 His Leu Leu Asu Asn Lys Gly Hxs Leu Phe Asp He Lys Ser Thr 355 360 365 Wing Thr Ser Tyr Ser Val Leu His Asn Ser Hxs Pro Gly Glu Lie Lys 370 375 380 Gly Lys Leu Wing Gln Wing Gly Thr Gly Ser Val Ser Val Asp Gly Lys 385 390 395 400 Ser Gly Lys Be Ser Leu Gly Ser Gly Thr Gln Ser His Asn Lys Thr 405 410 415 Met Leu Ser Gln Pro Gly Glu Wing His Arg Ser Leu Leu Thr Gly He 420 425 430 Trp Gln Hxs Pro Wing Gly Wing Wing Arg Pro Gln Gly Glu Ser He Arg 435 440 445 Leu His Asp Asp Lys He His He Leu His Pro Glu Leu Gly Val Trp 450 455 460 Gln Ser Wing Asp Lys Asp Thr Hie Ser Gln Leu Ser Arg Gln Wing Asp 465 470 475 480 Gly Lys Leu Tyr Wing Leu Lys Asp Asn Arg Thr Leu Gln Asn Leu Ser 485 490 495 Asp Asn Lys Ser Ser Glu Lys Leu Val Asp Lys He Lys Ser Tyr Ser 500 505 510 Val Asp Gln Arg Gly Gln Val Wing He Leu Tnr Asp Thr Pro Gly Arg 515 520 525 Hxs Lys Met Ser Met Met Pro Ser Leu Asp Ala Ser Pro Glu Ser Hxs 53 0 535 540 He Ser Leu Ser Leu His Phe Wing Asp Wing Hxs Gln Gly Leu Leu Hxs 545 550 555 560 ..- fc--. »^ Gly Lys Ser Glu Leu Glu Wing Gln Ser Val Wing He Ser His Gly Arg 565 570 575 Leu Val Val Wing Asp Ser Glu Gly Lys Leu Phe Ser Wing Wing Pro 580 585 590 Lys Gln Gly Asp Gly Asn Glu Leu Lys Met Lys Wing Met Pro Gln His 595 600 605 Wing Leu Asp Glu His Phe Gly His Asp His Gln He Ser Gly Phe Phe 610 615 620 His Asp Asp His Gly Gln Leu Asn Ala Leu Val Lys Asn Asn Phe Arg 625 630 635 640 Gln Gln His Wing Cys Pro Leu Gly Asn Asp His Gln Phe His Pro Gly 645 650 655 Trp Asn Leu Thr Asp Ala Leu Val He Asp Asn Gln Leu Gly Leu His 660 665 670 His Thr Asn Pro Glu Pro His Glu He Leu Asp Mee Gly His Leu Gly 675 680 685 Ser Leu Ala Leu Gln Glu Gly Lys Leu His Tyr Phe Asp Gln Leu Thr 690 695 700 Lye Gly Trp Thr Gly Wing Glu Ser Aep Cys Lys Gln Leu Lye Gly 705 710 715 720 Leu Asp Gly Wing Ala Tyr Leu Leu Lys Asp Gly Glu Val Lys Arg Leu 725 730 735 Asn He Asn Gln Ser Thr Ser Ser He Lys His Gly Thr Glu Asn Val 740 745 750 Phe Ser Leu Pro His Val Arg Asn Lys Pro Glu Pro Gly Asp Al to Leu, 755 760 765 Gln Gly Leu Asn Lys Asp Asp Lys Wing Gln Wing Met Wing Val He Gly 770 775 780 Val Asn Lys Tyr Leu Wing Leu Thr Glu Lye Gly Asp He Arg Ser Phe 785 790 795 800 Gln He Lys Pro Gly Thr Gln Gln Leu slu Arg Pro Wing Gln Thr Leu 805 810 815 Ser Arg Glu Gly He Ser Gly Glu Leu Lys Asp He His Val Asp His 820 825 830 Lys Gln Asn Leu Tyr Ala Leu Thr His Glu Gly Glu Val Phe Hxs Gln 835 840 845 Pro Arg Glu Wing Trp Gln Asn Gly Wing Glu Ser Ser Ser Trp His Lys 850 855 860 ^^ lüj ^ i ^ - ^ A¿d ------- i - Leu Ala Leu Pro Gln Ser Glu Ser Lys Leu Lys Ser Leu Asp Met Ser 865 870 875 880 His Glu Hxs Lys Pro He Wing Thr Phe Glu Asp Gly Ser Gln His Gln 885 890 895 Leu Lys Wing Gly Gly Trp Hxs Wing Tyr Wing Wing Pro Glu Arg Gly Pro 900 905 910 Leu Wing Val Gly Thr Ser Gly Ser Gln Thr Val Phe Asn Arg Leu Met 915 920 925 Gln Gly Val Lys Gly Lys Val He Pro Gly Ser Gly Leu Thr Val Lys 930 935 940 Leu Ser Wing Gln Thr Gly Gly Met Thr Gly Wing Glu Gly Arg Lys Val 945 950 955 960 Ser Ser Lys Phe Ser Glu Arg He Arg Wing Tyr Wing Phe Asn Pro Thr 965 970 975 Met Ser Thr Pro Arg Pro He Lys Asn Wing Wing Tyr Wing Thr Gln Hxe 980 985 990 Gly Trp Gln Gly Arg Glu Gly Leu Lys Pro Leu Tyr Glu Met Gln Gly 995 1000 1005 Wing Leu He Lys Gln Leu Asp Wing Hxs Asn Val Arg His Asn Wing Pro 1010 1015 1020 Gln Pro Asp Leu Gln Ser Lys Leu Glu Thr Leu Asp Leu Gly Glu His 1025 1030 1035 1040 Gly Ala Glu Leu Leu Asn Asp Met Lys Arg Phe Arg Asp Glu Leu Glu 1045 1050 1055 Gln Ser Ala Thr Arg S er Val Thr Val Leu Gly Gln His Gln Gly Val 1060 1065 1070 Leu Lys Ser Asn Gly Glu He Asn Ser Glu Phe Lys Pro Ser Gly 1075 1080 1085 Lys Ala Leu Val Gln Ser Phe Asn Val Asn Arg Ser Gly Gln Asp Leu 1090 1095 1100 Ser Lys Ser Leu Gln Gln Ala Val His Wing Thr Pro Pro Ser Wing Glu 1105 1110 1115 1120 Ser Lys Leu Glp Ser Met Leu Gly Hxs Phe Val Ser Wing Gly Val Asp 1125 1130 1135 Met Ser HIS Gln Lys Gly Glu He Pro Leu Gly Arg Gln Arg Asp Pro 1140 1145 1150 Asn Asp Lys Thr Wing Leu Thr Lys Ser Arg Leu He Leu Asp Thr Val 1155 1160 1165 Thr He Gly Glu Leu Hxs Glu Leu Wing Asp Lys Wing Lys Leu Val Ser 1170 1175 1180 Müü-aii Asp His Lys Pro Asp Wing Asp Gln He Lys Gln Leu Arg Gln Gln Phe 1185 1190 1195 1200 Asp Thr Leu Arg Glu Lys Arg Tyr Glu Ser Asn Pro Val Lys His Tyr 1205 1210 1215 Thr Asp Met Gly Phe Thr His Asn Lys Wing Leu Glu Wing Asn Tyr Asp 1220 1225 1230 Wing Val Lye Wing Phe He Asn Wing Phe Lys Lys Glu His His Gly Val 1235 1240 1245 Asn Leu Thr Thr Arg Thr Val Leu Glu Ser Gln Gly Ser Wing Glu Leu 1250 1255 1260 Wing Lys Lys Leu Lys Asn Thr Leu Leu Ser Leu Asp Ser Gly Glu Ser 1255 1270 1275 1280 Me: Being Phe Being Arg Being Tyr Gly Gly Gly Val Being Thr Val Phe Val 1285 1290 1295 Pro Thr Leu Ser Lys Val Val Pro Val He Pro Gly Wing Gly 1300 1305 1310 He Thr Leu Asp Arg Ala Tyr Asn Leu Ser Phe Be Arg Thr Ser Gly 1315 1320 1325 Gly Leu Asn Val Ser Phe Gly Arg Asp Gly Gly Val Ser Gly Asn He 1330 1335 1340 Mel: Val Ala Thr Gly His Asp Val Met Pro Tyr Met Thr Gly Lys Lys 1345 1350 1355 1360Ma.

Th :; Being Wing Gly Asn Wing Being Asp Trp Leu Being Wing Lys His Lys He 1365 1370 1375 Ser Pro Asp Leu Arg He Gly Wing Wing Val Ser Gly Thr Leu Gln Gly 1380 1385 1390 Th: r Leu Gln Asn Ser Leu Lys Phe Lys Leu Thr Glu Asp Glu Leu Pro 1395 1400 1405 Gly Phe He His Gly Leu Thr His Gly Thr Leu Thr Pro Wing Glu Leu 1410 1415 1420 Leu Gln Lys Gly He Glu His Gln Met Lys Gln Gly Ser Lys Leu Thr 1425 1430 1435 1440 Ph Ser Val Asp Thr Ser Wing Asn Leu Asp Leu Arg Wing Gly He Asn 1445 1450 1455 Leu Asn Glu Asp Gly Ser Lys Pro Asn Gly Val Thr Ala Arg Val Ser 1460 1465 1470 Ale, Gly Leu Ser Ala Be Ala Asn Leu Ala Ala Gly Ser Arg Glu Arg 1475 1480 1485 Ser Thr Thr Ser Gly Gln Phe Gly Ser Thr Thr Ser Wing Ser Asn Asn 1490 1495 1500 i &amámSm. . i s. ,, i «. < ., ..

Arg Pro Thr Phe Leu Asn Gly Val Gly Wing Gly Wing Asn Leu Thr Wing 1505 1510 1515 1520 Wing Leu Gly Val Wing Hie Being Ser Thr His Glu Gly Lys Pro Val Gly 1525 1530 1535 He Phe Pro Wing Phe Thr Ser Thr Asn Val Ser Wing Wing Leu Wing 1540 1545 1550 ... Asp Asn Arg Thr Ser Gln Ser Be Leu Glu Leu Lys Arg Wing Glu 1555 1560 1565 Pro Val Thr Ser As Asp He Ser Glu Leu Thr Ser Thr Leu Gly Lys 1570 1575 1580 His Phe Lys Asp Be Ala Thr Thr Lye Met Leu Ala Ala Leu Lys Glu 1585 1590 1595 1600 Leu Asp Asp Ala Lys Pro Ala Glu Gln Leu His He Leu Gln Gln His 1605 1610 1615 Phe Ser Ala Lys Asp Val Val Gly Asp Glu Arg Tyr Glu Ala Val Arg 1620 1625 1630 Asn Leu Lys Lys Leu Val He Arg Gln Gln Wing Wing Asp Ser His Ser 163S 1640 1645 Met Glu Leu Gly Ser Ala Ser His Ser Thr Thr Tyr Asn Asn Leu Ser 1650 1655 1660 Arg He Asn Asn Asp Gly He Val Glu Leu Leu His Lys His Phe Asp 1665 1670 1675 1680 Ala Ala Leu Pro Ala Ser Be Ala Lys Arg Leu Gly Met Glu Met Met 1685 1690 1695 Asn Asp Pro Ala Leu Lys Asp He He Lys Gln Leu Gln Ser Thr Pro 1700 1705 1710 Phe Ser Wing Being Val Ser Met Glu Leu Lys Asp Gly Leu Arg Glu 1715 1720 1725 Gln Thr Glu Lye Wing He Leu Asp Gly Lys Val Gly Arg slu Glu Val 1730 1735 1740 Gly Val Leu Phe Gln Asp Arg Asn Asn Leu Arg Val Lys Ser Val Ser 1745 1750 1755 1760 Val Ser Gln Ser Val Ser Lys Ser Glu Gly Phe Asn Thr Pro Ala Leu 1765 1770 1775 Leu Leu Gly Thr Ser Asn Ser Ala Ala Met Ser Met Glu Arg Asn He 1780 1785 1790 Gly Thr He Asn Phe Lys Tyr Gly Gln Asp Gln Asn Thr Pro Arg Arg 1795 1800 1805 Phe Thr Leu Glu Gly Gly He Wing Gln Wing Asn Pro Gln Val Wing Ser .1810 1815 1820 Wing Leu Thr Asp Leu Lys Lys Glu Gly Leu Glu Met Lys Ser 1825 1830 1835 - ^^^^ This protein or polypeptide is approximately 198 kDa and has a pl of 8.98. The present invention relates to an isolated DNA molecule having a nucleotide sequence of SEQ. ID. No. 29 as follows: ATGACATCGT CACAGCAscs GGTTGA? AGG TTTTTACAGT ATTTCTCCGC CGGGTGTAAA 60 ACGCCCATAC ATCTGAAAGA CGGGGTGTGC GCCCTGTATA ACGAACAAGA TGAGGAGGCG 120 GCGGTGCTGG AAGTACCGCA ACACAGCGAC AGCCTGTTAC TACACTGCCG AATCATTGAG 180 GCTGACCCAC AAACTTCAAT AACCCTGTAT TCGATGCTAT TACAGCTGAA TTTTGAAATG 240 GCGGCCATGC GCGGCTGTTG GCTGGCGCTG GATGAACTGC ACAACGTGCG TTTATGTTTT 300 CAGCAGTCGC TGGAGCATCT GGATGAAGCA AGTTTTAGCG ATATCGTTAG CGGCTTCATC 360 3AACATGCGG CAGAAGTGCG TGAGTATATA GCGCAATTAG ACGAGAGTAG CGCGGCATAA 420 This is known as the dspF gene. This isolated molecule of the present invention codes for a protein or polypeptide promoter of the hypersensitive response, having an amino acid sequence of SEQ. ID. No. 30 as follows: Met Thr Ser Ser Gln Gln Arg Val Glu Arg Phe Leu Gln Tyr Phe Ser 1 5 10 15 Wing Gly Cys Lys Thr Pro V. and His Leu Lys Asp Gly Val Cys Ala Leu 20 25 30 Tyr Asn Glu Gln Asp Glu Glu Wing Ala Val Leu Glu Val Pro Gln Hxs 35 40 45 Ser Asp Ser Leu Leu Leu Hxs Cys Arg He He Glu Wing Asp Pro Gln 50 55 60 . . . . ... I. ....,. . , Thr Ser He Thr Leu Tyr Ser Met Leu Leu Gln Leu Asn Phe Glu Met 65 70 75 80 Ala Ala Met Arg Gly Cys Trp Leu Ala Leu Asp Glu Leu Hxs Asn Val 85 90 95 Arg Leu Cys Phe Gln Gln Ser Leu Glu His Leu Asp Glu Wing Being Phe 100 105 110 Being Asp He Val Being Gly Phe He Glu His Wing Wing Glu Val Arg Glu 115 120 125 Tyr He Wing Gln Leu Asp Glu Being Wing Wing 130 135 This protein or polypeptide is approximately 16 kDa and has a pl of 4.45. The polypeptide or protein promoter of the hypersensitive response derived from Pseudomonas syringae has an amino acid sequence corresponding to SEQ. ID. No. 31 as follows: 15 Met Gln Being Leu Being Leu Asn Being Being Leu Gln Thr Pro Wing Met 1 5 10 15 Wing Leu Val Leu Val Arg Pro Glu Wing Glu Thr Thr Gly Ser Thr Ser 20 25 30 Ser Lys Wing Leu Gln Glu Val Val Val Lys Leu Wing Glu Glu Leu Met 35 40 45 Arg Asn Gly Gln Leu Asp Asp Being Pro Pro Leu Gly Lys Leu Leu Wing 50 55 60 20 Lys Ser Met Wing Wing Asp Gly Lys Wing Gly Gly Gly He Glu Asp Val 65 70 75 80 He Ala Ala Leu Asp Lys Leu He His Glu Lys Leu Gly Asp Asn Phe 85 90 95 Gly Ala Ser Ala Asp Ser Ala Ser Gly Thr Gly Gln Gln Asp Leu Met 100 105 110 Thr Gln Val Leu Asn Gly Leu Ala Lys Ser Met Leu Aep Asp Leu Leu 25 115 120 125 goIfifffff ífiHi íí? , * < ? . . - - ~. - * ~ ~ ~ ~ Thr Lys Gln Asp Gly Gly Thr Ser Phe Ser Glu Asp Asp Met Pro Met 130 135 140 Leu Asn Lys He Wing Gln Phe Met Asp Asp Asn Pro Wing Gln Phe Pro 145 150 155 160 Lys Pro Asp Ser Gly Ser Trp Val Asn Glu Leu Lys Glu Asp Asn Phe 165 170 175 Leu Asp Gly Asp Glu Thr Wing Wing Phe Arg Ser Wing Leu Asp He He 180 185 190 Gly Gln Gln Leu Gly Asn Gln Gln Ser Asp Wing Gly Ser Leu Wing Gly 195 200 205 T.ar Gly Gly Gly Leu Gly Thr Pro Ser Ser Phe Ser Asn Asn Ser Ser 210 215 220 10 Val Met Gly Asp Pro Leu He Asp Ala Asn Thr Gly Pro Gly Asp Ser 225 230 235 240 Gly Asn Thr Arg Gly Glu Wing Gly Gln Leu He Gly Glu Leu He Asp 245 250 255 Arg Gly Leu Gln Ser Val Leu Wing Gly Gly Gly Leu Gly Thr Pro Val 260 265 270 Asm Thr Pro Gln Thr Gly Thr Ser Wing Asn Gly Gly Gln Ser Wing Gln 275 280 285 15 Asp Leu Asp Gln Leu Leu Gly Gly Leu Leu Lys Gly Leu Glu Wing 290 295 300 Thr Leu Lys Asp Wing Gly Gln Thr Gly Thr Asp Val Gln Ser Ser Ala 305 310 315 320 A3a Gln He Ala Thr Leu Leu Val Ser Thr Leu Leu Gln Gly Thr Arg 325 330 335 A = n Gln Ala Ala Wing 20 340 This polypeptide or hypersensitive response promoter protein has a molecular weight of 34-35 kDa. It is rich in glycine (approximately 13.5%) and lacks 25 of cysteine and tyrosine. Additional information regarding t ^ t? aat? lii? iiibaífeii-iWt- *. . . ».. ..- * to the hypersensitive response promoter derived from Pseudomonas s syringa e is found in He, S. Y. H. C Huang and A. Collmer "Pseudomonas s syringa e pv. Syringae Harp? NPSs: a Protein that is Secreted via the Hrp Pathway and Elicits the Hypersensitive Response in Plants ", Cell 73: 1255-1266 (1993), which is incorporated by reference herein. The DNA molecule encoding the hypersensitive response promoter of Pseudomonas s syringa e has a nucleotide sequence corresponding to SEQ. ID. No. 32 as follows: ATGCAGAGTC TCAGTCTTAA CAGCAGCTCG CTGCAAACCC CGGCAATGGC CCTTGTCCTG 60 G1ACGTCCTG AAGCCGAsAC GACTGGCAGT ACGTCGAGCA AGGCGCTTCA CGAAGTTGTC 120 GTGAAsCTGG CCGAGGAACT GATGCGCAAT GGTCAACTCG ACGACAGCTC GCCATTGGGA 180 AÍACTCTTGG CCAAGTCGAT GGCCGCAGAT GGCAAGGCGG GCGGCGGTAT TGAGGATGTC 240 ATCGCTGCGC TGGACAAGCT GATCCAT3AA AAGCTCGGTG ACAACTTCGG CGCGTCTGCG 300 G? CAGCGCCT CGGGTACCGG ACAGCAGGAC CTGATGACTC AGGTGCTCAA TOGCCTGGCC 360 A? GTCGATGC TCGATGATCT TC GACCAAG CAGGATGGCG GGACAAGCTT CTCCGAAGAC 420 GATATGCCGA TGCTGAACAA GATCGCGCAG TTCATGGATG ACAATCCCGC ACAGTTTCCC 480 AGCCGGACT CGssCTCCTG GGTGAACGAA CTCAAGGAAG ACAACTTCCT TGATGGCOAC 540 GJiAACGsCTG CGTTCCGTTC GGCACTCGAC ATCATTGGCC AGCAACTGGG TAATCAGCAG 600 BC? TGACGCTG GCAGTCTGGC AGGGACGGGT GGAGsTCTGG GCACTCCGAG CAGTTTTTCC 660 A CAACTCGT CCGTGATGGG TGATCCGCTG ATCGACGCCA ATACCGGTCC CGGTGACAGC 720 GCrCAATACCC GTGGTGAAGC GGGGCAACTG ATCGGCGAGC TTATCOACCG TGGCCTGCAA 780 TC 'GGTATTGG CCGGTGGTGG ACTGGGCACA CCCGTAAACAENTOAGAC CGGTACGTCG 840 GCG AATGGCG GACAGTCCGC TCACGATCTT GATCAGTTGC TGG3CGGCTT GCTGCTCAAG 900 GGCCTGGAGG CAACGCTCAA GGATGCCGGG CAAACAGGCA CCGACGTGCA GTCGAGCGCT 960 GCsCAAATCG CCACCTTGCT GGTCAGTACG CTGCTGCAAG GCACCCGCAA TCAGGCTGCA 1020 GCCTGA 026 Another hypersensitive, potentially suitable response promoter of Pseudomonas syringae is described in U.S. Patent Application No. 09 / 120,817, which is incorporated by reference herein. The protein has a nucleotide sequence of the SEQ. ID. No. 33 as follows: TCCACTTCGC TGATTTTGAA ATTGGCAGAT TCATAGAAAC GTTCAGGTGT GGAAATCAGG 60 CT3AGTGCGC AGATTTCGTT GATAAGGGTG TGGTACTGGT CATTGTTGGT CATTTCAAGG 120 CCTCTGAGTG CGsTGCGGAG CAATACCAGT CTTCCTGCTG GCGTGTGCAC ACTGAGTCGC 180 AG3CATAGGC ATTTCAGTTC CTTGCGTTGG TTGGGCATAT AAAAAAAssA ACTTTTAAAA 240 ACAGTGCAAT GAGATGCCGG CAAAACGGGA ACCGGTCGCT GCCC-TTOCC ACTCACTTCG 300 AGCAAGCTCA ACCCCAAACA TCCACATCCC TATCGAACGG ACAGCGATAC GGCCACTTGC 360 TCTOsTAAAC CCTGGAGCTG GCGTCGGTCC AATTGCCCAC TTAsCGAOsT AACGCAGCAT 420 GA3CATCGGC ATCACACCCC GGCCGCAACA GACCACCACG CCACTCGATT TTTCGscsCT 480 AA3CGGCAAG AGTCCTCAAC CAAACACGTT CGGCGAGCAG AACACTCAGC AAGCGATCGA 540 CCCGAGTGCA CTGTTGTTCG GCAGCGACAC ACAGAAAGAC GTCAACTTCG GCACGCCCGA 600 CA3CACCGTC CAGAATCCGC AGGACGCCAG CAAGCCCAAC GACAGCCAGT CCAACATCGC 660 TAAATTGATC AGTGCATTGA TCATGTCGTT GCTGCAGATG CTCACCAACT CCAATAAAAA 720 GCAGGACACC AATCAGGAAC AGCCTGATAG CCAGGCTCCT TTCCAGAACA ACGGCGGGCT 780 C3GTACACCG TCGGCCGATA GCGGGGGCGG CGGTACACCG GATGCGACAG GTGGCGGCGG 840 CSGTGATACG CCAAGCGCAA CAGGCGGTGG CGGCGGTGAT ACTCCGACCG CAACAOGCGG 900 T3GCGGCAGC GGTGsCGGCG GCACACCCAC TGCAACAGGT GGCGsCAGCG GTGGCACACC 960 CACTGCAACA GGCGGTsGCG AGGGTGGCGT AACACCGCAA ATCACTCCGC AGTTGGCCAA 1020 CCCTAACCGT ACCTCAGGTA CTGGCTCGGT GTCGGACACC GCAGGTTCTA CCGAGCAAGC 1080 5 C3GCAAGATC AATGTGGTGA AAGACACCAT CAAGGTCGGC GCTGGCGAAG TCTTTGACGG 1140 CCACGGCGCA ACCTTCACTG CCGACAAATC TATGGGTAAC GGAGACCAGG GCGAAAATCA 1200 G.tVAGCCCATG TTCGAGCTGs CTGAAGGCGC TACGTTGAAO AATGTGAACC TGGGTGAOAA 1260 OSAGGTCGAT GGCATCCACG TGAAAGCCAA AAACGCTCAG GAAGTCACCA TTGACAACGT 1320 G: ATGCCCAG AACsTCGsTG AAGACCGGAT TACGGTCAAA GGCGAGGGAG GCGCAGCGGT 1380 C ^ CTAATCTG AACATCAAGA ACAGCAGTGC CAAAGGTGCA GACGACAAGG TTGTCCAGCT 1440 10 Ci \ ACGCCAAC ACTCACTTGA AAATCGACAA CTTCAAGGCC GACGATTTCG GCACGATOGT 1500 TCGCACCAAC GGTGOCAAGC AGTTTGATGA CATGAGCATC GAGCTGAACG GCAT CGAAGC 1560 T. ^ ACCACGGC AAGTTCGCCC TGGTGAAAAG CGACAGTGAC GATCTGAAGC TGGCAACGGG 1620 CftACATCGCC ATGACCGACG TCAAACACGC CTACGATAAA ACCCAGGCAT CGACCCAACA 1680 CACCGAGCTT TGAATCCAGA CAAGTAGCTT GAAAAAAGGG GGTGGACTC 1729 15 This DNA molecule is known as the dspE gene for Pseudomonas syringae. This isolated DNA molecule of the present invention codes for a protein or polypeptide that promotes a hypersensitive response to the plant pathogen which has an amino acid sequence of 20 the SEQ. ID. No. 34 as follows: Met Be He Gly He Thr Pro Arg Pro Gln Gln Thr Thr Thr Pro Leu 5 10 15 Asp Phe Be Wing Leu Ser Gly Lys Ser Pro Gln Pro Asn Thr Phe Gly 20 25 30 Glu Gln Asn Thr Gln Gln Wing He Asp Pro Being Wing Leu Leu Phe Gly 35 40 45 25 Be Asp Thr Gln Lys Asp Val Asn Phe Gly Thr Pro Asp Ser Thr Val 50 55 60 , -? ff-tfiiitt-go "ai" "4i *" '- - Gln Asn Pro Gln Asp Wing Ser Lys Pro Asn Asp Ser Gln Ser Asn He 65 70 75 80 Wing Lys Leu Wing Being Wing Leu He Met Being Leu Leu Gln Met Leu Thr 85 90 95 Asn Being Asn Lys Lys Gln Asp Thr Asn Gln Glu Gln Pro Asp Ser Gln 100 105 110 Wing Pro Phe Gln Asn Asn Gly Gly Leu Gly Thr Pro Be Wing Asp Ser 115 120 125 Gly Gly Gly Gly Gly Thr Pro Asp Wing Thr Gly Gly Gly Gly Asp Thr 130 135 140 Pro Be Wing Thr Gly Gly Gly Gly Gly Asp Thr Pro Thr Wing Thr Gly 145 150 155 160 Gly Gly Gly Gly Gly Gly Gly Gly Thr Pro Thr Gly Gly Gly 165 170 175 Gly Gly Thr Pro Thr Wing Thr Gly Gly Gly Gly Gly Val Thr 180 185 190 ro Gln He Thr Pro Gln Leu Wing Asn Pro Asn Arg Thr Ser Gly Thr 195 200 205 Gly Ser Val Ser Asp Thr Wing Gly Ser Thr Glu Gln Wing Gly Lys He 210 215 220 Asn Val Val Lys Asp Thr He Lys Val Gly Wing Gly Glu Val Phe Asp 225 230 235 240 Gly His Gly Wing Thr Phe Thr Wing Asp Lys Ser Met Gly Asn Gly Asp 245 250 255 Gln Gly Glu Asn Gln Lys Pro Met Phe Glu Leu Wing Glu Gly Wing Thr 260 265 270 Leu Lys Asn Val Asn Leu Gly Glu Asn Glu Val Asp Gly He His Val 275 280 285 Lys Wing Lys Asn Wing Gln Glu Val Thr He Asp Asn Val His Wing Gln 290 295 300? Sn Val Gly Glu Asp Leu He Thr Val Lys Gly Glu Gly Gly Ala Wing 05 310 315 320 Val Thr Asn Leu Asn He Lys Asn Ser Be Wing Lys Gly Wing Asp Asp 325 330 335 Lys Val Val Gln Leu Asn Wing Asn Thr His Leu Lys He Asp Asn Phe 340 345 350 - ** - ** »Lys Wing Asp Asp Phe Gly Thr Met Val Arg Thr Asn Gly Gly Lys Gln, 355 360 365 Phe Asp Asp Met Ser He Glu Leu Asn Gly He Glu Wing Asn His Gly 370 375 380 Lys Phe Ala Leu Val Lys Ser Aep Ser Asp Asp Leu Lys Thu Leu Thr 385 390 395 400 Gly Asn He Wing Met Thr Asp Val Lys His Wing Tyr Asp Lys Thr Gln 405 410 415 Wing Ser Thr Gln HIS Thr Glu Leu 420 This protein or polypeptide is approximately 42. 9 kDa. The polypeptide or hypersensitive response promoter protein derived from Pseudomonas solana cearum has an amino acid sequence corresponding to SEQ. ID. Do not . 35 as follows: M = t Ser Val Gly Asn He Gln Ser Pro Be Asn Leu Pro Gly Leu Gln 1 5 10 15 Asn Leu Asn Leu Asn Thr Asn Thr Asn Ser Gln Gln Ser Gly Gln Ser 20 25 30 Val Gln Asp Leu He Lys Gln Val Glu Lys Asp He Leu Asn He He 35 40 45 Wing Wing Leu Val Gln Lys Wing Wing Gln Ser Wing Gly Gly Asn Thr Gly 50 55 60 Asn Thr Gly Asn Wing Pro Wing Lys Asp Gly Asn Wing Asn Wing Gly Wing 65 70 75 80 Asn Asp Pro Ser Lys As Asp Pro Ser Lys Ser Gln Wing Pro Gln Ser 85 90 95 Wing Asn Lys Thr Gly Asn Val Asp Asp Wing Asn Asn Gln Asp Pro Met 100 * 105 110 G n Wing Leu Met Gln Leu Leu Glu Asp Leu Val Lys Leu Leu Lys Wing 115 120 125 ., .. _. ? ^ .. .. .....

The Leu His Met Gln Gln Pro Gly Gly Asn Aep Lye Gly Asn Gly Val 130 135 140 Gly Gly Wing Aen Gly Wing Lys Gly Wing Gly Gly Gln Gly Gly Leu Wing 145 150 155 160 Glu Ala Leu Gln Glu He Glu Gln He Leu Wing Gln Leu Gly Gly Gly 165 170 175 Gly Wing Gly Wing Gly Wing Gly Wing Gly Gly Val Gly Wing Gly Wing Gly 180 185 190? Asp Gly Gly Wing Gly Wing Gly Wing Gly Wing Gly Wing Wing Asn Gly Wing 195 200 205? Sp Gly Gly Asn Gly Val Asn Gly Asn Gln Wing Asn Gly Pro Gln Asn 210 215 220? Gly Asp Val Asn Gly Wing Asn Gly Wing Asp Asp Gly Ser Glu Asp 225 230 235 * 240 10 Gln Gly Gly Leu Thr Gly Val Leu Gln Lys Leu Met Lys He Leu Asn 245 250 255? The Leu Val Gln Met Met Gln Gln Gly Gly Leu Gly Gly Gly Asn Gln 260 265 270 Gone Gly Gly Lys Gly Wing Gly Asn Wing Ser Pro Wing Gly Ser 275 280 285 Wing Asn Pro Gly Wing Asn Gln Pro Gly Be Wing Asp Asp Gln Be Ser 15 290 295 300 Gly Gln Asn Asn Leu Gln Be Gln He Met Asp Val Val Lys Glu Val 305 310 315 320 Val Gln He Leu Gln Gln Met Leu Ala Ala Gln Asn Gly Gly Ser Gln 325 330 335 Gln Ser Thr Ser Thr Gln Pro Met 340 20 This is encoded by a DNA molecule having a nucleotide sequence corresponding to SEQ. 25 ID. No. 36 as follows: - ^ -.- ^ ita-- ATGTCAGTCG GAAACATCCA GAGCCCGTCG AACCTCCCGG GTCTGCAGAA CCTGAACCTC 60 AACACCAACA CCAACAGCCA GCAATCGGGC CAGTCCGTGC AAGACCTGAT CAAGCAGGTC 120 GAGAAGGACA TCCTCAACAT CATCGCAGCC CTCGTGCAGA AGGCCGCACA GTCGGCGGGC 180 GGCAACACCG GTAACACCGG CAACGcsccs GCGAAGGACG GCAATGCCAA CGCGGGCGCC 240 AACGACCCGA GCAAGAACGA CCCGAGCAAG AsccAsscTC CGCAGTCGGC CAACAAGACC 300 GGCAACGTCG ACGACGCCAA CAACCAGGAT CCGATGCAAG CGCTGATGCA GCTGCTGGAA 360 GACCTGGTGA AGCTGCTGAA GGCGGCCCTG CACATGCAGC AGCCCGGCGG CAATGACAAG 420 GGCA? CGGCG TGGGCGGTGC CAACGGCGCC AAGGGTGCCG GCGGCCAGGG CGGCCTGGCC 480 GAAGCGCTGC AGGAGATCGA GCAGATCCTC GCCCAGCTCG sCGGCGGCGG TGCTGGCGCC 540 GGCGCrCGCGG GTGGCGGTGT CGGCGGTGCT GGTGGCGCGG ATGGCGGCTC CGGTGCGGGT 600 GGCGCAGGCG GTGCGAACGO CGCCGACGGC GGCAATsscs TGAACGGCAA CCAGGCGAAC 660 GGCCCGCAGA ACGCAGGCGA TGTCAACGGT GCCAACGGCG CGGATGACGG CAGCGAAGAC 720 CAGGGCGGCC TCACCGGCGT GCTGCAAAAG CTGATGAAGA TCCTGAACGC GCTGGTGCAG 780 ATGATGCAGC AAGGCGGCCT CGGCGGCGGC AACCAGGCGC AGGGCGGCTC GAAGGGTG CC 840 GGCAACGCCT csccsspTC CGGCGCGAAC CCGGGCGCGA ACCAGCCCGG TTCGGCGGAT 900 GATCA? TCGT CCGGCCAGAA CAATCTGCAA TCCCAGATCA TGGATGTGGT GAAGGAGGTC 960 GTCCAGATCC TGCAGCAGAT GCTGGCGGCG CAGAACsGCG GCAGCCAGCA GTCCACCTCG 1020 ACGCACCCGA TGTAA 1035 Additional information regarding the polypeptide or hypersensitive response promoter protein derived from Pseudomonas solanacearum is described in Arlat, MF Van Gijsegem, JC Huet, JC Pemollet, and CA Boucher, "PopA ?, a Protein which Induces a Hypersensitive-like Response in Specific Petunia Genotypes, is Secreted via the Hrp Pathway of Pseudomonas solanacearum ", EMBO J., 13: 543-53, 1994), which is incorporated by reference herein.The polypeptide or hypersensitive response protein of Xanthomonas campestris pv. Glycines has an amino acid sequence corresponding to SEQ ID No. 37 as follows: Thr Leu He Glu Leu Met He Val Val Ala He He Ala Ala Leu Ala 1 5 10 15 10 Ala lie Ala Leu Pro Ala Tyr Gln Asp Tyr 20 25 This sequence is an amino-terminal sequence that has only 26 residues originating from the polypeptide or promoter protein of the hypersensitive response of Xan thomonas campestris pv. Wisteria This agrees with fimbrial subunit proteins determined in other pathogenic varieties of Xan thomonas 20 campestris. The polypeptide or protein promoter of the hypersensitive response of Xanthomonas campestris pv. Pelargonii is heat stable, sensitive to protease, and has a molecular weight of 20 kDa. This includes an amino acid sequence corresponding to SEQ. ID. No. 38 as follows: iiíi-Tiri-iifaiiiifinh ir ari i i Ser Ser Gln Gln Ser Pro Ser Wing Gly Ser Glu Gln Gln Leu Asp Gln 1 5 10 15 Leu Leu Ala Met 20 The isolation of the protein or polypeptide promoter of the hypersensitive response of Erwinia carotovora is described in Cui et al, "The RsmA 10 Mutant s of Erwinia carotovora subsp. carotovora Strain Ecc71 Overexpres hrp NEcc and Elicit a Hypersensitive Reaction-like Response in Tobacco Leaves "MPMI, 9 (7): 566-73 (1996), which is incorporated by reference herein The protein or polypeptide promoter of the response 15 hypersensitive of Erwinia stewartii is described in Ahmad et al., "Harpin is Not Neccesary for the Pathogenicity of Erwinia stewartii on Maize", 8th Int'l. Cong. Molec. Plant-Microbe Interact., July 14-19, 1996 and Ahmad et al., "Harpin is Not Necessary for the 20 Pathogenicity of Erwinia stewartii on Maize "Ann. Mt. Am. Phytopath Soc., July 27-31, 1996, which are incorporated herein by reference." Proteins or polypeptides promoting the hypersensitive response of Phytophthora parasitica, 25 Phytoph thora cryptogea, Phytophthora cinnamoni, Phytophthora capsici, Phytophthora megasperma, and Phytophora ci trophthora are described in Kaman et al.

"Extracellular Protein Elicitors from Phytophthora: Most Specificity and Induction of Resistance to Bacterial and Fungal Phytopathogens", Molec. Plant-Microbe Interact., 6 (1): 15-25 (1993), Ricci et al, "Structure and Activity of Proteins from Pathogenic Fungi Phythophthora Eliciting Necrosis and Acquired Resistance in Tobacco", Eur., J. Biochem., 183 : 555-63 (1989), Ricci et al., "Differential Production of Parasiticin, and Elicitor of Necrosis and Resistance in Tobacco, by Isolates of Phytophthora parasitica", Plant Path, 41: 298- 307 (1992), Baillreul et al., "A New Elicitor of the Hypersensitive Response in Tobacco: A Fungal Glicoprotein Elicits Cell Death, Expression of Defense Genes, Production of Salicylic Acid, and Induction of Systemic Acquired Resistance", Plant J., 8 (4): 551-60 (1995), and Bonnet and collaborators, "Acquired Resistance Triggered by Elicitors in Tobacco and Other Plants ", Eur.

J. Plant Path., 102: 181-92 (1996), which are incorporated by reference herein. Another promoter of the hypersensitive response according to the present invention is from Claviba cter mi chi ganensi s subspecie sepedoni cus which is fully described in U.S. Patent Application Serial No. 09 / 136,625, which is incorporated by reference in the present. ? . - - - - - - - - '---- - ..., r,, mf The above promoters are exemplary. Other promoters can be identified by the development of fungi or bacteria that promote the hypersensitive response, under conditions in which the genes encoding a promoter are expressed. Free cell preparations from culture supernatants can be tested for promoter activity (eg, local necrosis) by using these to infiltrate appropriate plant tissues. Fragments of the aforementioned hypersensitive response promoter polypeptides or proteins, as well as fragments of full length promoters from other pathogens are encompassed by the present invention. Suitable fragments can be produced by various methods. First, subclones of the gene encoding a known promoter protein are produced by convergent molecular genetic manipulation by subcloning gene fragments. The subclones are then expressed in vi tro or in vivo in bacterial cells to produce a small protein or peptide that can be tested for promoter activity according to the procedure described below.

As an alternative, fragments of a promoter protein can be produced by digestion of a full-length promoter protein with proteolytic enzymes such as chymotrypsin or proteinase A of Staphylococcus, or trypsin. Different proteolytic enzymes are likely to break down promoter proteins at different sites, based on the amino acid sequence of the promoter protein. Some of the fragments that result from proteolysis can be 10 active resistance promoters. In yet another procedure, based on the knowledge of the primary structure of the protein, the fragments of the promoter protein gene can be synthesized by using the PCR technique, together 15 with specific groups of primers chosen to represent particular portions of the protein. These could then be cloned with an appropriate vector for the expression of a truncated peptide or protein. The chemical synthesis can also be used 20 to make suitable fragments. Such a synthesis is carried out using known amino acid sequences for the promoter that is produced. Alternatively, by attaching a full-length promoter at high temperatures and high pressures, 25 will produce fragments. These fragments can be later separated by conventional procedures (eg, chromatography, SDS-PAGE). An example of suitable fragments of a hypersensitive response promoter that does not elicit a hypersensitive response includes fragments of the hypersensitive response promoter of Erwinia amylovora. Suitable fragments include a C-terminal fragment of the amino acid sequence of SEQ. ID. No. 23, an N-terminal fragment of the amino acid sequence of the 10 SEQ. ID. No. 23, or an internal fragment of the amino acid sequence of SEQ. ID. No. 23. The C-terminal fragment of the amino acid sequence of SEQ. ID. No. 23 can encompass the following amino acids of SEQ. ID. No. 23: 169 and 403, 210 and 403, 267 and 403, or 343 and 403. The fragment 15 of the amino acid sequence of the SEQ. ID. No. 23 can encompass the following amino acids of SEQ. ID. No. 23: 105 and 179, 137 and 166, 121 and 150, or 137 and 156. Other suitable fragments can be identified according to the present invention. Yet another example of a useful fragment of a hypersensitive response promoter, whose fragment itself does not elicit a hypersensitive response, is the protein fragment containing amino acids 190 to 294 of the amino acid sequence (SEQ ID No. 31) for the 25 hypersensitive response promoter of Pseudomonas syringae j ^ g ^ gu »^ --------- Í _-------- i ---- ^ ------ i pv. syringae. This fragment is useful in imparting resistance against the disease and improving plant development. Yet another example of a useful fragment of a hypersensitive response promoter is the peptide having an amino acid sequence corresponding to SEQ. ID. No. 39. This peptide is derived from the glycoprotein promoter of the hypersensitive response of Phytophthora megasperma and improves plant development. Variants can be elaborated, for example mediating the suppression or addition of amino acids that have minimal influence on the properties, secondary structure, and hydropathic nature of the polypeptide. For example, a polypeptide can be 15 conjugated to a signal sequence (or guide) at the N-terminus of the protein which co-translationally or post-translationally directs the transfer of the protein. The polypeptide can also be conjugated to a linker or to another sequence for ease of synthesis, purification, or Identification of the polypeptide. The fragment of the present invention is preferably in isolated form (for example separated from its host organism) and more preferably produced in purified form (preferably at least about 25 60%, more preferably 80% pure) by techniques - ~ »-" ^ "* '' -" ^ conventional. Typically, the fragment of the present invention is produced but not secreted into the growth medium of the recombinant host cells. Alternatively, the protein or polypeptide of the present invention is secreted into the growth medium. In the case of the non-secreted protein, to isolate the protein fragment, the host cell (e.g., E. coli) which possesses the recombinant plasmid is propagated, used by sonication, heat or chemical treatment, and the homogenate is centrifuged for eliminate bacterial waste. The supernatant is then subjected to heat treatment and the hypersensitive response promoter is separated by centrifugation. The supernatant fraction containing the hypersensitive response promoter is subjected to gel filtration on a dextran or polyacrylamide column of adequate size to separate the fragment. If necessary, the protein fraction can be purified by ion exchange or HPLC high-resolution liquid chromatography. The DNA molecule that codes for the polypeptide fragment or hypersensitive response promoter protein can be incorporated into the cells using conventional recombinant DNA technology. In general, this involves the insertion of the DNA molecule into an expression system for which the DNA molecule is heterologous (for example not normally present). The heterologous DNA molecule is inserted into the expression system or vector in the sense orientation and in the correct reading structure. The vector contains the necessary elements for the transcription and translation of the inserted protein coding sequences. U.S. Patent No. 4,237,224 to Cohen and Boyer, which is incorporated by reference herein, describes the production of expression systems in the form of recombinant plasmids using restriction enzyme cleavage and ligation with DNA ligase. . These recombinant plasmids are then introduced by means of transformation and replicated into unicellular cultures 15 including prokaryotic organisms and eukaryotic cells grown in tissue culture. Recombinant genes can also be introduced into viruses, such as vaccinia virus. Recombinant viruses can be generated by transfection of plasmids in cells infected with the virus. Suitable vectors include, but are not limited to, the following viral vectors such as the gtll system of the lambda vector, gt.WES.tB, Charon 4, and the 25 plasmid vectors such as pBR322, pBR325, pACYC177, -, g-? ¡ia¡a-j »- l-i-ta-Bt-a5a« .... A < - "y-uf *" "'* pACYC1084, pUC8, püC9, püC18, püC19, pLG339, pR290, pKC37, pKClOl, SV 40, pBluescript II SK +/- or KS +/- (see Catalog" Stratagene Cloning Systems " (1993) by Stratagene, La Jolla, California, incorporated by reference in the present 5) series pQE, pIH821, pGEX, pET (see FW Studier et al., "Use of T7 RNA Polymerase to Direct Expression of Cloned Genes" , Gene Expression Technology vol.185 (1990), which is incorporated by reference herein), and any derivatives of the 10 same. Recombinant molecules can be introduced into cells via transformation, particularly transduction, conjugation, mobilization or elect oporation. The DNA sequences are cloned into the vector using standard cloning procedures in 15 the technique, as described by Sambrook et al Molecular Cloning: A Laboratory Manual, Cold Springs Laboratory, Cold Springs Harbor, New York (1989) which is incorporated by reference herein. A variety of systems can be used 20 vector-host to express the sequence (s) coding for the protein. Primarily, the vector system must be compatible with the host cell used. Host-vector systems include but are not limited to the following: bacteria transformed with DNA 25 of teriophage, plasmid DNA or cosmid DNA; the ^^^^^ - ^^^ microorganisms such as yeast containing yeast vectors; mammalian cell systems infected with virus (for example vaccinia virus, adenovirus, etc.); insect cell systems infected with the virus (eg Baculovirus); and plant cells infected by bacteria. The expression elements of these vectors vary in their resistance and specificities. Depending on the host vector system used, any of a number of suitable transcription and translation elements can be used. Different genetic signals and processing events control many levels of gene expression (eg, transcription of DNA and translation of messenger RNA (mRNA).) Transcription of DNA is dependent on the presence of a promoter that is a sequence. of DNA that directs the binding of RNA polymerase and thereby promotes the synthesis of mRNA The DNA sequences of eukaryotic promoters differ from those of prokaryotic promoters In addition, eukaryotic promoters and accompanying genetic signals can to be recognized in or may not work in a procaiotic system, in addition, prokaryotic promoters are not recognized and do not work in eukaryotic cells. j-at * i «? - - * - ** * Similarly, the translation of mRNA in prokaryotes depends on the presence of adequate prokaryotic signals that differ from those of eukaryotes. Efficient translation of mRNA in prokaryotes requires a ribosome binding site called the Shine-Dalgarno ("SD") sequence on the mRNA. This sequence is a short nucleotide sequence of the mRNA that is located before the start codon, usually AUG, which codes for the amino-terminal methionine of the protein. The SD sequences are complementary to the 3 'end of the 16S rRNA (ribosomal RNA) and probably promote the binding of the mRNA to the ribosomes, by duplication or duplexing with the rRNA to allow correct positioning of the ribosome. For a review on maximizing gene expression, see Roberts and Luer. Methods in Enzymology. 68: 473 (1979), which is incorporated by reference herein. The promoters vary in their "strength or resistance" (for example their ability to promote transcription). For purposes of expressing a cloned gene, it is desirable to use strong promoters in order to obtain a high level of transcription and, therefore, expression of the gene. Depending on the system of the host cell used, any of a number of suitable promoters can be used. For example, when fea- * • u * ^ clone in E. coli their bacteriophages or promoter plasmids such as the phage T7 promoter, the c promoter, the trp promoter, the recA promoter, the ribosomal RNA promoter, the PR and PL promoters of the lambda coliphage and others, including but not limited to lacUV5, ompF, bla, lpp, and the like, can be used to direct high levels of transcription of adjacent DNA segments. In addition, a trp-2acUV5 hybrid promoter (tac) or other E. coli promoters produced by recombinant DNA or other synthetic DNA techniques can be used to provide transcription of the inserted gene. Bacterial host cell strains and expression vectors can be chosen, which inhibit the action of the promoter, unless specifically induced. In certain operations, the addition of specific inductors is necessary for the efficient transcription of the inserted DNA. For example, the lac operon is induced by the addition of lactose or IPTG (isopropylthio-beta-D-galactoside). A variety of other operons, such as trp, pro, etc., are under different controls. The specific start signals are also required for efficient transcription and translation of the prokaryotic cell genes. These signals of initiation of transcription and translation may vary in "strength" as measured by the amount of the specific messenger RNA of the gene and the synthesized protein, respectively. The DNA expression vector, which contains a promoter, can also contain any combination of various "strong" start transcription and / or translation signals. For example, efficient translation in E. coli requires that an SD sequence of approximately 7-9 bases, 5 'to the start codon ("ATG"), provide a ribosome binding site. In this way, any combination of SD-ATG that can be used by the ribosomes of the host cell can be used. Such combinations include, but are not limited to, the SD-ATG combination from the ero gene or the AJ gene from the lambda coliphage, or from the E, D, C, B or A genes of tryptophan, from E. coli. In addition, any SD-ATG combination produced by recombinant DNA or other techniques involving the incorporation of synthetic nucleotides can also be used. Once the isolated DNA molecule encoding the fragment of a polypeptide or hypersensitive response promoter protein has been cloned into an expression system, it is ready to be incorporated into a host cell. Such incorporation can be carried out by various forms of transformation noted above, depending on the system of the ^^^^ - ^ É ^^^^ g ^ | g ^ g | ^^ vector host-cell. Suitable host cells include, but are not limited to, bacteria, viruses, yeast, mammalian cells, insect, plants and the like. The present invention also relates to methods for imparting disease resistance to plants, increasing the growth of plants, and / or effecting insect control for plants. These methods involve the application of the fragment of a protein or polypeptide promoter of the hypersensitive response which does not promote a sensitive hypersensitivity response in a non-infectious form for all or part of a plant or a seed of a plant under effective conditions so that the fragment impart resistance against disease, increase growth and / or control insects. Alternatively, these fragments of a protein or polypeptide promoter of the hypersensitive response can be applied to plants, such that the seeds recovered from such plants by themselves are capable of imparting resistance to the disease in plants, increasing the growth of the plant, and / or perform insect control. As an alternative to the application of a fragment of a protein or polypeptide that promotes the hypersensitive response to plants or plant seeds, in order to impart resistance against the disease in plants, carry out the development of the plant and / or to control the insects on the plants or the plants developed from the seeds, transgenic plants or seeds of transgenic plants can be used. When transgenic plants are used, this involves the provision of a transgenic plant transformed with a DNA molecule that codes for a fragment of a polypeptide or hypersensitive response promoter protein, whose fragment does not promote a hypersensitive response, and the development of the plant under effective conditions to allow the DNA molecule to impart resistance against the disease to plants, increase the growth of the plant and / or control insects. Alternatively, a transgenic plant seed transformed with a DNA molecule encoding a fragment of a hypersensitive response promoter or polypeptide protein, which fragment does not promote a hypersensitive response, may be provided and planted in the soil. A plant is then propagated from the seeded seed, under effective conditions to allow the DNA molecule to impart resistance against the disease to the plants, increase plant growth and / or insect control.

The method of the present invention wherein the hypersensitive response promoting polypeptide or protein is applied to the plant or seed of the plant, can be carried out in a number of ways, including: 1) the application of an isolated fragment or 2) the application of bacteria that do not cause the disease and are transformed with a gene that codes for the fragment. In the latter embodiment, the fragment can be applied to plants or plant seeds by the application of bacteria containing the DNA molecule encoding the polypeptide fragment or hypersensitive response promoter protein, which fragment does not promote a hypersensitive response. Such bacteria must be capable of secreting or exporting the fragment, so that the fragment can make contact with the cells of the plant or with the seeds of the plants. In these modalities, the fragment is produced by the bacteria in plan t a or on the seeds, or just before the introduction of the bacteria to the plants or to the seeds of the plants. The methods of the present invention can be used to treat a wide variety of plants or their seeds, to impart resistance against the disease, enhance development and / or control insects. Suitable plants include dicotyledons and monocots. More particularly, useful harvest plants can include: alfalfa, rice, wheat, barley, rye, cotton, sunflower, peanut, corn, potato, sweet potato, beans, peas, chicory, lettuce, chicory, cabbage, Brussels sprouts, beets, chirivia , turnip, cauliflower, broccoli, radish, spinach, onion, garlic, eggplant, pepper, celery, carrot, squash or chayote, pumpkin, zucchini, cucumber, apple, pear, melon, citrus, strawberry, grape, raspberry, pineapple, bean of soy, tobacco, tomato, sorghum, and sugarcane. Examples of suitable ornamental planting are: Arabidopsis thaliana, Samtpa ulia, petunia, pelargonium, red shepherdess, chrysanthemum, clavula and zinia. With respect to the use of the protein or polypeptide promoter of the hypersensitive response of the present invention in imparting resistance against the disease, absolute immunity against infection may not be conferred, but the severity of the disease is reduced and the development of the symptoms It is retarded. The number of lesions, the size of the lesions, and the degree of sporulation of fungal pathogens are all diminished. This method of imparting resistance against the disease has the potential to treat previously untreatable diseases, the treatment of diseases systemically that can not be treated separately, due to cost, and to avoid the use of infectious agents or environmentally harmful materials. The method for imparting pathogen resistance to plants according to the present invention is useful in imparting resistance to a wide variety of pathogens, including viruses, bacteria and fungi. Resistance, among others, to the following viruses can be achieved by the method of the present invention: Tobacco mosaic virus and tomato mosaic virus. The resistance, among others, to the following bacteria can be imparted to plants according to the present invention: Pseudomonas solanacearum, Pseudomonas syringae pv. tabaci and Xanthomonas campestris pv. pelargonii. The plants can be made resistant, inter alia, to the following fungi by the use of the present invention: Fusarium um oxysporum and Phytophthora infes tans. With respect to the use of the fragments of the protein or polypeptide promoter of the hypersensitive response of the present invention, to improve or increase the development of the plants, various forms of growth enhancement or promotion of the plants can be achieved. This can happen as early as when the plant begins to develop from the seeds or later in the life of a plant. By , ...-. Aj ... ^ * J-example, the development according to the present invention encompasses higher yield, increased amount of seeds produced, increased percentage of germinated seeds, increased size of the plant, higher biomass , more and more large fruits, earlier coloration of the fruit, and earlier ripening of the fruit and the plant. As a result, the present invention provides significant economic benefits for growers. For example, early germination and early maturation allow crops to be grown in areas where short development seasons could otherwise exclude their development at that site. The increased percentage of germination of the seeds results in improved resistances in the harvests and more efficient use of the seeds. Higher yield, increased size, and increased biomass production allow greater income generation from a given portion of land. Yet another aspect of the present invention is directed to effecting any form of insect control for plants. For example, insect control according to the present invention covers preventing that insects come in contact with plants to which the hypersensitive response promoter has been applied, preventing direct damage by the insect to plants - "* - < through feeding damage, causing insects to move away from such plants, killing insects near such plants, interfering with the feeding of insect larvae on such plants, preventing insects from colonizing plants host, preventing colonizing insects from releasing phytotoxins, etc. The present invention also prevents subsequent damage by disease to plants, resulting from infection by the insect.The present invention is effective against a wide variety of insects. European maize is a major pest of maize (sweet and tooth corn) but it also feeds more than 200 plant species including green beans, serous bean and half-moon beans and edible soybeans, peppers, potatoes, tomatoes, plus many herb species, pests of additional insect larvae that feed on many plants that damage a wide variety of crops Vegetables include the following: beet devastating worm, cabbage measuring worm, corn ear worm, devastating autumn worm, diamond back moth, cabbage root larva, onion larva, larva of the corn seed, stripping worm (melon worm), pepper larva, tomato and larvae. Collectively, this group of insect pests represents the economically most important group of pests for the production of vegetables worldwide. The method of the present invention that involves the application of the fragment of a polypeptide or hypersensitive response-promoting protein, fragment that does not promote a hypersensitive response, can be carried out through a variety of procedures when all or part of the plant is treated, including leaves, stems, roots, propagules (for example, cuttings), etc. This may involve (but does not require) the infiltration of the polypeptide fragment or promoter protein of the hypersensitive response within the plant. Suitable application methods include spraying at high or low pressure, injection and abrasion of the sheet close to when the promoter application takes place. When plant seeds or propagules thereof are treated (e.g., cuttings, according to the embodiment of the present invention, the fragment of the hypersensitive response promoter or protein polypeptide, according to the present invention, can be applied by low or high pressure scrubbing, coating, immersion or injection Other suitable application procedures may be considered by those skilled in the art, provided they are capable of making the contact --------- Í ---- L of the fragment with the cells of the plant or the seed of the plant. Once treated with the hypersensitive response promoter fragment of the present invention, the seeds can be planted in natural or artificial soil and cultured using conventional methods to produce plants. After the plants have been propagated from the treated seeds according to the present invention, the plants can be treated with one or more applications of the hypersensitive response promoter protein or polypeptide fragment or whole promoters to impart resistance against the disease to the plants, to increase the growth of the plants, and / or to control the insects on the plants. The fragment of the hypersensitive response promoter or polypeptide protein, according to the present invention, can be applied to plants or plant seeds, alone or in admixture with other materials. Alternatively, the fragment can be applied separately to the plants with other materials that are applied at different times. A composition suitable for treating plants or plant seeds according to the embodiment of the present invention contains a fragment of a polypeptide or response-promoting protein. hypersensitive, fragment that does not promote a hypersensitive response in a carrier. Suitable carriers include water, aqueous solutions, suspensions or dry powders. In this embodiment, the composition contains more than 5,500 nM fragment. Although not required, this composition may contain additional additives including fertilizers, insecticides, fungicides, nematicides, and mixtures thereof. Suitable fertilizers include (NH4) 2N03. An example of a suitable insecticide is malathion. Useful fungicides include Captan. Other suitable additives include buffers, wetting agents, coating agents, and abrasive agents. These materials 15 can be used to facilitate the process of the present invention. In addition, the fragment that promotes the hypersensitive response can be applied to plant seeds with other conventional seed formulation and treatment materials, including clays and polysaccharides. In the alternative embodiment of the present invention, which involves the use of transgenic plants and transgenic seeds, a fragment of a hypersensitive response promoter need not be applied topically to plants or seeds. Rather, the - itHjnjuer ** * - * - '* * •' ifTlÉ'J? ff transgenic plants transformed with a DNA molecule encoding such a fragment are produced according to procedures well known in the art. The vector described above can be directly microinjected into plant cells by the use of micropipettes to mechanically transfer the recombinant DNA. Crossway, Mol. Gen. Genetics, 202: 179-85 (1985), which is incorporated by reference herein. The genetic material can be transferred to the plant cell using polyethylene glycol. Krens et al., Nature, 296: 72-74 (1982) which is incorporated by reference herein. Another method for transforming plant cells with a gene that imparts resistance against pathogens is the bombardment of particles (also known as biolistic transformation) of the host cell. This can be accomplished in one of several ways. The first involves the propulsion of inert or biologically active particles to the cells. This technique is described in U.S. Patent Nos. 4,945,050, 5,036,006 and 5,100,792, all to Sanford et al. Which are incorporated by reference herein. In general, this procedure involves the propulsion of inert or biologically active particles in the cells under effective conditions to penetrate the ^^^ outer surface of the cell, and to be incorporated into the interior thereof. When inert particles are used, the vector can be introduced into the cell by coating the particles with the vector containing the heterologous DNA. Alternatively, the target cell can be surrounded by the vector, so that the vector is brought to the cell by the awakening of the particle. Biologically active particles (eg, dehydrated bacterial cells containing the vector and heterologous DNA) can also be propelled into plant cells. Another method for the introduction is the fusion of protoplasts with other entities, either mini-cells, cells, lysosomes, or other fusible bodies with lipid surface. Fraley et al. Proc. Nati Acad. Sci USA. 79: 1859-62 (1982), which is incorporated by reference herein. The DNA molecule can also be introduced into plant cells by electroporation. Fromm et al., Proc. Nati Acad. Sci. USA, 82: 5824 (1985), which is incorporated by reference herein. In this technique, the plant protoplasts are subjected to electroporesis in the presence of plasmids containing the expression cassette. The high field strength electrical impulses reversibly permeabilize the ^ .AM. biome: mbranas, allowing the introduction of the plasmids. Plant protoplasts subjected to electroporesis reform the cell wall, divide it and regenerate it. 5 Another method for the introduction of the DNA molecule into plant cells is to infect a plant cell with Agrobacterium tumefaciens or A. rhi zogenes previously transformed with the gene. Under appropriate conditions known in the art, transformed plant cells are developed to form shoots or roots, and are further grown in plants. In general, this procedure involves inoculating the plant tissue with a suspension of bacteria and incubating the tissue for 48 to 72 hours on the regeneration medium without antibiotics at 25-28 ° C. Agrobacterium is a representative genus of the Gram negative family of Rhizobiaceas. Its species are responsible for diseases of the gall bladder (A. zumefa ciens) and the hairy root [A. rhizogenes). The 20 plant cells in crown vesicle tumors and hairy roots are induced to produce amino acid derivatives known as opinas, which are catabolized only by bacteria. The bacterial genes responsible for the expression of opines are a convenient source of control elements for cassettes of AaYes "2A-- '- -, tt-? U ...-, í -, -,..,,.".,.,.,.,. * - ~ ° i "" iíBliM chimeric expression. In addition, the assay for the presence of the opines can be used to identify the transformed tissue, the heterologous genetic sequences can be introduced into appropriate plant cells, by means of the Ti plasmid of A. tumefaciens or the Ri plasmid of A. rhizogenes. Plasmid Ti or Ri is transmitted to plant cells in infection by Agrobacterium and is stably integrated into the plant genome, J. Shell, Science, 237-1176-83 (1987), which is incorporated by reference herein. After transformation, the transformed plant cells must be regenerated Plant regeneration from cultured protoplasts is described in Evans et al., Handbook of Plant Cell Cultures, Vol. 1: (MacMillan Publishing Co., New York, 1983); and Vasil IR (ed), Cell Culture and Somatic Cell Genetics of Plants. Press, Orlando, Vol. I, 1984, and Vol III (1986), which are incorporated by reference herein. It is known that practically all plants can be regenerated from cultured cells or tissues, including but not limited to, all major species of sugarcane, sugar beets, cotton, fruit trees and legumes. ÍH ---. The means for regeneration vary from species to species of plants, but in general it is first provided a suspension of transformed protoplasts or a petri dish containing transformed explants. The callus tissue is formed and the shoots can be induced from the callus and subsequently rooted. Alternatively, the formation of the embryo can be induced in the callus tissue. These embryos germinate as natural embryos to form plants. The culture media will generally contain various amino acids and hormones, such as auxin and cytokinins. It is also advantageous to add glutamic acid and proline to the medium, especially for species such as corn and alfalfa. Efficient regeneration will depend on the medium, the genotype, and the history of the crop. If these three variables are controlled, then regeneration is usually reproducible and repeatable. After the expression cassette is stably incorporated in the transgenic plants, it can be transferred to other plants by sexual crossing. Any of a number of standard breeding techniques can be used, depending on the species that is to be crossed. Once transgenic plants of this type are produced the plants themselves can be cultured according to conventional procedures, with the presence of the gene encoding the hypersensitive response promoter fragment, resulting in resistance against the disease, increased growth of the plant, and / or control of insects on the plant. Alternatively, transgenic seeds or propagules (for example, cuttings) are recovered from the transgenic plants. The seeds can then be planted in the soil and grown using conventional procedures to produce transgenic plants. The transgenic plants are propagated from transgenic planted seeds, under effective conditions to impart resistance against the disease to the plants, to improve or increase the growth of the plant and / or to control the insects. While not wishing to be bound by any theory, such resistance against disease, increase in growth, and / or control of insects can be mediated by RNA, or can result from expression of the polypeptide or protein fragment. When the transgenic plants and the seeds of plants are used according to the present invention, they can also be treated with the same materials used to treat the plants and seeds, to which a fragment of a --_----- > "^^^^^^ hypersensitive response promoter according to the present invention. These other materials, including the hypersensitive response promoter according to the present invention, can be applied to other transgenic plants and plant seeds by the above-indicated procedures, including a.-ta or low pressure spraying, injection, coating. and immersion. Similarly, after the plants have been propagated from the seeds of transgenic plants, the plants can be treated with one or more applications of the fragment of a hypersensitive response promoter, according to the present invention, to impart resistance against the disease, increase the development and / or control the insects. Such plants can also be treated with conventional agents for the treatment of plants (for example, insecticides, fertilizers, etc.).

EXAMPLES Example 1 - Bacterial strains and plasmids The strains of Escherichia coli used in the following examples include DH5a and BL21 (DE3) purchased from Gibco BRL (Grand Island, N. Y) and Stratagene la Jolla California), respectively. The vector pET28 (b) was purchased from Novagen (Madison, Wl). Eco DH5a / 2139 contained the complete hrpN gene. Construction 2139 was produced by D. Bauer at Cornell University. The hrpN gene was excised from plasmid 2139 by restriction enzyme digestion with HindIII, then purified from an agarose gel to serve as the DNA template for the PCR synthesis of the truncated hrpN clones. These clones were subsequently inserted into the vector (His) 6 pET28 (b) which contained a Kanr gene for the selection of the transformants.

Example 2 - DNA manipulation Restriction enzymes were obtained from Boheminger Mannheim (Indianapolis, IN) or Gibco BRL, La T4 DNA-ligase, Calcium Alkaline Phosphatase, Calf (CIAP), and PCR SupermixMR were obtained from Gibco BRL. He QIAprep Rotary Miniprep Kit, the Quiagen Mini Plasmid Kit, and the QIAquick PCR Purification Kit were purchased from Quiagen (Hilden, Germany). The PCR primers were synthesized by Lofstrand Labs Limited (Gaithersburg, MD). The oligopeptides were synthesized by Bio-Synthesis, Inc. (Lewisville, TX). All DNA manipulations such as isolation ^ ^ ^ 2 ^ of the plasmid, restriction enzyme digestion, DNA ligature, and PCR were performed according to standard techniques (Sambrook et al., Laboratory Manual, Second Edition, Cold Spring Harbor Laboratory Press (1989) or the protocols provided by the manufacturer.

Example 3 - Fragmentation of the hrpN gene A series of hrpN genes truncated at the N-terminus and the C-terminus and internal fragments were generated via PCR (Figure 1). The full-length hrpN gene was used as the DNA template and the 3 'and 5' primers were designed for each truncated clone (Figure 2). The 3 'primers contained an Ndel enzyme that cleaves the site containing the start codon ATG (methionine) and the 5' primers contained the stop codon TAA and a HindIII enzyme that cleaves the site for ligation in the vector pET28 (b ). PCR was carried out in 0.5 ml tubes in a GeneAmpMR 9700 kit (Perkin-Elmer, Foster City, CA). 45 μl of Supermix ™ (Life Technology, Gaithersburg, MD) were mixed with 20 pmol of each pair of DNA primers, 10 ng of full-length harpin DNA, and deionized water to a final volume of 50 μl. After heating the mixture at 95 ° C for 2 minutes, PCR was performed for 30 minutes.

T -irw-ffl- Hirrt cicles at 94 ° C for 1 minute, 58 ° C for 1 minute and 72 ° C for 1.5 minutes. The PCR products were verified on a 6% TBE Gel (Novex, San Diego, CA). The amplified DNA was purified with QIAquick PCR purification equipment, digested with Ndel and HindIII at 37 ° C for 5 hours, extracted once with a mixture of phenol: chloroform: isoamyl alcohol (25: 25.1) and ethanol precipitated. 5 μg of the vector DNA pET28 (b) were digested with 15 units of Ndel and 20 units of HindIII at 37 ° C for 3 hours, followed by the treatment with CIAP to reduce the resultant artuate of incomplete digestion with simple enziira. The digested vector DNA was purified with QIAquick PCR purification equipment and directly used for ligation. The ligation was carried out at 14-16 ° C for 5 to 12 hours in a 15 μl mixture containing approximately 200 ng of digested pET28 (b), 30 ng of the targeted PCR fragment, and one DNA-ligase unit. T4 5-7.5 μl of the ligation solution was added to 100 μl of the competent DH5a cells in a 15 ml Falcon tube and incubated on ice for 30 minutes. After a thermal shock at 42 ° C for 45 seconds, 0.9 ml of SOC solution or 0.45 ml of LB medium was added to each tube, and incubated at 37 ° C for 1 hour. 20, 100 and 200 μl of the transformed cells were placed on the LB agar with 30 μg / ml kanamycin and incubated at 37 ° C overnight.

Single colonies were transferred to 3 ml of LB medium and incubated overnight at 37 ° C. The plasmid DNA was prepared from 2 ml of culture with the QIAprep Miniprep Miniprep team (QUIAGEN, Hilden, Germany). The DNA from the transformed cells was analyzed by restriction enzyme digestion or partial sequencing to verify the success of the transformations. Plasmids with the desired DNA sequence were transferred to strain BL21 using the standard chemical transformation method as indicated above. A clone containing the full-length harpin protein in the vector pET28 (b) was generated as a positive control, and a clone with only the vector pET28 (b) was generated as a negative control.

Example 4 - Expression of Promotional Truncated Proteins of the Hypersensitive Response BL21 (DE3) strains of Escherichia coli containing the hrpN clones were grown in Luria broth medium (5 g / l Difco yeast extract, 10 g / l Tryptone Difco, 5 g / l sodium chloride e 1 mM sodium hydroxide) containing 30 μg / ml kanamycin at 37 ° C overnight. The bacteria were then inoculated into 100 volumes of the same medium and developed at 37 ° C at an optical density (DÜ62o) of 0.6-0.8. The bacteria were subsequently inoculated in 250 μl volumes of the same medium and developed at 37 ° C to an OD620 of approximately 0.3 or 0.6-0.8. A millimolar of IPTG was then added and the cultures were grown at 19 ° C overnight (approximately 18 hours). Not all clones were successfully expressed using this strategy. Several of the clones had to be developed in Terrific broth (12 g / liter Tryptone Bacto, 24 g / liter Bacto yeast, 0.4% glycerol, 0.17 M KH2P04, and 0.72 M K2HP0), and / or developed at 37 ° C after induction with IPTG and / or harvested earlier than overnight (Table 1).

Table 1: Expression of the truncated proteins that promote the hypersensitive response conro 12 -342 LB 06-0.8 19 ° C 16-18 hr ui. _-_ ^ - -, Example 5 - Small Scale Purification of Promotional Truncated Proteins of Hypersensitive Response (Verification of Expression) A 50 ml culture of a hrpN clone was developed as described above to induce the expression of the truncated protein. After harvesting the culture, 1.5 ml of the cell suspension was centrifuged at 14,000 rpm for 5 minutes, resuspended in urea lysis buffer (8 M urea, 0.1 M Na2HP04, and 0.01 M Tris, pH 8.0), incubated at room temperature for 10 minutes, then centrifuged again at 14,000 rpm for 10 minutes, and the supernatant was saved. An aliquot of 50 μl of a 50% suspension of a nickel agarose gel resin that binds to (His) 6 equilibrated was added to the supernatant and mixed at 4 ° C for one hour. The nickel agarose was then washed three times with urea wash buffer (8 M urea, 0.1 M Na2HP04, and 0.01 Tris - pH 6.3), centrifuging at 5,000 rpm for five minutes between washes. The protein was eluted from the resin with 50 μl of the urea elution buffer (8 M urea, 0.1 M Na2HP04, 0.01 M Tris, and 0.1 M EDTA - pH 6.3). The eluate was run on a 4-20% Tris-glycine-pre-laden gel, one at 16% and one at 10-20%, depending on the size of the truncated protein, to verify expression.

Example 6 - Induction of HR in Tobacco A 1.5 ml aliquot from the 50 ml cultures developed for small-scale purification of the truncated proteins was centrifuged at 14,000 rpm for four minutes and resuspended in an equal volume of 5 mM potassium phosphate buffer, pH 6.8 . The cell suspension was sonicated for approximately 30 seconds and then diluted 1: 2 and 1:10 with the phosphate builder. Both dilutions plus the lysate of pure cells were infiltrated in the fourth to ninth leaves of tobacco plants with 10 to 15 leaves, by making a hole in single-leaf panels, and infiltrating the bacterial lysate into the intercellular space of the leaf. , using a syringe without a needle. HR response was recorded 24-48 hours after infiltration. Tobacco seedlings were developed (Ní cc tiana tabacum v. Xanthi) in an environmental chamber at 20-25 ° C, with a photoperiod of 12 hours of light / 12 hours of darkness and approximately 40% of RH. The cell lysate was used for the initial HR assays (in order to select the truncated proteins for the activity of a ... T,? li - iH «* -,!« - «,. - r -r. -to,, t il - -,. , - ^ i ^^^ HR) since the purification with urea on a small scale produced very little protein, which was denatured due to the purification process.

Example 7 - Native Purification on a Large Scale of the Truncated Protein Promoters of Response Hypersensitive for Integral Biological Activity Trials Six 500 ml cultures of the hrpN clone were developed as described at the beginning to induce the expression of the truncated protein. After harvesting the culture, the cells were centrifuged at 7,000 rpm for 5 minutes, resuspended in imidazole lysis buffer (5 mM imidazole, 0.5 M sodium chloride, 20 mM Tris) plus 0.05% Triton X-100 and lysozyme a 0.1 mg / ml, incubated at 30 ° C for 15 minutes, sonicated for 2 minutes, centrifuged again at 15,000 rpm for 20 minutes, and the supernatant was saved. A 4 ml aliquot of a 50% suspension of a nickel agarose resin that binds to (His) 6 / equilibrium was added to the supernatant and mixed at 4 ° C for about 4 hours. The nickel agarose was then washed three times with imidazole wash buffer (20 mM imidazole, 0.5 M sodium chloride, and 20 mM Tris), centrifuged at 5,000 rpm for five minutes between washes, then placed on a column of disposable chromatography. The column was centrifuged at 1100 rpm for one minute to remove any residual wash buffer and then the protein was eluted from resin 5 with 4 ml of imidazole elution buffer (1 M imidazole, 0.5 M sodium chloride, and 20 mM Tris) by incubating the column with the elution buffer for ten minutes at room temperature and then centrifuging the column at 1100 rpm for one minute. The eluate was run on a 4-20% Tris-glycine, a 16% or a 10-20% Tris-glycine gel, depending on the size of the truncated protein to verify expression. The concentration of the pyroteins was determined by comparison of the protein bands with a standard protein in Mark 12 molecular weight marker.

Example '8 - Purification with Large Scale Urea of the Truncated Proteins, Promoting the Hypersensitive Response, for the Integral Biological Activity Trial.

The procedure was the same as the large-scale native purification, except that the urea lysis buffer, the wash buffer, and the elution buffer were used, and the cells were not > - ^ ¡H ^? .. - .. i < . ,,. , .-,. is. ^. , ü? ^ A ^? e sonicated as in the native purification. After purification, the protein was renatured by dialysis against increasingly low concentrations of urea over a period of eight hours, then dialyzed overnight against 10 mM Tris / 20 mM NaCl. The renaturation process caused the N-terminal proteins to precipitate. The protein 1-168 precipitated was solubilized by the addition of 100 mM Tris-HCl at pH 10.4, then heating the protein at 30 ° C for about one hour. The concentration of the protein was determined by comparing the protein bands with a standard protein in the Mark 12 molecular weight marker. Protein fragments 1-75 and 1-104 were not successively solubilized using this strategy since they were sonicated in 100 mM Tris-HCl at pH 10.4, to solubilize as much of the protein as possible and expose the active sites of the protein for assays of biological activity.

Example 9 - Induction of Growth Increase (GE) Sixty tomato seeds (Lycopersicon spp. Marglobe) were soaked overnight in 10 and 20 μg / ml of the truncated protein diluted with 5 mM potassium phosphate buffer, pH 6.8. The next morning, the sixty seeds were sown in three pots and 2-15 days later and again 18-20 days later the heights of the 10 highest tomato plants per pot were measured and compared with the heights of the treated control plants only with the phosphate buffer. The analyzes were carried out on the heights to determine if there was a significant difference in the height of the plants treated with the truncated proteins, in comparison with the control with buffer, and with this to determine if the proteins induced or not the increase of growth .

Example 10 - Induction of Acquired Systemic Resistance (SAR) Three tobacco plants (Ni cotiana taba cum cv. Xanthi) with 8-12 leaves (plants approximately 75 days old) were used in the trial. One leaf of the tobacco plants was covered and the rest of the leaves were sprayed with approximately 50 ml of a solution at 20 μg / ml of the truncated proteins diluted with the 5 mM potassium phosphate buffer. Five to seven days later two leaves (the non-sprayed leaf and the opposite sprayed leaf and just above the non-sprayed leaf) were inoculated with 20 μl of a 1.8 μg / ml TMV solution along with a pinch of S "" "" "**" * diatomaceous earth by rubbing the mixture along the upper surface of the leaves. The TMV entered the plants through tiny lesions made by the diatomaceous earth. Approximately 3 to 4 days after inoculation with TMV, the number of TMV lesions was counted on both leaves, compared to the number of lesions on the negative control leaves treated with the buffer. Analyzes were performed to determine the effectiveness of reducing the number of TMV lesions by protein fragments compared to control with buffer. The percentage of effectiveness was calculated as: Reduction in the TMV lesions (% of effectiveness) = 100 x (1- # average of lesions on the treated leaves / # medium of lesions on the control leaves with buffer).

EXAMPLE 11 Expression of Promotional Truncated Proteins of the Hypersensitive Response The expression and small scale purification of the protein fragments was performed to select the expression and activity of HR (Table 2). .j ^^ TABLE 2 Expression and HR activity of the truncated proteins that promote the hypersensitive response (small scale selection) All cloned fragmentary proteins were expressed at varying levels except for the three small fragments (amino acids 169-209, 150-209, and 150-180). Fragments 210-403 and 267-403 were expressed very well, producing a high concentration of protein from a small-scale purification, resulting in a substantial protein band on SDS gel electrophoresis. Other fragments (such as amino acids 1-168 and 1-104) produced much less protein, resulting in faint protein bands after electrophoresis. It was difficult to determine if the 343-403 fragment, the smallest C-terminal protein, was expressed, since there were several previous proteins, 15 apparent on the gel, in addition to the 343-403 protein suspect. The positive control and negative control proteins, consisting of the promoter protein of the 1 »-, - ^ --- ^ - ^^^. . i. • - * • --b -----------------------_ ^^ - g ^^^ j hypersensitive, full-length response and only the background proteins , respectively, were tested for the expression and activity of HR as well. Large-scale expression and purification of the protein fragments was performed to determine the level of expression and the titre of HR activity (Table 3).

Table 3 Level of expression and titre of HR of the truncated proteins that promote the hypersensitive response (large-scale purification) The truncated proteins considered the most important in the promoter characterization of the hypersensitive response were chosen for large-scale expression. The positive control (promoter of full-length hypersensitive response) was expressed at a relatively high level at 3.7 mg / ml. All C-terminal proteins were expressed at relatively high levels of 2-5 mg / ml, except for fragment 343-403 as discussed at the beginning. The N-terminal fragments were expressed very well also; however, during the purification process, the protein precipitated and very little was re-solubilized. The concentrations in Table 3 reflect only the solubilized protein. The * B * aa »* internal fragments were expressed in the range of 2- 3.6 mg / ml. It was extremely difficult to determine the concentration of fragment 105-168 (it was suspected that the concentration was much higher than indicated), since the protein bands on the SDS gel were large, but poorly stained. The negative control had several background proteins, as expected, but not obviously the dominant protein induced. 10 Example 12 Induction of HR in Tobacco The positive control protein, full length, promoted HR only up to 5-7 μg / ml. The "protein" purified with imidazole (pET 28) negative control, which contained only previous proteins - promoted an HR response until the dilution of 1: 2, which decreased the sensitivity of the assay since the dilutions 1: 1 and 1 : 2 could not be used. This false HR was probably due to an affinity of the imidazole used in the purification process to bind to one or more of the background proteins, whereby they were not completely dialyzed. Imidazole at a concentration of approximately 60 mM did not promote a false HR response.

»J- .m ^ Mfc« »» MMwf- ^ ~? - ^? - 3-. -. • and * -, »atSiM.aBttf- A definitive domain spanning a small internal region of the protein from amino acid 137-180 (SEQ ID NO.23), only 44 amino acids, is identified as the smallest HR deminium. The other potential HR domain is thought to be located at the N-terminus of the protein from a. to. 1-104 (possibly amino acids 1-75) (SEQ ID NO.23). It was difficult to confirm or narrow the HR domain of the N-terminus due to the difficulties encountered in the purification of these protein fragments. (Protein fragments from the N-terminus had to be purified with urea since no proteins were recovered when the native purification process was used.) As a result, these proteins precipitated during the renaturation process and were difficult and almost impossible to put back into. solution, which made it difficult to run the proteins through the HR assay, since only the soluble protein is capable of promoting HR.The difficulty in narrowing the N-terminal HR domain was only made up of the fact that that the negative control promoted the false HR at low dilution levels, thereby reducing the sensitivity of the assay.Surprisingly, when the internal HR domain was cleaved between amino acids 168 and 169 (fragments 76-168 and 105-168) (SEQ ID NO: 23) the fragment lost its HR activity, which suggests that the HR activity of fragment 1-168 (SEQ ID NO.23) should not be attributed to the domain or internal HR, but rather to some other domain, which leads to the assumption that there probably was a second HR domain to be found in the N-terminal region of the protein. However, as discussed at the beginning, it was difficult to confirm this alleged. The C-terminus of the hypersensitive response promoter (amino acids 210-403 (SEQ ID NO.23)) did not contain an HR domain. This did not promote HR to a detectable level using the current HR test. Even the large C-terminal fragment of amino acid 169-403 (SEQ ID NO.23) did not promote HR even when it contained part of the internal HR domain. As stated above, the cleavage of the protein between amino acids 168 and 169 (SEQ ID NO 23) causes a loss of HR activity. Because some of the small cloned proteins with 61 amino acids or less were not expressed, several oligopeptides with 30 amino acids were synthesized to narrow the functional region of the internal HR domain. The oligopeptides were synthesized within the range of amino acids 121-179 (SEQ ID NO: 23). However, these oligos do not promote HR. It was not expected that there would be an HR from oligos 137-166, 121-150, and 25 137-156 (SEQ ID NO 23) since these fragments do not "¿?" • fc - • ~ t? B ^. "- • • - -HllilliÉliiriH contained the imperative amino acids 168 and 169 (SEQ ID NO.23) It was expected that oligo 150-179 (SEQ ID NO.23) could promote an HR It is possible that 30 amino acids is too small so that the protein promotes any activity, due to a lack of folding and, therefore, a lack of link or that during the synthesis of the peptides missing important amino acids (either in the process, or simply by the choice of which 30 amino acids synthesize) and, therefore, the fragments might not be able to promote HR.

Example 13 Induction of Increase in Plant Growth (PGE) C-terminal fragments increased tomato growth by 9% to 21%. N-terminal fragments increased tomato growth by 4% to 13%. The internal fragments increased the growth by 9% to 20%. Fragment 76-209 increased growth by 18% at a concentration of 60 μg / ml, but not at the typical 20 μg / ml. This was attributed to the imprecision of the quantification process (Table 4). -^^ &-á Table 4 * A height greater than 10% above the control with buffer was necessary to pass the PGE test. at »? i The oligopeptides increased the growth from 7.4% to 17.3% (Table 5).

Table 5 The data suggest that there is more than one PGE domain, although the C-terminal and internal domains seem to be dominant over the N-terminal domain, since the N-terminal fragments increased the growth the least amount.

Example 14 Induction of Acquired Systemic Resistance (SAR) All of the hypersensitive response promoter fragments tested to date appear to be 60% effective or higher, except for oligopeptide 137-156 (Tables 5 and 6). ? íT rtMñi Table 6 These data suggest that multiple SAR domains exist within the protein.

Example 15 Relationship Between HR, PGE and SAR It is clear that the hypersensitive response activity is separable from the activity of increasing the - ** ^ - »» "*»,, ^.? & ^^ plant growth C-terminal fragments clearly increase the growth of tomatoes by approximately 20% at a concentration of only 20 μg / ml, but these The same fragments were not able to promote HR in tobacco, even at higher concentrations than 200 μg / ml.The SAR activity also seems to be separable from the HR activity.This finding was highly significant for the future work on the transgenic applications of the Hypersensitive response promoter technology 10. Fragments that induce PGE and / or SAR but that do not promote HR will be imperative for this technology, since the constitutive expression of even low levels of an HR promoter can kill a plant. 15 Example 16 Fragments Not Promoting HR Derived from the Promoter of the Hypersensitive Response of Pseudomonas syringae 'pv. syringae, Induce Resistance in Tobacco to TMV and Promote Tomato Growth 20 To test whether fragments that do not promote HR derived from HrpZ, the hypersensitive response promoter of Pseudomonas syringae pv. syringae, are able or not to induce resistance against the disease, several constructions of 25 fragments and protein fragments expressed were i-hmmriiiTifi-r-tested for the promotion of HR and the induction of resistance against diseases in tobacco and the promotion of growth in tomatoes The following segments of hrpZ, the gene that codes for the promoter of the hypersensitive response of Pseudomonas syringae pv. syringae, were amplified by PCR using Pfu Turbo (Stratagene): The regions coding for amino acids 152-190, amino acids 152-294, amino acids 190-294, amino acids 301-341, and Hrpz of full length (amino acids 1-341) The DNA fragments were cloned into pCAL-n (Stratagene) to create the C-terminal fusion proteins for the calmodulin binding peptide. that the fusion protein could be 15 easily and gently purified on the calmodulin resin. The DNA was transformed into E. coli DH5a, and the correct clones were identified. The clones were then transferred to E. BLR DE3 coli for the expression of the protein. The bacteria were developed in the 20 Terrific Broth at a D062o of 0.8-1.0. The expression of the protein was then induced with IPTG and the bacteria were incubated for an additional 3 hours. All fragments of HrpZ were able to be expressed in this way. The fragments of amino acids 152-294 and 190-294 25 were chosen for the analysis and characterization later. It was expected that fragment 152-294 contained a domain that promoted HR, while fragment 190-294 contained no domain that promoted HR. The cultures were centrifuged, and the bacteria were resuspended in 40 ml of 10 mM Tris at pH 8.0. Twenty μl of antifoam and 40 μl of 200 mM PMSF were added, and the bacteria were sonicated to break the cells. The bacterial waste was removed by centrifugation, and the supernatant was placed in a water bath for 10 minutes. 10 minutes. The precipitate was removed by centrifugation and the supernatant, a crude protein preparation, was retained for testing. Fifteen μl of each supernatant were run on a gel and stained to determine if the protein 15 was present. It was estimated that approximately five times more of fragment 152-294 was present than fragment 190-294. Several dilutions of each preparation were infiltrated into tobacco leaves on two plants for the HR tests (Table 7). As shown in Table 7, the 20 fragment 152-194 promoted an HR, but fragment 190-294 did not.

Table 7 The results of the HR test of HrpZ fragments Fragment Hrpz Dilution of Fragment Preparation 1: 2 1: 5 1:25 1: 125 152-294 +, + b +, + +, + -, - 190-294 a The preparations were diluted with MilliQ water. b The results were indicated for each of the two plants. +, HR; -, without Hr.

Fragment preparations were then tested for the induction of TMV resistance and for growth enhancement. Due to the difference in the concentration of the HrpZ fragments, the preparation of 152-294 was diluted 40 times and the 190-294 preparation was diluted 8 times. The results showed that the fragment of 190-294 amino acids reduced the number of TMV lesions by 85% compared to the controls with buffer (Table 8). In contrast, the 152-294 amino acid fragment reduced the number of TMV lesions by only 55%. As also shown in Table 8, the plants treated with the 152-294 amino acid fragment developed 4.64% more than the plants treated with the t - * "- 'buffer, while plants treated with the 190-294 amino acid fragment developed 2.62% more than plants treated with buffer.

Table 8 HR test, TMV and PGE test results Fragment Promotion of TMV (% of PGE (%> shock absorber HrpZ HRefficiency) 13 ht) c 152-294 + 54.64 4.64 19C-294 - 85.25 2.62 a +, promotes HR in tobacco leaves; -, without HR in tobacco leaves. b% reduction in TMV lesions on non-sprayed tobacco leaf. c higher percentage of height than plants sprayed with shock absorber.

The results of these tests show that amino acids 152-190 appear to be involved in HR promotion because their withdrawal eliminated the ability to promote HR. Both preparations of fragments achieved control of the disease and increased growth. In this way, the ability to promote HR is not the determining factor for the reduction in TMV infection and the increase in growth.

Example 17 The Use of 13 Amino Acid Peptide Derived from Phytophthora megasperma Stimulates the Growth of Tomato Seedlings The parsley leaves develop a typical resistance reaction against the soybean pathogen, Phytoph thora megasperma comprising the death of hypersensitive cells, the activation of defense-related genes, and the phytoalexin formulation. Several years ago, a 42 kDa glycoprotein promoter was purified from the fungal culture filtrate of Phytophthora megasperma (Parker et al., "An Extra? Ellular Glycoprotein from Phytophthora megasperma f.sp. gl'ycinea Elicits Phytoalexin Synthesis in Cultured Parsley Cells and Protoplasts, "Mol. Plant Microbe Interact 4: 19-27 (1991), which is incorporated by reference herein). Then, a 13 amino acid oligopeptide was identified within the 42 kDa glycoprotein. The 13 amino acid peptide appeared to have biological activity similar to that of the full-length glycoprotein (42 kDa). It is sufficient to promote a complete defense response in parsley cells that includes influxes of H + / Ca2 +, effluxes of K + / C1", the production of active oxygen, induction of the SAR gene, and the accumulation of the phytoalexin compound (Nurnberger et al. , "High Affinity Binding of a Fungal Oligopeptide Elicitor to 5 Parsley Plasma Membranes Multiple Triggers Defense Response", Cell 78: 449-460 (1994), which is incorporated by reference herein to test whether the 13 amino acid peptide derived from the 42 kDa protein also increased the growth of the plant, 20 mg of the oligopeptide of Biosynthesis Corp. were synthesized. The synthesized sequence of the peptide is NH2-Val-Trp-Asn-Gln-Pro-Val-Arg-Gly-Phe- Lys-Val-Tyr-Glu-COOH (SEQ ID NO: 39) The synthesized peptide was resuspended in 10 ml of 5 mM potassium phosphate buffer and then diluted from 1 to 100 ng / ml with the same buffer Approximately 100 tomato seeds (variety, Marglo be) were immersed in 20 ml of the peptide solution overnight. The soaked seeds were planted in a 20 cm (8 inch) pot with 20 artificial soil. The seeds soaked in the buffer without the peptide were used as a control. After the seedlings emerged and the first two true leaves were fully expanded, the height of the tomato seedlings was recorded. The peptide was not able to promote HR in ^^^ ¡H ^ j ^ ------------ to -----------------. There is tobacco and other plants tested. However, this had a profound effect on the promotion of plant growth. Table 9 shows that the tomato seedlings treated with the peptide were increased 12.6% in height, 5 indicating that the fungal peptide derived from the 42 kDa glycoprotein can promote the growth of tomato seedlings. Prolonged studies showed that the peptide also had similar growth effect in other crops including tobacco. The effects of similar growth promotion were achieved by the plants sprayed with the peptide solution.

Table 9 Treatment Height of plants (cm) Average% of (cm) change Shock absorber 6.0 6.0 6.0 5.5 5.5 5.55 - 5.5 5.5 5.0 5.0 5.5 Peptide solution 6.5 6.0 6.5 6.5 6.5 6.25 12.6 (100 ng / ml) 6.0 6.0 6.0 6.0 6.5 15 Although the invention has been described in detail for purposes of illustration, it should be understood that such detail is solely for that purpose, and variations may be made therein by those of experience in the art. , ^^^ * ta *** ^ technique without departing from the spirit and scope of the invention, which is defined by the following reivifications.

It is noted that in relation to this date, the best method known to the applicant to carry out the aforementioned invention is that which is clear from the present description of the invention. j ^^^ ¿^ fc aaaJtfe? LIST OF SEQUENCES < 110 > Eden Bioscience Corporation < 120 > FRAGMENTS OF THE CTCR OF THE HYPERSENSITIVE RESPONSE THAT ARE ACTIVE, BUT NOT CAUSING A HYPERSENSITIVE RESPONSE < 130 > 21829/32 < 140 > < 141 > < 150 > 60 / 103,050 < 151 > 1998-10-05 < 160 > 39 < 170 > Patentln Ver. 2.0 < 210 > 1 < 211 > 31 < 212 > DNA < 213 > Erwinia anylovora < 400 > 1 gggaattcat atgagtctga atacaagtgg g 31 < 21C > 2 < 211 > 31 < 212 > DNA < 213 > Erwinia a ylovora < 40C? > 2 gggíiattcat atgggcggtg gcttaggcgg t 31 < 21 (l> 3 <213.> 29 <212!> DNA <21i> Erwinia aaylovora < 400 > 3 ggcutatgtc gaaegcgctg aacgatatg 29 < 210 > 4 < 21 > 31 < 2i: í > DNA < 2i: i > Erwinia am lovora < 40C »4 gggaiattcat atgttaggcg gttcgctgaa c 31 < 210 > 5 < 211 > 29 < 212: > DNA < 213 > Erwinia anylovora < 400 > 5 ggcaitatgct gaacacgctg ggctcgaaa 29 < 21C 6 < 211 > 29 < 212 > DNA < 213 > Erwinia anylovora < 40C > e ggca.tatgtc aacgtcccaa aacgacgat 29 < 210 > 7 < 211 > 27 < 212 > DNA < 213 > Erwinia asrylovora < 4O0 > 7 ggcatatgtc cacctcagac tccagcg 27 < 210 > 8 < 211 > 34 < 212 > DNA < 213 > Erwinia anrylovora < 4O0 > 8 gggaattcat atgcaaagcc tgtttggtga tggg 34 < 210 > 9 < 211 > 31 < 212 > DNA < 213 > Erwinia amylovora < 40C > 9 gggaattcat atgggtaatg gtctgagcaa g 31 < 21C > 10 < 211 > 31 < 212 > DNA < 213 > Erwinia a-nylovora < 400 10 gggauttcat atgaaagcgg gcattcaggc g 31 < 210 11 < 211 34 < 2 2 > DNA < 213: > Erwinia aunylovora < 400: > 11 gggaiittcat atgacaccag ccagtatgga gcag 34 < 210 > 12 < 211 > 31 < 212 > DNA < 213 > Erwinia aprylovora < 400 > 12 gcaagcttaa cagcccacca ccgcccatca t 31 < 210 > 13 < 211 > 31 < 212 > DNA < 213 > Erwinia amylovora < 400 > 13 gcaagcttaa ategttcagc gcgttcgaca g 31 < 210 > 14 < 211 > 34 < 212 > DNA < 213 > Erwinia amylovora < 400 > 14 gcaagcttaa tatctcgctg aacatcttca gcag 34 s < 210 > 15 < 211 > 30 < 212 > DNA < 213 > Erwinia amylovora < 400 > 15 gcaagcttaa ggtgccatct tgcccatcac 30 < 21C > 16 < 211 > 34 < 21I > DNA < 212 > Erwinia amylovora < 400a 16 gcaagettaa atcagtgact ccttttttat aggc 34 < 210 ?. 17 < 211 > 31 < 212 > DNA < 213: - Erwinia amylovora < 400 =. 17 gcaagcttaa caggcccgac agcgcatcag t 31 < 210 > 18 < 211: - 31 < 212: > DNA < 213 > Erwinia amylovora < 400: - 18 gcaagcttaa accgataccg gtacccacgg c 31 < 210 :. 19 < 211: > 34 < 212: > DNA < 213: > Erwinia a ylovora < 400 > 19 gcaagcttaa tccgtcgtca tctggcttgc tcag 34 < 210: > 20 < 211: > 25 < 212 DNA < 213: > Erwinia am lovora < 400 »20 gcaagcttaa gccgcgccca gcttg 25 < 210 > 21 < 211 > 338 < 212 > PRT < 213 > Erwinia chrysanthemi < 400 > 21 Met ln Zle Thr lie Lys Wing His Zle Gly Gly Asp Leu Gly Val Ser 1 5 10 15 Gly tißu Gly Wing Gln Gly Leu Lys Gly Leu Asn Wing Wing Being Ser 20 25 30 Leu Sly Ser Ser Val? ßp Lys Leu Ser Be Thr lie Aßp Lys Leu Thr 4 - ^ jjfc 35 40 45 Ser? Leu Thr Ser Met Met Met Phe Gly Gly? the Leu? the Gln Gly Leu 50 55 60 Gly? the Being Ser Lys Gly Leu Gly Met Ser? sn Gln Leu Gly Gln Ser 65 70 75 80 Phe Gly? Sn Gly? The Gln Gly? The Ser? Sn Leu Leu Ser Val Pro Lys 85 90 95 Being Gly Gly? Sp? The Leu Ser Lys Met Phe? Sp Lyß? The Leu? ßp? ßp 100 105 110 Leu Leu Gly His? Sp Thr Val Thr Lyß Leu Thr? Sn Gln Ser? ßn Gln 115 120 125 Leu? La ? ßn Ser Met Leu? sn? the Ser Gln Met Thr Gln Gly? sn Met 130 135 140? sn? the Phe Gly Ser Gly Val? ßn? sn? the Leu Ser Ser Xle Leu Gly 145 150 155 160? ßn Gly Leu Gly Gln Ser Met Ser Gly Pbe Ser Gln Pro Ser Leu Gly 165 170 175? The Gly Gly Leu Gln Gly Leu Ser Gly? The Gly? The Phe? ßn Gln Leu 180 185 190 Gly? Sn? The Zle Gly M? T Gly Val Gly Gln? Sn? La? La Leu Ser? La 195 200 205 Leu Ser? ßn Val Ser Thr Hi? Val? Sp Gly? Sn? ßn? Rg Hi? Phe Val 210 215 220? Sp Ly? G? ßp? Rg Gly Met? La Lys Glu Zle Gly Gln Phe Met? Sp 225 230 235 240 Gis Tyr Pro Glu Zle Phe Gly Lyß Pro Glu Tyr ßln Lyß? ßp Gly Trp 245 250 255 Being Ser Pro Lyß Thr? ßp? ßp Lys Sßr Trp? The Lyß? The Leu Ser Ly? 260 265 270 Pro? ßp? ßp? ßp Gly Met Thr Gly? The Ser Met? ßp Lyß Phe? Rg Gln 275 280 285? Met Gly Met Zle Lyß Ser? Val? Gly? ßp Thr Gly? ßn Thr 5 290 295 300 Asa Leu? ßn Leu? Rg Gly? The Gly Gly? The Ser Leu Gly Zle? ßp? The 30¡5 310 315 320? Val Val Gly? ßp Lyß lie? ßn Mßt Ser Leu Gly Lys Leu? 325 330 335 ? sn? < 210 > 22 < 211 > 2141 < 2 2 > DNA < 213 > Erwinia chrysanthemi < 4I) 0 > 22 cguttttacc cgggtgaacg tgctatgacc gacagcatca cggtattcga caccgttacg 60 ge tttatgg ccgcgatgaa ccggcatcag gcggcgcgct ggtcgccgca atccggcgtc 120 gai: ctggtat ttcagtttgg ggacaccggg cgtgaactca tgatgcagat tcagccgggg 180 cagcaatatc ccggcatgtt gcgcacgctg ctcgctcgtc gttatcagca ggcggcagag 240 tgcgatggct gccatctgtg cctgaacggc agcgatgtat tgatcctctg gtggccgctg 300 cc tcggatc ccggcagtta tccgcaggtg atcgaacgtt tgtttgaact ggcgggaatg 360 acgttgcegt cgctatccat agcaccgacg gcgcgtccgc agacagggaa cggacgcgcc 420 cgntcattaa gataaaggcg gcttttttta ttgcaaaacg gtaacggtga ggaaccgttt 480 caccgtcggc gtcactcagt aacaagtatc catcatgatg cctacatcgg gatcggcgtg 540 ggcatccgtt gcagatactt ttgcgaacac ctgacatgaa tgaggaaacg aaattatgca 600 aal: tacgatc aaagcgcaca tcggeggtga tttgggcgtc tccggtctgg ggctgggtgc 660 tcugggactg aaaggactga attccgcggc ttcatcgctg ggttccagcg tggataaact 720 g eagcacc atcgataagt tgacctccgc gctgacttcg atgatgtttg gcggcgcgct 780 ggcgcagggg ctgggcgcca gctcgaaggg gctggggatg agcaatcaac tgggccagtc 840 ttl: cggcaat ggcg cgcagg gtgcgagcaa cctgctatcc gtaccgaaat ccggcggcga 900 tgcgttgtca aaaatgtttg ataaagcgct ggacgatctg ctgggtcatg acaccgtgac 960 -caugctgact aaccagagca accaactggc taattcaatg ctgaacgcca gccagatgac 1020 ccagggtaat atgaatgcgt tcggcagcgg tgtgaacaac gcactgtcgt ccattctcgg 1080 ggccagtcga cancggtctc tgagtggctt ctctcagcct tctctggggg caggcggctt 1140 gcugggcctg agcggcgcgg gtgcattcaa ccagttgggt aatgccatcg gcatgggcgt 1200 gg gcagaat gctgcgctga gtgcgttgag taacgtcagc acccacgtag acggtaacaa 1260 cc ecacttt gtagataaag aagatcgcgg catggcgaaa gagatcggcc agtttatgga 1320 tcngtatccg gaaatattcg gtaaaccgga ataccagaaa gatggctgga gttcgccgaa 1380 gacggacgac aaatcctggg ctaaagcgct gagtaaaccg gatgatgacg gtatgaccgg 1440 cgocagcatg gacaaattcc gtcaggegat gggtatgatc aaaagcgcgg tggcgggtga 1500 taucggcaat accaacctga acctgcgtgg cgcgggcggt gcatcgctgg gtatcgatgc 1560 ggctgtcgtc ggcgataaaa tagccaacat gtcgctgggt aagctggcca acgcctgata 1620 gcctgataaa atetgtgctg gcggaaacga aaaaagagac ggggaagcct gtctcttttc 1680 ttuttatgcg gtttatgcgg ttacctggac cggttaatca tcgtcatcga tctggtacaa 1740 acgcacattt tcccgttcat tegcgtcgtt acgcgccaca atcgcgatgg catcttcctc 1800 gtcerctcaga ttgcgcggct gatggggaac gccgggtgga atatagagaa actcgccggc 1860 cagattggaga cacgtctgeg ataaatctgt gccgtaacgt gtttctatcc gcccctttag 1920 caga.tagatt gcggtttcgt aatcaacatg gtaatgcggt tccgcctgtg cgccggccgg 1980 gatcaccaca atattcatag aaagetgtet tgcacctacc gtatcgcggg agataccgac 2040 aaaatagggc agtttttgcg tggtatccgt ggggtgttcc ggcctgacaa tcttgagttg 2100 gt egtcatc atctttctcc atctgggcga cctgatcggt t 2141 <; 210 > 23 < 211 > 403 < 212 > PRT < 213 > Erwinia amylovora < 400 > 23 Met Ser Leu? ßn Thr Ser Gly Leu Gly? The Ser Thr M? T Gln Zl? S? R 1 5 10 15 Zle? Y Gly? The Gly Gly? ßn? ßn Gly Leu Leu Gly Thr Ser? Rg Gln 20 25 30? Sn? the Gly Leu Gly Gly? sn It? s the Leu Gly Leu Gly Gly Gly? sn 35 40 45 Gln? sn? sp Thr Val? ßn Gln Leu? the Gly Leu Leu Thr Gly Met Met 50 55 60 Met lüss Met Met Met Met Gly Gly Gly Gly Leu Met Gly Gly Gly Gly Leu 65 70 75 80 Gly Gly Gly Leu Gly? ßn Gly Leu Gly Gly Gly Gly Glu Gly Leu Gly Glu 85 90 95 Gly: C? ßu Ser? ßn? The Leu? ßn? Sp Met Leu Gly Gly Ser Leu? ßn Thr 100 105 110 Leu Gly Ser Lyß Gly Gly? ßn? ßn Thr Thr Ser Thr Thr? ßn Ser Pro 115 120 125 Leu? ßp Gln? The Leu Gly Zle? ßn Ser Thr Ser Gln? ßn ? ßp? ßp Sßr 130 135 140 Thr JSer Gly Thr? ßp Ser Thr Ser? ßp Ser Ser? ßp Pro Mßt Gln Gln 145 150 155 160 Leu Leu Lyß Met Phe Ser Glu Zle Mßt Gln Ser Leu Phe Gly? ßp Gly 165 170 175 Gln Jksp Gly Thr Gln Gly Sßr Ser Gly Gly Lyß Gln Pro Thr Glu 180 185 190 Gly Glu Gln? Sn? The Tyr Lys Lys Gly Val Thr? Sp? The Leu Ser Gly 195 200 205 Leu Met Gly? Sn Gly Leu Ser Gln Leu Leu Gly? ßn Gly Gly Leu Gly 210 215 220 Gly Gly Gln Gly Gly? ßn? the Gly Thr Gly Leu? ßp Gly Ser Ser Leu 225 230 235 240 Gly? Ly Lys Gly Leu Gln? Sn Leu S? R Gly Pro Val?? P Tyr Gln Gln 245 250 255 Leu Gly? ßn? The Val Gly Thr Gly Zle Gly Met Lyß? The Gly Zle Gln 260 265 270? The Leu? Sn? Sp Zle Gly Thr Hi? Rg Hi? Ser Ser Thr? Rg Ser Phe 275 280 285 Val? ßn Lyß Gly? ßp? Rg? The Met Wing Lyß Glu Zle Gly Gln Phe Met 290 295 300? Sp? Ln Tyr Pro Glu Val Phe Gly Lys Pro Gln Tyr Gln Ly? Gly Pro 305 310 315 320 Gly Without Glu Val Lyß Thr? Sp? ßp Lyß Ser Trp? The Lyß? The Leu Ser 325 330 335 Lys Pro? ßp? Sp? Sp Gly Met Thr Pro? Ser Met Glu Gln Phe? ßn 340 345 350 Lyß? The Lyß Gly Met Zle Ly?? Rg Pro Met? The Gly? ßp Thr Gly? ßn 355 360 365 s Gly ? ßn Leu Gln? the? rg Gly? the Gly Gly Ser Ser Leu Gly Zle? ßp 370 375 380? the Met Met? the Gly? ßp? the Zle? ßn? ßn Met? the Leu Gly Lyß Leu 385 390 395 400 Gly? La? < 210 > 24 < 211 > 1288 < 212 > DNA < 213 > Erwinia amylovora < 400 > 24 aagctteggc atggcacgtt tgaccgttgg gtcggcaggg tacgtttgaa ttattcataa 60 gaggnatacg ttatgagtct gaa acaagt gggctgggag cgtcaacgat gcaaatttct 120 atcggcggtg cgggcggaaa taacgggttg ctgggtacca gtcgccagaa tgctgggttg 180 ggtggcaatt ctgcactggg gctgggcggc ggtaatcaaa atgataccgt caatcagctg 240 gctggcttac tcaccggcat gatgatgatg atgagcatga tgggcggtgg tgggctgatg 300 ggcggtggct taggcggtgg cttaggtaat ggcttgggtg gctcaggtgg cctgggcgaa 360 gtcga GGAC acgcgctgaa cgatatgtta ggcggttcgc tgaacacgct gggctcgaaa 420 caaca ggeg ataccacttc aacaacaaat tccccgctgg accaggcgct gggtattaac 480 tcaacgtccc aaaacgacga ttccacctec ggcacagatt ccacetcaga ctccagcgac 540 ccgatgcagc agctgctgaa gatgttcagc gagataatgc aaagcctgtt tggtgatggg 600 caagatggca cccagggcag ttcctctggg ggcaagcagc cgaccgaagg cgagcagaac 660 gcctataaaa aaggagtcac tgatgcgctg tcgggcctga tgggtaatgg tctgagccag 720 ctccttggca acgggggact gggaggtggt cagggcggta atgctggcac gggtcttgac 780 tgggcggcaa ggttcgtcgc agggctgcaa aacctgagcg ggecggtgga ctaccagcag 840 ttaggtaacg ccgtgg GTAC cggtatcggt atgaaagcgg gcattcaggc gctgaatgat 900 atcggtacgc acaggcaeag ttcaacccgt tctttcgtca ataaaggcga tcgggcgatg 960 gcgaaggaaa tcggtcagtt catggaccag tatcctgagg tgtttggcaa gccgcagtac 1020 cgggtcagga cagaaaggcc ggtgaaaacc gatgacaaat catgggcaaa agcactgagc 1080 aagccagatg acgacggaat gacaccagcc agtatggagc agttcaacaa agccaagggc 1140 Atgal: caaaa ggcccatggc gggtgatacc ggcaacggca acctgcaggc acgcggtgcc 1200 ggtggttett cgctgggtat tgatgccatg atggccggtg atgccattaa caatatggca 1260 cttggcaagc tgggcgcggc ttaagctt 1288 < 210 > 25 < 211 > 1344 < 212 > DNA < 213 > Erwinia amylovora < 400 > 25 atgtsaattc ttacgcttaa caacaatacc tcgtcctcgc cgggtctgtt ccagtccggg 60 ggggacaacg ggcttggtgg tcataatgca aattctgcgt tggggcaaca acccatcgat 120 cggcaaacca ttgagcaaat ggctcaatta ttggeggaac tgttaaagtc aetgctatcg 180 ccacaatcag gtaatgcggc aaccggagcc ggtggcaatg accagactac aggagttggt 240 aacgctggcg gcctgaacgg acgaaaaggc acagcaggaa ccactccgca gtctgacagt 300 cagaacatgc tgagtgagat gggcaacaac gggetggatc aggccatcac gcccgatggc 360 cagggcggcg ggcagatcgg cgataatcct ttactgaaag gcttattgca ccatgetgaa 420 cgcatgatgg acggccaaag cgatcagttt ggccaacctg gtacgggcaa caacagtgcc 480 tettccggta cttcttcatc tggcggttcc ccttttaacg atctatcagg ggggaaggcc 540 ccttccggca actccecttc eggcaactac tctcccgtca gtaccttctc acccccatcc 600 acgccaacgt eccctacctc accgcttgat ttcccttctt ctcccaccaa agcagccggg 660 ggcagcaegc cggtaaccga tcatcctgac cctgttggta gcgcgggcat cggggccgga 720 aattcggtgg ccttcaccag cgccggcgct aatcagacgg tgctgcatga caccattacc 780 gtgaaagcgg gtcaggtgtt tgatggcaaa ggacaaacet tcaccgccgg ttcagaatta 840 ggcgatggcg gccagt ctga aaaccagaaa ccgetgttta tactggaaga cggtgccagc 900 ctgaaaaacg tcaccatggg cgacgacggg gcggatggta ttcatcttta cggtgatgcc 960 aaaa.tagaca atctgeacgt caccaacgtg ggtgaggacg cgattaccgt taagccaaac 1020 gg &g ^ g »j« > • '-..-..- ,, ,, .- aaaaatccca agcgcgggca cgttgaaatc actaacagtt ccttcgagca cgcctctgac 1080 aagatcctgc agctgaatgc cgatactaac ctgagcgttg acaacgtgaa ggccaaagac 1140 tttggtaett ttgtacgcac taacggcggt caacagggta actgggatct gaatctgagc 1200 catatcageg cagaagaegg taagttctcg ttcgttaaaa gcgatagcga ggggctaaac 1260 gtcaatacca gtgatatctc actgggtgat gttgaaaacc actacaaagt gccgatgtcc 1320 gccaacctga aggtggctga atga 1344 < 210 > 26 < 211 > 447 < 212 > PRT < 213 > Erwinia amylovora < 400 > 26 Met Ser Zle Leu Thr Leu? ßn? ßn? ßn Thr Ser Ser Ser Pro Gly Leu 1 5 10 15 Phe Sin Ser Gly? Sp? ßn Gly Leu Gly Gly Hi?? Sn? La? Sn Ser 20 25 30? Leu Gly Gln Gln Pro Zle? Sp? Rg Gln Thr Zle Glu Gln Met? The 35 40 45 Gln Leu Leu? The Glu Leu Leu Lys Ser Leu Leu Ser Pro Gln Ser Gly 50 55 60? ßn? The? Thr Gly? the Gly Gly? ßn? ßp Gln Thr Thr Gly Val Gly 65 70 75 80? ßn Wing Gly Gly Leu? ßn Gly? rg Lys Gly Thr? the Gly Thr Thr Pro 85 90 95 Gln Ser? sp Ser Gln? sn Mßt Leu Ser Glu Met Gly? ßn? ßn Gly Leu 100 105 110? ßp Gln? The Zle Thr Pro? ßp Gly Gln Gly Gly Gly Gln Zle Gly? ßp 115 120 125? Sn Pro Leu Leu Lyß? The Met Leu Lyß Leu Zle? the? rg Met Met? ßp 130 135 140 Gly Gln Ser? sp Gln Phe Gly Gln Pro Gly Thr Gly? ßn? ßn Ser? la 145 150 155 160 Ser Ser Gly Thr Ser Ser Ser Gly Gly Ser Pro Phe? sn? sp Leu Ser 165 170 175 Gly Gly Lys the Pro Sßr Gly? Sn Ser Pro Ser Gly? ßn Tyr Ser Pro 180 185 190 10 Val Ser Thr Phe Ser Pro Pro Ser Thr Pro Thr Ser Pr or Thr Ser Pro 195 200 205 Leu? sp Phe Pro Ser Ser Thr Lys? the? the Gly Gly Ser Thr Pro 210 215 220 Val Thr? sp Hi? Pro? ßp Pro Val Gly Ser? the Gly Zle Gly? the Gly 225 230 235 240? Sn Ser Val? The Phe Thr Ser? The Gly? The? Sn Gln Thr Val Leu Hi? 245 250 255? Sp Thr Zle Thr Val Lys? The Gly Gln Val Phe? ßp Gly Lys Gly Gln 260 265 270 Thr Phe Thr? La Gly Ser Glu Leu Gly? Sp Gly Gly Gln Ser Glu? ßn 275 280 285 Gln Lyß Pro Leu Phe Zle Leu Glu? Sp Gly? The Ser Leu Lys? Sn Val 290 295 300 Thr Met Gly? ßp? ßp Gly? La? ßp Gly Zle Hiß Leu Tyr Gly? ßp? La 305 310 315 320 Lyß Zle? Sp? Sn Leu His Val Thr? Sn Val Gly Glu? Sp? La Zle Thr 325 330 335 Val Lys Pro? Sn Ser? La Gly Lyß Lyß Ser His Val Glu Zle Thr? Sn 340 345 350 Ser Ser Phe Glu His? La Ser? ßp Lyß Zle Leu Gln Leu? ßn? La? ßp 355 360 365 Thr? ßn Leu Ser Val? Sp? ßn Val Lys? The Lys? ßp Phe Gly Thr Phe 370 375 380 Val? Rg Thr? ßn Gly Gly Gln Gln Gly? Sn Trp? ßp Leu? ßn Leu Ser 385 390 395 400 Hiß Zle Ser? Glu? ßp Gly Lyß Phe Ser Phe Val Lyß Ser? ßp Ser 405 410 415 Glu Gly Leu? ßn Val? Sn Thr Ser? ßp Zle Ser Leu Gly? ßp Val Glu 420 425 430? ßn Hi? Tyr Ly? Val Pro Met Ser? La? ßn Leu Ly? Val? Glu 435 440 445 11 < 210 > 27 < 211 > 5517 < 212 > DNA < 213 > Erwinia aaylovora < 400 > 27 atggaattaa aatcactggg aactgaacac aaggcggcag tacacacagc ggcgcacaac 60 cctgtggggc atggtgttgc cttacagcag ggcagcagca gcagcagccc gcaaaatgcc 120 gct catcat tggcggcaga aggcaaaaat cgtgggaaaa tgccgagaat tcaccagcca 180 tctactgcgg ctgatggtat cagcgctgct caccagcaaa agaaatcctt cagtctcagg 240 ggcrgtttgg ggacgaaaaa attttccaga tcggcaccgc agggccagcc aggtaccacc 300 cacagcaaag gggcaacatt gcgcgatctg ctggcgcggg acgacggcga aacgcagcat 360 gag cggccg cgccagatgc ggcgcgtttg acccgttcgg gcggcgtcaa acgccgcaat 420 atg acgaca tggccgggcg gccaatggtg aaaggtggca taaggtacca gcggcgaaga 480 aacggcatca acgcagcaaa gctgaacaat tttggccaga tgcgccaaac gatgttgagc 540 aaaiitggctc acccggcttc agccaacgcc ggcgatcgcc tgcagcattc accgccgcac 600 gccaccacga atcccgggta aatcaaggaa gaaccggttg gctccaccag caaggcaaca 660 acg cccacg cagacagagt ggaaatcgct caggaagatg attccagcaa acgacagcga 720 ctgcatcaac agcggctggc gcgcgaacgg gaaaatccac cgcagccgcc caaactcggc 780 gttgecacac cgattagcgc caggtttcag cccaaactga ctgcggttgc ggaaagcgtc 840 ct tgagggga cagataccac gcagtcaccc cttaagccgc aatcaatgct gaaaggaagt 900 ggagccgggg taaegccgct ggcggtaacg ctggataaag gcaagttgca gctggcaccg 960 gataatccac ccgcgctcaa tacgttgttg aagcagacat tgggtaaaga cacccagcac 1020 tatctggcgc accatgccag cagcgacggt agccagcatc tgctgctgga caacaaaggc 1080 cacctgtttg atatcaaaag cacegccacc agctatageg tgetgeacaa cagccacccc 1140 ggtgagataa agggcaagct ggcgcaggcg ggtactggct cegtcagcgt agacggtaaa 1200 agcggcaaga tctcgctggg gagcggtacg caaagtcaca acaaaacaat gctaagccaa 1260 cegggggaag cgcaccgttc cttattaacc ggeatttggc agcatcctgc tggcgcagcg 1320 cggecgcagg gcgagtcaat ccgcctgcat gacgacaaaa ttcatatcct gcatccggag 1380 ctgggcgtat ggcaatctgc ggataaagat acecacagcc agctgtctcg ceaggcagac 1440 ggtaagctet atgcgctgaa agacaaccgt accctgcaaa aeetctecga taataaatcc 1500 tca aaaagc tggtegataa aatcaaatcg tattccgttg atcagcgggg gcaggtggcg 1560 atcctgacgg atactcccgg ccgccataag atgagtatta tgccctcgct ggatgcttcc 1620 ccggagagcc atatttccct cagcctgcat tttgccgatg cccaccaggg gttattgcac 1680 gggaagtcgg agettgaggc acaatctgtc gcgateagcc atgggcgact ggttgtggcc 1740 gatagcgaag gcaagctgtt tagcgccgcc attccgaagc aaggggatgg aaacgaactg 1800 aaaatgaaag ccatgectca gcatgcgctc gatgaacatt ttggtcatga ccaccagatt 1860 tcttjgatttt tccatgacga ccacggccag cttaatgcgc tggtgaaaaa taacttcagg 1920 cagcagcatg cctgcccgtt gggtaacgat catcagtttc accccggctg gaacctgact 1980 gatgcgctgg ttategacaa tcagctgggg ctgeatcata ccaatcctga aecgcatgag 2040 attcttgata tggggcattt aggcagcctg gcgttacagg agggcaagct tcactatttt 2100 gaccagctga ecaaagggtg gactggcgcg gagtcagatt gtaagcagct gaaaaaaggc 2160 ctggatggag cagcttatct actgaaagac ggtgaagtga aacgcctgaa ta ttaatcag 2220 agcacctcet ctatcaagca cggaacggaa aacgtttttt cgctgccgca tgtgegcaat 2280 aaaccggagc cgggagatgc cctgcaaggg ctgaataaag acgataaggc ccaggccatg 2340 gcggtgattg gggtaaataa atacetggcg ctgacggaaa aaggggacat tcgctccttc 2400 12 '^^^? ^, ^ .. -. . . .. . .... -. ,. . . ^ rt | to . shits AAAAC ccggcaccca geagttggag cggccggcac aaactctcag ccgcgaaggt 2460 atcagcggcg aactgaaaga catteatgtc gaccacaagc agaacctgta tgccttgace 2520 aggtgtttca cacgngggag tcagccgcgt gaagcctggc agaatggtgc cgaaagcagc 2580 AGCT gcaca aactggcgtt gccacagagt gaaagtaagc taaaaagtct ggacatgagc 2640 aaeegattgc catgiigcaca cacctttgaa gaeggtagcc ageatcaget gaaggctggc 2700 ggctergcacg cctatgcggc acctgaacgc gggccgctgg cggtgggtac cagcggttca 2760 caaacicgtct ttaaccgact aatgcagggg gtgaaaggca aggtgatccc aggcagcggg 2820 ttgaeggtta agctctcggc tcagacgggg ggaatgaccg gcgccgaagg gcgcaaggtc 2880 Agca? rtaaat tttccgaaag gatccgcgcc tatgcgttca acccaacaat gtccaegccg 2940 egacegatta aaaatgctgc ttatgecaca cagcacggct ggcaggggcg tgaggggttg 3000 aagcegttgt aegagatgea gggagcgctg attaaacaac tggatgcgca taacgttcgt 3060 cataeicgcgc eacagecaga tttgcagagc aaactggaaa ctctggattt aggcgaacat 3120 ggcgaagaat tgettaaega catgaagcgc ttccgcgacg aactggagca gagtgcaacc 3180 cgttcggtga ccgttttagg tcaacatcag ggagtgctaa aaagcaacgg tgaaatcaat 3240 a gcgnattta agccatcgcc cggcaaggcg ttggtccaga gctttaacgt caatcgctct 3300 ggtciiggatc taagcaagtc actgcaacag gcagtacatg ccacgccgcc atccgcagag 3360 agtaaiactgc aatecatget ggggcacttt gtcagtgccg gggtggatat gagtcatcag 3420 aagggcgaga tcccgctggg ccgceagcgc gatcegaatg ataaaaccgc actgaccaaa 3480 tcgcgtttaa ttttagatac cgtgaccatc ggtgaactgc atgaactggc cgataaggcg 3540 aaactggtat ctgaccataa acccgatgcc gatcagataa aacagctgcg ccagcagttc 3600 gataegctgc gtgaaaagcg gtatgagagc aatccggtga ageattacae cgatatgggc 3660 ttcacccata ataaggcgct ggaagcaaac tatgatgcgg tcaaagcctt tatcaatgee 3720 tttaj.gaaag agcaccacgg cgtcaatctg accacgcgta ccgtactgga atcacagggc 3780 agtgcggagc tggcgaagaa gctcaagaat acgetgttgt ccetggacag tggtgaaagt cttca 3840 ATGA gccggtcata tggcgggggc gtcagcaetg tctttgtgcc taccettage 3900 cagttccggt aagaaiggtgc gatcecegga gccggcatca cgctggatcg cgcctataac 3960 ctgagcttca gtcgtaceag cggcggattg aacgtcagtt ttggccgcga cggcggggtg 4020 agtggtaaca tcatggtcgc taecggccat gatgtgatgc cctatatgac cggtaagaaa 4080 acc acrtgcag gtaacgccag tgactggttg agcgcaaaac ataaaatcag cccggacttg 4140 cgtateggcg ctgctgtgag tggcaccctg caaggaacgc tacaaaacag cctgaagttt 4200 aagctgacag aggatgagct gcctggcttt atccatggct tgacgcatgg cacgttgacc 4260 tgttgcaaaa ccggaagaac ggggatcgaa catcagatga agcagggcag caaactgacg 4320 TTTA cgtcg atacctcggc aaatctggat ctgcgtgccg gtatcaatct gaacgaagac 4380 ggcagtaaac caaatggtgt cactgcccgt gtttctgccg ggctaagtgc atcggcaaac 4440 ctggccgccg gctcgcgtga acgcagcacc acctctggcc agtttggcag cacgacttcg 4500 gccagcaata accgcccaac cttcctcaac ggggtcggcg cgggtgctaa cctgacggct 4560 gctttagggg ttgcccattc atetaegeat gaagggaaac cggtcgggat cttcccggca 4620 ctega TTTA ccaatgtttc ggcagcgctg gcgctggata accgtacctc acagagtatc 4680 agcctggaat tgaagcgcgc ggagccggtg accagcaacg atatcagega gttgacctcc 4740 gggaa ACGC aacactttaa ggatagcgcc aeaacgaaga tgcttgccgc tctcaaagag 4800 ttagatgacg ctaagcccgc tgaacaactg catattttac ageageattt cagtgcaaaa 4860 gatg cgtcg gtgatgaacg ctacgaggcg gtgcgeaacc tgaaaaaact ggtgatacgt 4920 caacaggc tg cggacagcca cagcatggaa ttaggatctg ccagtcacag cacgacctac 4980 aatantctgt cgagaataaa taatgacggc attgtcgagc tgetacacaa acatttcgat 5040 gcggcattac cagcaagcag tgccaaacgt tgatgaataa cttggtgaaa cgatccggca 5100 ttattaagea ctganagata gctgcaaagt acgccgttca gcagcgccag cgtgtcgatg 5160 gagc gaaag atggtctgcg tgagcagacg gaaaaagcaa tactggacgg taaggtcggt 5220 cgtguagaag tgggagtact tttecaggat cgtaacaact tgcgtgttaa atcggtcagc 5280 13 gtcíigtcagt ccgtcagcaa aagcgaaggc ttcaataccc cagcgctgtt actggggacg 5340 agciiacagcg ctgctatgag catggagcgc aacatcggaa ccattaattt taaatacggc 5400 cagcratcaga acaccccacg gcgatttacc ctggagggtg gaatagctca ggctaatccg 5460 caggtcgcat ctgcgcttac tgatttgaag aaggaagggc tggaaatgaa gagctaa 5517 < 21C »28 < 211 > 1838 < 212 > PRT < 213 > > Erwinia amylovora < 40C > 28 Met Glu Leu Lys Ser Leu Gly Thr Glu His Lyß Ala Ala Val Hiß Thr 1 5 10 15? The? His? Sn Pro Val Gly Hi? Gly Val? The Leu Gln Gln Gly Being 20 25 30 Being Being Pro Gln? ßn??? Being? Le? Glu Gly 35 40 45 Lyß? ßn? Rg Gly Lyß Met Pro? Rg Zle Hi? Gln Pro Being Thr? La? 50 55 60? ßp Gly Zlß Ser? La? His Gln Gln Lys Lys S? R Phe Ser Leu? Rg 65 70 75 80 Gly Cys Leu Gly Thr Ly? Ly? Phe Ser? Rg Ser? The Pro Gln Gly Gln 85 90 95 Pro Gly Thr Thr His Ser Lyß Gly? The Thr Leu? Rg? ßp Leu Leu? The 100 105 110? Rg? ßp? ßp Gly Glu Thr Gln His Glu? La? The Pro? Sp? The? 115 120 125? rg Leu Thr? rg Ser Gly Gly Val Lyß? rg? rg? ßn Met? ßp? ßp Met 130 135 140? the Gly? rg Pro Met Val Lys Gly Gly Ser Gly Glu? ßp Lyß Val Pro 145 150 155 160 Thr Gln Gln Lyß? Rg Hiß Gln Leu? ßn? ßn Phe Gly Gln Met? Rg Gln 165 170 175 Thr Met Leu Ser Lyß Met? Hi? Pro? Ser? La? ßn? Gly? ßp 180 185 190? Rg Leu Gln Hiß Ser Pro Pro Hiß Zle Pro Gly Ser Hiß Hiß Glu Zle 14 195 200 205 Lyß Glu Glu Pro Val Gly Ser Tbr Ser Lys? Thr Tbr? His? 210 215 220? ßp? Rg Val Glu Zle? La Gln Glu Aßp? ßp? ßp Ser Glu Pbe Gln Gln 225 230 235 240 Leu Hiß Gln Gln? Rg Leu? La? Rg Glu? Rg Glu? ßn Pro Pro Gln Pro 245 250 255 Pro Lyß Leu Gly Val? The Thr Pro Zle Ser? La? Rg Phe Gln Pro Lyß 260 265 270 Leu Thr? Val? Glu Ser Val Leu Glu Gly Thr? Sp Thr Tbr Gln 275 280 285 Ser:? Ro Leu Lys Pro Gln Ser Met Leu Lys Gly Ser Gly? the Gly Val .290 295 300 Thr l? ro Leu? the Val Thr Leu? sp Lyß Gly Lyß Leu Gln Leu? the Pro 305 310 315 320? ßp Jlßn Pro Pro? the Leu? ßn Tbr Leu Leu Lyß Gln Tbr Leu Gly Lyß 325 330 335? ßp? Hr Gln Hi? Tyr Leu? The His Hi?? Ser? ßp Gly Ser Gln 340 345 350 Hi? Leu Leu? Sp? ßn Ly? Gly His Leu Phe? ßp Zle Ly? Ser Thr 355 360 365 ? the "hr Ser Tyr Ser Val Leu Hiß? ßn Ser Hiß Pro Gly Glu Zle Lyß and: 70 375 380 Gly Lyß Leu? the Gln? the Gly Thr Gly Ser Val Ser Val? ßp Gly Lyß 385 390 395 400 Sßr Cily Lyß Zlß Ser Leu Gly Sßr Gly Thr Gln Sßr Hiß? ßn Lyß Thr 405 410 415 Met Leu Ser Gln Pro Gly Glu? La Hi ß? rg Ser Leu Leu Thr Gly Zle 420 425 430 Trp Clin His Pro? Gly? la? rg Pro Gln Gly Glu Ser Zle? rg 435 440 445 Leu His? ßp? ßp Lyß Zle Hi? Zle Leu His Pro Glu Leu Gly Val Trp 15 < ^ ®m 450 455 460 Gln Ser? La? ßp Lyß? ßp Thr Hiß Ser Gln Leu Ser? Rg Gln? La? Sp 465 470 475 480 Gly Lyß Leu Tyr? Leu Lyß? ßp AB ?. ? rg Thr Leu Gln? sn Leu Ser 485 490 495? ßp? ßn Lys Sßr Ser Glu Lyß Leu Val? ßp Lyß Zle Lyß Ser Tyr Ser 500 505 510 Val? sp Gln? rg Gly Gln Val? the Zle Leu Thr? ßp Tbr Pro Gly? Rg 515 520 525 His Lys Met Ser Zle Met Pro Ser Leu? Sp? The Ser Pro Glu Ser His 530 535 540 Zle Ser Leu Ser Leu Hi? Phe? La? ßp? His Gln Gly Leu Hi? 545 550 555 560 Gly Lyß Ser Glu Leu Glu? Gln Ser Val? La Zle Ser His Gly? Rg 565 570 575 Leu Val Val? La? Sp Ser Glu Gly Lys Leu Phe Ser? La? La Zle Pro 580 585 590 Lyß Gln Gly ? ßp Gly? sn Glu Leu Lys Met Lyß? the Met Pro Gln His 595 600 605? the Leu? sp Glu Hiß Phe Gly Hiß Asp Hiß Gln Zle Ser Gly Phe Phe 610 615 620 His ft.sp? ßp Hiß Gly Gln Leu ? ßn? the Leu Val Lyß? sn? ßn Phe? rg 625 630 635 640 Gln Sin Hiß? the Cyß Pro Leu Gly? ßn? ßp Hiß Gln Phß Hiß Pro Gly 645 650 655 Trp? ßn Leu Thr? sp? la Leu Val Zle? ßp? ßn Gln Leu Gly Leu Hiß 660 665 670 Hiß Thr? ßn Pro Glu Pro Hi? Glu Zle Leu? Sp Met Gly H is Leu Gly 675 680 685 Being Leu? the Leu Gln Glu Gly Lyß Leu Hiß Tyr Phe? ßp ßln Leu Tbr? S90 695 700 Lyß (Sly Trp Thr Gly? Glu Ser? ßp Cyß Lyß Gln Leu Lyß Lyß Gly 16 70! J 710 715 720 Leu? Sp Gly? The? Tyr Lau Leu Lys? Sp Gly Glu Val Ly? Rg Leu 725 730 735 Asn Zle? ßn Gln Ser Thr Ser Ser Zle Lys Hiß Gly Thr Glu? Sn Val 740 745 750 Phe Ser Leu Pro His Val? Rg? Sn Lys Pro Glu Pro Gly? ßp? The Leu 755 760 765 Gl »Gly Leu? Sn Lyß? Sp? ßp Lys? The Gln? The Met? The Val Zle Gly 770 775 780 Val? ßn Lyß Tyr Leu? The Leu Tbr ßlu Lys Gly? Sp Zle? Rg Ser Phe 78! > 790 795 800 Gil. Zle Lyß Pro Gly Thr Gln Gln Leu Glu? Rg Pro? Gln Thr Leu 805 810 815 Ser? Rg Glu Gly Zle Ser Gly Glu Leu Lys? Sp Zle Hi? Val? ßp Hi? 820 825 830 Lyii Gln? ßn Leu Tyr? The Leu Thr Hi? Glu Gly Glu Val Phe His Gln 835 840 845 Pro? Rg Glu? The Trp ßln? ßn ßly? the Glu Being Ser Trp His Lys 850 855 860 Leu? the Leu Pro Gln Ser ßlu Ser Lyß Leu Lyß Ser Leu? ßp Met Ser 86 !! 870 875 880 Hill ßlu Hiß Lyß Pro Zle? Thr Phe ßlu? ßp Gly Ser Gln Hiß ßln _, 885 890 895 Leu Lyß? The Gly Gly Trp His? The Tyr? The? The Pro Glu? Rg Gly Pro 900 905 910 Leu? The Val ßly Thr Ser ßly Ser ßln Thr Val Phe? ßn? Rg Leu Met 915 920 925 ßln ßly Val Lys ßly Lys Val Zle Pro ßly Ser Gly Leu Thr Val Lyß 930 935 940 Leu Ser? Gln Thr ßly ßly Met Thr ßly? Glu Gly? rg Lyß Val 94! ¡950 955 960 Being Ser Lys Phe Ser ßlu? Rg Zle? Rg? The Tyr? The Phe? Sn Pro Thr 17 965 970 975 Met. Be Thr Pro? Rg Pro Zle Lyß? Sn? La? The Tyr? The Tbr ßln His 980 985 990 ßlj- Trp ßln ßly? Rg ßlu ßly Leu Lys Pro Leu Tyr Glu Met Gln Gly 995 1000 1005? The Leu Zle Lys ßln Leu? ßp? The Hiß? ßn Val? Rg Hi?? Sn? The Pro 1010 1015 1020 ßln Pro? ßp Leu Gln Ser Lys Leu Glu Thr Leu? ßp Leu Gly Glu Hiß 1025 1030 1035 1040 Gly? The Glu Leu Leu? ßn? ßp Met Lyß? Rg Phe? Rg? Sp Glu Leu ßlu 1045 1050 1055"ßln Ser? The Thr? Rg Ser Val Thr Val Leu Gly Gln His Gln ßly Val 1060 1065 1070 Leu Lyß Ser ? ßn Gly Glu Zle? ßn Ser ßlu Phe Lyß Pro Ser Pro ßly 1075 1080 1085 Lyß? the Leu Val ßln Ser Phe? ßn Val? an? rg Ser ßly ßln? ßp Leu 1090 1095 1100 Ser Lyß Ser Leu ßln ßln? la Val Hiß? The Thr Pro Pro Ser? La Glu 1105 1110 1115 1120 Ser Lyß Leu Gln Ser Met Leu ßly Hiß Phe Val Ser? La Gly Val? ßp 1125 1130 1135 Met Ser Hiß ßln Lyß Gly Glu Zle Pro Leu ßly? Rg Gln? Rg? ßp Pro, 1140 1145 1150? ßn? ßp Lyß Thr? The Leu Thr Lyß Ser? Rg Leu Zl? Leu? ßp Thr Val 1155 1160 1165 Thr Zle ßly Glu Leu Hiß Glu Leu? La? ßp Lyß? Lyß Leu Val Ser .1170 1175 1180? ßp Hiß Lyß Pro? ßp? La? ßp ßln Zle Lyß ßln Leu? Rg ßln Gln Phe 118.5 1190 1195 1200? ßp Thr Leu? rg Glu Lyß? rg Tyr Glu Ser? ßn Pro Val Lyß Hiß Tyr 1205 1210 1215 Tbr? ßp Mßt ßly Pbe Thr Hiß? ßn Lyß? The Leu ßlu? The? Sn Tyr? ßp 18 1220 1225 1230? The Val Lys? The Phe Zle? Sn? The Phe Lys Lys Glu His Hi? Gly Val 1235 1240 1245? ßn Leu Thr Thr? rg Thr Val Leu Glu Ser Gln ßly Ser? the Glu Leu i: > 50 1255 1260 - the Lys Lys Leu Lys? Sn Thr Leu Leu Ser Leu? ßp Ser Gly Glu Ser 1265 1270 1275 1280 Met Sßr Phe Ser? Rg Ser Tyr Gly Gly Gly Val Sßr Thr Val Phe Val 1285 1290 1295 Pro "hr Leu Ser Lys Lys Val Val Pro Pro Val Zle Pro ßly Ala ßly 1300 1305 1310 Zle" hr Leu Asp? Rg? The Tyr? ßn Leu Ser Phe Ser? Rg Thr Ser ßly 1315 1320 1325 Gly Leu? ßn Val Ser Phe Gly? Rg? ßp ßly Gly Val Ser ßly? Sn Zle 1330 1335 1340 Met Val? Thr ßly Hiß? ßp Val Mßt Pro Tyr Mßt Thr ßly Lyß Lyß 1345 1350 1355 1360 Thr 3ßr? The ßly? ßn? The Ser? ßp Trp Leu Ser? The Lyß Hiß Lyß Zle 1365 1370 1375 Ser:? Ro? ßp Leu? Rg Zle ßly? The Wing Val Ser ßly Thr Leu Gln Gly 1380 1385 1390 Thr Leu Gln? ßn Ser Leu Lyß Phe Lyß Leu Thr Glu? ßp ßlu Leu Pro 1395 1400 1405 Gly Phe lie His Gly Leu Thr His Gly Thr Leu Thr Pro? Glu Leu 1410 1415 1420 Leu Without Lyß Gly Zle Glu His ßln Met Lyß Gln Gly Ser Lys Leu Thr 1425 1430 1435 1440 Phe Ser Val? ßp Thr Ser? La? Sn Leu? ßp Leu? Rg? La ßly Zle? ßn 1445 1450 1455 Leu? ßn ßlu? ßp ßly Ser Lyß Pro? ßn ßly Val Thr? La? Rg Val Ser 1460 1465 1470? The ßly Leu Ser? The?? Sn Leu? The? ßly Ser? Rg ßlu? Rg 19 1475 1480 1485 Ser "hr Tbr Ser ßly ßln Phe ßly Ser Thr Tbr Ser? The Ser? ßn? ßn 1490 1495 1500? Rg Pro Thr Phe Leu? Sn ßly Val Gly? La ßly? La? Sn Leu Thr? La 1505 1510 1515 1520? The Leu Gly Val? The His Being Ser Thr His Glu Gly Ly? Pro Val ßly 1525 1530 1535 Zle Phe Pro? The Phe Thr Ser Thr? Sn Val Ser? The? The Leu? The Leu 1540 1545 1550? Sp? Sn ? rg Thr Ser ßln Ser Zle Ser Leu ßlu Leu Lys? rg? the ßlu 1555 1560 1565 Pro Val Tbr Ser Aßn? ßp Zle Ser Glu Leu Tbr Ser Thr Leu ßly Lys 1570 1575 1580 His Fhe Lyß? ßp Ser? the Thr Thr Lys Met Leu? The? Leu Lyß ßlu 1585 1590 1595 1600 Leu? ßp? Sp? The Lyß Pro? The ßlu Gln Leu Hi? Zle Leu Gln Gln Hi? 1605 1610 1615 Phe Ser? La Ly?? P Val Val Gly? ßp Glu ? rg Tyr Glu? the Val? rg 1620 1625 1630? ßn leu Lys Lys Leu Val Zle? rg Gln Gln? la? la Aßp Ser Hi ß Sßr 1635 1640 1645 Met Glu Leu ßly Ser? the Being His Ser Thr Thr Tyr Aßn? ßn Leu Ser 1650 1655 1660? rg Zle? sn? sn? sp ßly Zle Val Glu Leu Leu His Lys Hiß Phe? ßp 1665 1670 1675 1680? The? The Leu Pro? The Being? The Lyß? Rg Leu Gly Glu Met Met? Sn 1685 1690 1695? ßn? ßp Pro? The Leu Lyß? ßp Xle Zle Lyß ßln Leu ßln Ser Thr Pro 1700 1705 1710 Pbe Be Ser? The Ser Val Val Met Met Glu Leu Lyß? ßp Gly Leu? Rg ßlu 1715 1720 1725 Gln Tbr ßlu Lyß? The Zle Leu? ßp ßly Lyß Val ßly? Rg ßlu ßlu Val 20 1730 1735 1740 Gly Val Leu Pbe Gln? Sp? Rg? ßn? Sn Leu? Rg Val Lys Ser Val Ser 1745 1750 1755 1760 Val, 3rd Gln Ser Val Ser Lyß Ser Glu Gly Phe? ßn Thr Pro? La Leu 1765 1770 1775 Leu Leu Gly Thr Ser? ßn Ser? La? The Met Ser Met Glu? Rg? ßn Zle 1780 1785 1790 Gly Thr Zle? ßn Phe Lyß Tyr Gly Gln? ßp Gln? ßn Thr Pro? Rg? Rg 1795 1800 1805 Phe Thr Leu ßlu Gly ßly Zle? Gln? La? ßn Pro ßln Val? Ser 1B10 1815 1820? Leu Tbr? ßp Leu Lyß Lys ßlu Gly Leu ßlu Met Lyß Ser 1825 1830 1835 < 210 > 29 < 211 > 420 < 212 > DN? < 213 > Erwinia amylovora < 400 > 29 atgacatcgt cacagcageg ggttgaaagg tttttacagt atttctccgc cgggtgtaaa 60 atctgaaaga acgcccatac gecctgtata cggggtgtgc acgaacaaga tgaggaggcg 120 aagtaccgca gcggtgctgg acacagcgac agcctgttae taeactgecg aatcattgag 180 gctgacccac aaaettcaat aaecetgtat tcgatgctat taeagetgaa ttttgaaatg 240 gcggccatge gcggctgttg gctggcgctg gatgaactgc acaacgtgcg tttatgtttt 300 cagcagtcgc tggagcatet ggatgaagca agttttagcg atatcgttag cggcttcatc 360 gaacatgcgg cagaagtgcg tgagtatata gcgcaattag acgagagtag cgeggcataa 420 < 210 > 30 < 211 > 139 < 2i :: > PRT < 213 > > Erwinia amylovora < 40 (l> 30 Met Thr Ser Ser ßln ßln? Rg Val Glu? Rg Phe Leu Gln Tyr Phe Ser 1 5 10 15? The ßly Cys Lys Thr Pro Zle Hi? Leu Ly?? P? Sly Val Cy? The Leu 20 25 30 Tyr? ßn ßlu ßln? ßp ßlu ßlu? The? Val Leu ßlu Val Pro ßln Hiß 21 35 40 45 Se ::? Sp Ser Leu Leu Leu Hiß Cyß? Rg Xle Xle Glu? La? Sp Pro Gln 50 55 60 Thi: Ser Xle Thr Leu Tyr Ser Met Leu Leu Gln Leu? ßn Phe ßlu Met 6! »70 75 80? Ln? The Met? Rg Gly Cys Trp Leu? The Leu? ßp Glu Leu Hi? ßn Val 85 90 95 Argr Leu CYSS Phe ßln ßln Ser Leu Glu Hiss Leu? SSPs Glu? Ser Phe 100 105 110 Sex? SSPs Zle Val Ser Gly Phe Zle SSLU Hiss? The? Glu Val? Rg Glu 115 120 125 Tyr Xle? Gln Leu ? ßp Glu Ser Ser? la? la 130 135 < 210 > 31 < 21L > 341 < 212 > PRT < 21.3 > Pseudomonas syringae < 400 > 31 Met Gln Ser Leu Ser Leu? ßn Ser Ser Leu ßln Thr Pro? La Met 1 5 10 15? Leu Val Leu Val? Rg Pro ßlu? La ßlu Thr Thr ßly Ser Tbr Ser 20 25 30 Ser Lyß? La Leu ßln SSLU Val Val Val Lyss Leu Glu SSLU Leu Met - '35 40 45 rg SSNs Gly ßln Leu SSP SSPs Ser Ser Pro Leu ßly Lyss Leu Leu la 50 55 60 Lyss Being Met la la???????? ßp Gly Lyß? the ßly ßly ßly Zle Glu? ßp Val 65 70 75 80 Zle? La? The Leu? ßp Lyß Leu Zle Hiß ßlu Lyß Leu Gly? ßp? ßn Pbe 85 90 95 Gly? The Ser? La? ßp Ser? The Ser Gly Tbr ßly Gln Gln? ßp Leu Mßt 100 105 lio 22 Thr Gln Val Leu? SSN Gly Leu? The Lyss Ser Met Leu? Sp? Sp Leu Leu 115 120 125 Thr Lys Gln? Sp Gly ßly Tbr Ser Phe Ser Glu? SSPs? Sp Het Pro Met 130 135 140 Leu? SSN Lyss Zle? The Gln Phe Met? Sp? Sp? Sn Pro? La ßln Phe Pro 145 150 155 160 Lyß Pro? ßp Ser Gly Ser Trp Val? Sn Glu Leu Ly? Glu? Sp? Sn Phe 165 170 175 Leu? SSPs Gly? SSPs Glu Thr? The? Phe? Rg Ser? Leu? SSP Xle Xle 180 185 190 Gly Gln Gln Leu ßly? SSN ßln ßln Ser? SSPs? The ßly Ser Leu? The ßly 195 200 205 Thr Gly Gly ßly Leu ßly Thr Pro Ser Ser Phe Ser? SSN? SSN Ser Ser 210 215 220 Val Met ßly? sp Pro Leu Xle? SSP? the? SSN Thr ßly Pro ßly? SSP Ser 225 230 235 240 ßly Assn Thr? rg ßly ßlu? the ßly Gln Leu Zle ßly ßlu Leu Zle? ßp 245 250 255? rg Gly Leu ßln Ser Val Leu? the Gly Gly Gly Leu Gly Thr Pro Val 260 265 270? ßn Thr Pro ßln Tbr ßly Thr Ser? la? ßn Gly Gly Gln Ser? Gln 275 280 285? ßp Leu? ßp Gln Leu Leu ßly ßly Leu Leu Leu Lyß ßly Leu ßlu? la, '290 295 300 Thr Leu Lyß? ßp? the Gly Gln Thr Gly Thr? ßp Val Gln Ser Sßr? La 305 310 315 320? La (Without Zle? The Thr Leu Leu Val Ser Thr Leu Leu ßln ßly Thr? Rg 325 330 335? An? <? N? L??? The? 340 < 210: > 32 < 211: > 1026 23 < 212 > DNA < 213 > Pßeudoaonaß syringae < 400 > 32 atgcagagtc tcagtcttaa cagcagctcg ctgcaaaccc cggcaatggc ccttgtcctg 60 gtacgtectg aagcegagac gactggcagt aggcgcttca acgtcgagca ggaagttgtc 120 gtgaagctgg ccgaggaaet gatgcgcaat ggtcaactcg acgacagctc gccattggga 180 aaact TTGG ccaagtcgat ggccgcagat ggcaaggcgg gcggcggtat tgaggatgtc 240 atcgctgcgc tggacaagct gatccatgaa aagctcggtg acaaettcgg cgcgtctgcg 300 gacagegcct cgggtaccgg acagcaggac ctgatgactc aggtgctcaa tggcctggcc 360 aagtegatgc tcgatgatct tetgaccaag caggatggcg ggacaagctt ctccgaagac 420 tgctgaacaa gatatgccga gatcgcgcag ttcatggatg acaatcccgc acagtttccc 480 aagccggact cgggctcctg ggtgaacgaa eteaaggaag acaacttcct tgatggcgac 540 gaaacggctg egttccgttc ggcactcgac atcattggcc agcaactggg taatcagcag 600 agtgacgctg gcagtctggc agggacgggt ggaggtctgg gcactccgag cagtttttcc 660 aacaactegt ccgtgatggg tgatccgetg atcgacgcca ataccggtcc cggtgacagc 720 ggcaaeaccc gtggtgaagc ggggeaaetg atcggcgagc ttatcgaccg tggcctgcaa 780 tcggtüttgg ccggtggtgg cccgtaaaca actgggcaca ccccgcagac cggtacgtcg 840 gcgaacggcg gaeagt ccgc tcaggatctt gatcagttgc tgggcggctt gctgctcaag 900 ggcct gagg caacgctcaa ggatgccggg caaacaggca ccgacgtgca gtcgagcgct 960 gcgcaiíatcg ccaccttgct ggtcagtacg ctgctgcaag gcacccgeaa tcaggctgca 1020 gcctg.i 1026 < 210 > 33 < 211 > 1729 < 212 > DNA < 213 > Pseudomonas syringae < 400 > 33 tccacitcgc tgattttgaa attggcagat tcatagaaac gttcaggtgt ggaaatcagg 60 ctgagtegcgc agatttcgtt gataagggtg tggtactggt cattgttggt catttcaagg 120 cctct agtg cggtgcggag caataccagt cttcctgctg gcgtgtgcac actgagtcgc 180 aggcaeaggc atttcagttc cttgcgttgg ttgggcatat aaaaaaagga acttttaaaa 240 acagt caat gagatgecgg caaaacggga accggtcgct gcgctttgcc actcacttcg 300 agcaai jetea accccaaaca tccacatccc tatcgaacgg acagcgatac ggccacttgc 360 tctgg caaac cetggagctg gcgtcggtec aattgcccac ttagcgaggt aacgcagcat 420 gagc tcggc atcacacccc ggccgeaaca gaeeaccacg ccactcgatt tttcggcgct 480 aageg caag agtectcaac caaacacgtt cggcgagcag aaeactcagc aagcgatcga 540 TGCA eccga ctgttgttcg gcagcgacac acagaaagac gtcaacttcg gcacgcccga 600 eagcaccgtc cagaatccgc aggacgccag caageccaac gacagecagt ceaacategc 660 agtgcattga taaattgate tcatgtcgtt gctgcagatg etcaccaact ccaataaaaa 720 gcaggicacc aatcaggaac agectgatag ccaggetect ttceagaaca acggcgggct 780 cggtaaaceg tcggcegata gcgggggcgg cggtacaccg gatgcgacag gtggcggcgg 840 cggtg tacg ccaagcgeaa caggcggtgg cggcggtgat actccgaccg caacaggcgg 900 tggcggcagc ggtggcggcg gcacacceac tgcaacaggt ggeggcagcg gtggcacacc 960 cactgcaaca ggeggtggeg agggtggcgt aacaccgcaa atcactccgc agttggccaa 1020 ccetaiftcegt acctcaggta ctggctcggt gtcggacacc gcaggttcta cegagcaagc 1080 cggca »gatc aatgtggtga aagacaccat caaggtcggc gctggegaag tctttgacgg 1140 24 - ^ j ^ s - ^^ ccacggcgca accttcactg cegaeaaatc tatgggtaac ggagaccagg gcgaaaatca 1200 gaagcccatg ttcgagctgg ctgaaggcgc tacgttgaag aatgtgaacc tgggtgagaa 1260 cgaergtcgat ggcatccacg tgaaagceaa aaacgctcag gaagtcacca ttgacaacgt gca 1320 GECCAG aacgtcggtg aagacctgat tacggtcaaa ggcgagggag gcgcagcggt 1380 cac aatctg aacateaaga acagcagtgc caaaggtgca gacgacaagg ttgtecagct 1440 actcaettga caacgccaac aaatcgacaa cttcaaggcc gaegatttcg gcacgatggt 1500 tcg accaac ggtggcaage agtttgatga catgagcate gagctgaacg gcatcgaagc 1560 taaccacggc aagttcgccc tggtgaaaag cgacagtgac gatctgaagc tggcaacggg 1620 caacatcgcc atgaccgacg tcaaacacgc ctacgataaa acccaggcat cgacccaaca 1680 caccgagett tgaatccaga caagtagctt gaaaaaaggg ggtggaetc 1729 < 210 > 34 < 2U > 424 < 212 > PRT < 213 > Pseudomonas syringae < 400 > 34 Met Ser Zle ßly Xle Thr Pro? Rg Pro ßln ßln Thr Thr Thr Pro Leu 1 5 10 15? Sp Phß Ser? The Leu Ser Gly Lyß Ser Pro ßln Pro? ßn Thr Phe Gly 20 25 30 Glu Sin? ßn Thr ßln ßln? the Xle? ßp Pro Ser? the Leu Leu Phe Gly 35 40 45 Ser? ßp Thr Gln Lyß? ßp Val? ßn Phe Gly Thr Pro? ßp Ser Thr Val 50 55 60 Gln? ßn Pro ßln? sp? the Ser Lys Pro? Sn Aßp Ser ßln Ser? ßn Xle 65 70 75 80? The Lyß Leu Xle Ser? The Leu Xle Met Ser Leu Leu ßln Met Leu Thr and 85 90 95? ßn Would it? ßn Lyß Lyß ßln? Sp Thr? ßn Gln ßlu ßln Pro? ßp Ser Gln 100 105 110? Pro Phe Gln? ßn? ßn Gly ßly Leu Gly Thr Pro Ser? la? ßp Ser 115 120 125 Gly Gly ßly Gly Thr Pro? ßp? Thr Gly Gly Gly Gly Gly? ßp Thr: .30 135 140 Pro ílßr? Thr ßly ßly ßly ßly ßly? ßp Thr Pro Thr? Thr ßly 145 150 155 160 Gly Cily ßly Ser ßly ßly ßly ßly Thr Pro Thr? Thr ßly ßly ßly 25 ^ j ^? ^? ^ e ^^? ^ s? 165 170 175 Ser ßly ßly Thr Pro Thr? Tbr ßly ßly Gly ßlu ßly Gly Val Thr 180 185 190 Pro ßln Xle Tbr Pro ßln Leu? La? ßn Pro? ßn? Rg Thr Ser ßly Tbr 195 200 205 Gly Ser Val Ser ? ßp Tbr? the Gly Ser Thr Glu Gln? the Gly Lyß Xle 210 215 220? sn Val Val Lyß? ßp Thr Xle Lys Val ßly? the ßly ßlu Val Phe? ßp 225 230 235 240 ßly Hiß ßly? the Tbr Phe Thr ? ßp Lyß Ser Met ßly? ßn ßly? ßp 245 250 255 Gln ßly ßlu? ßn ßln Lyß Pro Met Phe Glu Leu? ßlu Gly? Thr 260 265 270 Leu Lyß? ßn Val? sn Leu Gly Glu? sn Glu Val? Sp Gly Xle His Val 275 280 285 Lys? Lys? ßn? Gln ßlu Val Thr Xle? ßp? ßn Val Hiß? Gln 290 295 300? ßn Val ßly ßlu? ßp Leu Xle Thr Val Lyß ßly ßlu ßly Gly? la? la 305 310 315 320 Val Thr? ßn Leu? ßn Xle Lyß? sn Ser Ser? Lyß Gly? Asp? sp 325 330 335 Lyß Val Val ßln Leu? ßn? la? ßn Thr Hiß Leu Lys Xle? ßp? ßn Phe 340 345 350 Lyß .Ma? Sp? ßp Phe ßly Thr Met Val? Rg Thr? ßn Gly Gly L yß Gln 355 360 365 Phe? ßp? ßp Met Ser Zle ßlu Leu? ßn ßly Zle ßlu? la? ßn Hiß Gly: J70 375 380 Lyß Phe? the Leu Val Lyß Ser? sp Ser? ßp? sp Leu Lyß Leu? la Thr 385 390 395 400 Gly lian Zle? The Met Thr? ßp Val Lyß Hiß? The Tyr? ßp Lyß Thr Gln 405 410 415? The Tbr Gln His Thr Glu Leu 26 jm ^^^ - t »». 420 < 2] .0 > 35 < 211 > 344 < 2 2 > PRT < 213 > Pseudomonaß solanacearum < 220 > < 2 > Description of unknown organism: Pseudcmonas solanacearan < 400 > 35 Het Ser Val ßly? ßn Zle ßln Ser Pro Ser? ßn Leu Pro ßly Leu ßln 1 5 10 15? Sn Leu? ßn Leu? ßn Thr? ßn Thr? ßn Ser Gln Gln Ser ßly ßln Ser 20 25 30 Val ßln? ßp Leu Zle Lyß Gln Val Glu Lyß? ßp Zle Leu? ßn Zle Zle 35 40 45? the? the Leu Val Gln Lyß? the? the ßln Ser? the ßly ßly? ßn Thr ßly 50 55 60? ßn Thr ßly? ßn The Pro? la Lys? ßp ßly? ßn? the? sn? la ßly? the 65 70 75 80? ßn? sp Pro Ser Lys? ßn? sp Pro Ser Lys Ser ßln? the Pro ßln Ser 85 90 95? ? s Lyß Thr ßly? ßn Val? ßp? ßp? la? ßn? ßn ßln? ßp Pro Met 100 105 110 Gln? the Leu Met ßln Leu Leu Glu? sp Leu Val Lys Leu Leu Lyß? the 115 120 125? Leu Hiß Met ßln ßln Pro ßly ßly? ßn? ßp Lys Gly? Sn Gly Val 130 135 140 Gly Gly? The? ßn ßly? The Lyß Gly? The Gly Gly Gln Gly Gly Leu? The 145 150 155 160 Glu? The Leu ßln Glu Zle Glu ßln Zle Leu? The ßln Leu ßly ßly ßly 165 170 175 Gly? The ßly? The Gly Gly? The Gly Gly Gly Val Gly Gly? The Gly Gly 180 185 190 27? The? ßp Gly Gly Sßr Gly? The ßly ßly? The Gly Gly? The? ßn Gly? The 195 200 205 ? ßp Gly Gly? ßn Gly Val? ßn Gly? ßn Gln? la? ßn ßly Pro Gln? ßn 210 215 220? the Gly? ßp Val? sn ßly? the? ßn ßly? the? ßp? sp ßly Ser ßlu? sp 225 230 235 240 Gln Gly Gly Leu Thr Gly Val Leu Gln Lyß Leu Met Lyß Zle Leu? ßn 245 250 255? The Leu Val ßln Met Met ßln ßln ßly ßly Leu ßly ßly ßly ßn ßln 260 265 270? The ßln ßly ßly Ser Lys ßly? the ßly? ßn? the Ser Pro? the Ser ßly 275 280 285? the? sn Pro Gly? the? sn ßln Pro ßly Ser? the Asp Asp Gln Ser Ser 290 295 300 Gly Gln Asn? ßn Leu ßln Ser ßln Zle Met ? ßp Val Val Lyß ßlu Val 305 310 315 320 Val ßln Zle Leu ßln ßln Met Leu? The? Gln? ßn ßly ßly Ser ßln 325 330 335 Gln Ser Thr Ser Thr ßln Pro Met 340 < 21D > 36 < 21L > 1035 < 212 > DNA < 2U > Pßeudomonaß ßola-nacearum < 40 > 36 atgtcagtcg gaaacatcca gagcccgtcg aacctcccgg gtctgcagaa cctgaacctc 60 eeaacagcca aacaecaaca gcaatcgggc cagtcegtgc aagacctgat caagcaggtc 120 gag & aggaca teetcaacat categeagcc etcgtgcaga aggcegcaea gtcggegggc 180 ggciacaccg gtaacaccgg caacgcgecg gcgaaggacg gcaatgceaa cgcgggcgec 240 gcaagaaega aacgacccga cccgagcaag agccaggctc egcagtcggc eaacaagaee 300 ggcaacgtcg acgacgccaa caaccaggat ecgatgeaag cgetgatgea getgctggaa 360 agctgctgaa gaestggtga ggeggccctg cacatgcagc agcccggcgg caatgacaag 420 ggcaaeggcg tgggcggtgc caacggcgcc aagggtgccg gcggccaggg eggcctggcc 480 gaagcgctge aggagatcga gcagatcctc gcecagctcg gcggcggegg tgetggcgec 540 ggcggcgcgg gtggcggtgt cggcggtget ggtggcgcgg atggcggctc cggtgcgggt 600 28 * " '* • GGC caggcg gtgcgaacgg cgccgacggc ggcaatggeg tgaacggcaa ccaggcgaac 660 ggcccgcaga acgcaggcga tgtcaaeggt gecaaeggcg cggatgaegg eagcgaagac 720 cag.jgcggcc tcaccggcgt gctgcaaaag ctgatgaaga tcctgaacgc gctggtgcag 780 atgitgcagc aaggcggeet cggcggcgge aaccaggegc agggcggetc gaagggtgcc 840 GGC acgcct cgccggctte cggcgcgaac ecgggcgcga aceagcccgg ttcggcggat 900 gat aatcgt ccggccagaa eaatetgcaa tcceagatca tggatgtggt gaaggaggtc 960 gtecagatec tgcagcagat gctggcggcg cagaacggcg gcagccagca gtccacctcg 1020 acgcagccga tgtaa 1035 < 21D > 37 < 21L > 26 < 21.2 > PRT < 213 > Xanthomonaß caapeßtrxß pv. glyeines < 400 > 37 Thr Leu Zle Glu Leu Met Xle Val Val? The Zle Zle? The Xle Leu? 1 5 10 15? The Xle? The Leu Pro? The Tyr ßln? ßp Tyr 20 25 < 210 > 38 < 211 > 20 < 212 > PRT < 213 Xanthomonas ca peßtriß pv. pelargonii < 400 > 38 Ser Ser ßln Gln Ser Pro Ser? La Gly Ser Glu Gln Gln Leu? ßp Gln 1 5 10 15 Leu Leu? La Het 20 < 210 > 39 < 211 > 13 < 212 > PRT < 213 > Phytophthora megaßperma < 400 > 39 Val Trp? ßn Gln Pro Val? Rg Gly Phe Ly? Val Tyr Glu 1 5 10 29

Claims (1)

104 CLAIMS Having described the invention as above, the content of the following claims is claimed as property: 1. An isolated fragment of a protein or polypeptide promoter of the hypersensitive response, wherein the protein or polypeptide promoter of the hypersensitive response characterized in that it is capable of promoting a hypersensitive response in non-host plants, and is characterized by a high content of glycine and substantially without cysteine, and where the fragment does not promote a hypersensitive response but induces increased growth, resistance to disease, or control of insects in plants. 2. An isolated fragment according to claim 1, characterized in that the protein or polypeptide promoting the hypersensitive response is derived from Erwinia, Pseudomonas, Xanthomonas, or Phyt oph thora. 3. An isolated fragment according to claim 2, characterized in that the protein or polypeptide promoter of the hypersensitive response is derived from Erwinia amylovora. . a ^ l i á 105 4. An isolated fragment according to claim 3, characterized in that the fragment is selected from the group consisting of a C-terminal fragment of the amino acid sequence of SEQ ID NO. 23, an N-terminal fragment of the amino acid sequence of SEQ ID NO. 23, and an internal fragment of the amino acid sequence of SEQ ID NO. 23. An isolated fragment according to claim 4, characterized in that the fragment is a The C-terminal fragment of the amino acid sequence of SEQ "D NO. 23" encompasses the following amino acids of SEQ ID No. 23: 169 and 403, 210 and 403, 267 and 403, or 343 and 403. 6. An isolated fragment according to claim 4, characterized in that the fragment is an N-terminal fragment of the amino acid sequence of SEQ ID NO 23. 23. An isolated fragment according to claim 4, characterized in that the fragment is a The internal fragment of the amino acid sequence of SEQ ID NO. 23 which covers the following amino acids of SEQ ID NC. 23: 105 and 179, 137 and 166, 121 and 150, or 137 and 156. 8. An isolated fragment according to claim 2, characterized in that the promoter of the 106 Hypersensitive response is derived from Pseudomonas syringae. 9. An isolated fragment according to claim 8, characterized in that the fragment contains amino acids 190 to 294 of SEQ ID NO. 31. A molecule isolated from DNA, characterized in that it encodes a fragment according to claim 1. 11. A DNA isolated molecule according to claim 10, characterized in that the protein or hypersensitive response promoter polypeptide is derived from Erwinia, Pseudomonas, Xanthomonas, or Phytophthora. 12. An isolated DNA molecule according to claim 11, characterized in that the hypersensitive response promoter protein or polypeptide is derived from Erwinia amylovora. 13. An isolated DNA molecule according to claim 12, characterized in that the fragment is selected from the group consisting of a C-terminal fragment of the amino acid sequence of SEQ ID NO. 23, an N-terminal fragment of the amino acid sequence of SEQ ID NO. 23, and an internal fragment of the amino acid sequence of SEQ ID NO. 2. 3. 'rfc M IiT1' * 107 14. An isolated DNA molecule according to claim 12, characterized in that the fragment is a C-terminal fragment ur of the amino acid sequence of SEQ ID NO. 23, which covers the following amino acids of SEQ ID NO. 23: 169 and 403, 210 and 403, 267 and 403 or 343 and 403. 15. An isolated DNA molecule according to claim 12, characterized in that the fragment is an N-terminal fragment of the amino acid sequence of SEQ. ID NO. 23. 16. An isolated molecule of DNA according to claim 12, characterized in that the fragment is an internal fragment of the amino acid sequence of SEQ ID NO. 23 which encompasses the following amino acids of SEQ ID NO. 23: 105 and 179, 137 and 166, 121 and 150, or 137 and 156. 17. An isolated DNA molecule according to claim 11, characterized in that the hypersensitive response promoter is derived from the Pseudomonas syringae. 18. An isolated DNA molecule according to claim 18, characterized in that the fragment contains amino acids 190 to 294 of SEQ ID NO. 31 108 19. An expression system, characterized in that it is transformed with a DNA molecule according to claim 10. 20. An expression system according to claim 19, characterized in that the molecule of DNA is in orientation in the proper sense and in the correct reading structure. 21. A host cell, characterized in that it is transformed with a DNA molecule according to claim 10. 22. A host cell according to claim 21, characterized in that the host cell is selected from the group consisting of a plant cell and a bacterial cell. 23. A host cell according to claim 21, characterized in that the DNA molecule is transformed with an expression system. 24. A transgenic plant, characterized in that it is transformed with the DNA molecule according to claim 10. 25. A transgenic plant according to claim 24, characterized in that the plant is selected from the group consisting of alfalfa, rice, wheat , barley, rye, cotton, sunflower, peanut, corn, potato, sweet potato, bean, peas, chicory, lettuce, endive, cabbage, 109 brussel sprouts, beets, chirivia, turnip, cauliflower, broccoli, radish, spinach, onion, garlic, eggplant, pepper, celery, carrot, chayote, pumpkin, zucchini, cucumber, apple, pear, melon, citrus, strawberry, grape, raspberry, pineapple, soybeans, tobacco, tomato, sorghum, and sugar cane. 26. A transgenic plant according to claim 24, characterized in that the plant is selected from the group consisting of Arabidopsis thaliana, Sain tpaulia, petunia, pelargonium, red shepherd, chrysanthemum, carnation, and zinnia. 27. A transgenic plant seed, characterized in that it is transformed with the DNA molecule according to claim 10. 28. A transgenic plant seed according to claim 27, characterized in that the seed of the plant is selected from the group that consists of alfalfa, rice, wheat, barley, rye, cotton, sunflower, peanut, corn, potato, sweet potato, peas, chicory, lettuce, endive, cabbage, brussel sprouts, beets, chirivia, turnip, cauliflower, broccoli, radish, spinach, onion, garlic, eggplant, pepper, celery, carrot, chayote, pumpkin, zucchini, cucumber, apple, pear, melon, citrus, strawberry, grape, raspberry, pineapple, soybean, tobacco, tomato, sorghum, and sugar cane. ^^^ ¡^^^ »^ * 110 29. A transgenic plant seed of confection with claim 27, characterized in that the plant seed is selected from the group consisting of Arabidopsis thaliana, Sain tpa ulia, petunia, pelargonium, red pastera, chrysanthemum, carnation, and zinia. 30. A method for imparting disease resistance to plants, the method characterized in that it comprises: the application of a fragment of a protein or polypeptide promoter of the hypersensitive response that promotes a hypersensitive response in non-host plants, whose fragment does not promote a response hypersensitive, in a non-infectious manner, to a plant or plant seed under effective conditions to impart resistance against the disease. 31. A method according to claim 30, characterized in that the plants are treated during said application. 32. A method according to claim 20, wherein the seeds of the plants are treated during the application, the method is further characterized because it comprises: the sowing of the seeds treated with the fragment of the hypersensitive response promoter, in soil natural or artificial and 111 the propagation of plants from the seeds planted in the soil. 33. A method for increasing the growth of plants, characterized in that it comprises: the application of a fragment of a protein or polypeptide that promotes the hypersensitive response that promotes a hypersensitive response in non-host plants, whose fragment does not promote a hypersensitive response, in a non-infectious way for a plant or plant seed, under conditions effective to increase the growth of the plant. 34. A method according to claim 33, characterized in that the plants are treated during said application. 35. A method according to claim 33, wherein the seeds of the plant are treated "during application, the method is characterized in that it comprises: the sowing of the seeds treated with the hypersensitive response promoter fragment, in the natural or artificial soil and the propagation of plants from seeds planted in the soil 36. A method for controlling insects for plants, characterized in that it comprises: 112 the application of a fragment of a protein or polypeptide promoter of the hypersensitive response that promotes a hypersensitive response in non-host plants, whose fragment does not promote a hypersensitive response, in a non-infectious manner for a plant or plant seed under effective conditions to control insects 37. A method according to claim 36, characterized in that the plants are treated during said application. 38. A method according to claim 36, wherein the seeds of plants are treated during application, the method is characterized in that it further comprises: sowing the seeds treated with the fragment of the hypersensitive response promoter, in the soil natural or artificial and the propagation of plants from the seeds planted in the soil. 39. A method for imparting disease resistance to plants, the method characterized in that it comprises: the provision of a transgenic plant or seed of a transgenic plant, transformed with a DNA molecule that encodes a fragment of a protein or polypeptide promoter of the hypersensitive response that 113 it promotes a hypersensitive response in non-host plants, whose fragment does not promote a hypersensitive response, and the development of the transgenic plant or of the transgenic plants produced from the seeds of transgenic plants, under conditions effective to impart resistance against the disease. 40. A method according to claim 39, characterized in that a transgenic plant is provided. 41. A method according to claim 39, characterized in that a transgenic plant seed is provided. 42. A method for increasing the growth of plants, characterized in that it comprises: the provision of a transgenic plant or a plant seed transformed with a DNA molecule which codes for a fragment of a protein or polypeptide promoter of the hypersensitive response, which it promotes a hypersensitive response in non-host plants, whose fragment does not promote a hypersensitive response, and the development of the transgenic plant or of the transgenic plants produced from the seeds of transgenic plants, under effective conditions to increase the growth of the plants. 114 43. A method according to claim 42, characterized in that a transgenic plant is provided. 44. A method according to claim 42, characterized in that a transgenic plant seed is provided. 45. A method for controlling insects for plants, characterized in that it comprises: the provision of a transgenic plant or seed of a transgenic plant transformed with a DNA molecule that codes for a fragment of a protein or polypeptide that promotes the hypersensitive response which promotes a hypersensitive response in non-host plants, whose fragment does not promote a hypersensitive response, and the development of the transgenic plant or of the transgenic plants produced from the seeds of transgenic plants under conditions effective to control insects. 46. A method according to claim 45, characterized in that a transgenic plant is provided. 47. A method according to claim 45, characterized in that a transgenic plant seed is provided. ^ * ^ * ^ ~ '- * - --.- »- > ..... ^ fc ^ 115 48. A method according to claim 30, characterized in that the protein or polypeptide promoting the hypersensitive response is derived from Erwinia, Pseudomonas, Xanthomonas, or Phytcphthora. 49. A method according to claim 48, characterized in that the fragment is: an N-terminal fragment of the amino acid sequence of SEQ ID NO. 2. 3; an internal fragment of the amino acid sequence of SEQ ID NO. 23 which encompasses the following amino acids of SEQ ID NO. 23: 105 and 179, 137 and 166, 121 and 150, or 137 and 156; a C-terminal fragment of the amino acid sequence of SEQ ID NO. 23 which encompasses the following amino acids of SEQ ID NO. 23: 169 and 403, 210 and 403, 267 and 403, or '343 and 403; a fragment comprising amino acids 190 to 294 of SEQ ID NO. 31; or a fragment comprising the amino acid sequence of SEQ ID NO. 39. 50. A method according to claim 33, characterized in that the protein or polypeptide promoter of the hypersensitive response is 116. derived from Erwinia, Pseudomonas, Xan thomonas or Phytophthora. 51. A method according to claim 50, characterized in that the fragment is: an N-terminal fragment of the amino acid sequence of SEQ ID NO. 2. 3; an internal fragment of the amino acid sequence of SEQ ID NO. 23 which encompasses the following amino acids of SEQ ID NO. 23: 105 and 179, 137 and 166, 121 and 150, or 137 and 156; a C-terminal fragment of the amino acid sequence of SEQ ID NO. 23 which encompasses the following amino acids of SEQ ID NO. 23: 169 and 403, 210 and 403, 267 and 403, or 343 and 403; a fragment comprising amino acids 190 to 294 of SEQ ID NO. 31; or a fragment comprising the amino acid sequence of SEQ ID NO. 39. 52. A method according to claim 36, characterized in that the protein or polypeptide promoting the hypersensitive response is derived from Erwinia, Pseudomonas, Xan thomonas, or Phytophthora. 53. A method according to claim 36, characterized in that the fragment is: 117 an N-terminal fragment of the amino acid sequence of SEQ ID NO. 2. 3; an internal fragment of the amino acid sequence of SEQ ID NO. 23 which encompasses the following amino acids of SEQ ID NO. 23: 105 and 179, 137 and 166, 121 and 150, or 137 and 156; a C-terminal fragment of the amino acid sequence of SEQ ID NO. 23 which encompasses the following amino acids of SEQ ID NO. 23: 169 and 403, 210 and 403, 267 and 403, or 343 and 403; a fragment comprising amino acids 190 to 294 of SEQ ID NO. 31; or a fragment comprising the amino acid sequence of SEQ ID NO. 39. 54. A method according to claim 39, characterized in that the protein or polypeptide promoting the hypersensitive response is derived from Erwinia, Pseudomonas, Xan thomonas, or Phytophthora. 55. A method according to claim 54, characterized in that the fragment is: an N-terminal fragment of the amino acid sequence of SEQ ID NO. 2. 3; an internal fragment of the amino acid sequence of SEQ ID NO. 23 which covers the following ,? a?., m é? 118 amino acids of SEQ ID NO. 23: 105 and 179, 137 and 166, 121 150, or 137 and 156; a C-terminal fragment of the aminocacid sequence of SEQ ID NO. 23 which covers the following 5 amincacidos of SEQ ID NO. 23: 169 and 403, 210 and 403, 267 and 403, or 343 and 403; a fragment comprising amino acids 190 to 294 of SEQ ID NO. 31; or a fragment comprising the sequence of 10 amino acids of SEQ ID NO. 39. 56. A method according to claim 42, characterized in that the protein or polypeptide promoting the hypersensitive response is derived from Erwinia, Pseudomonas, Xan thomonas, or Phytoph thora. 57. A method according to claim 56, characterized in that the fragment is: an N-terminal fragment of the amino acid sequence of SEQ ID NO. 2. 3; 20 an internal fragment of the amino acid sequence of SEQ ID NO. 23 which encompasses the following amino acids of SEQ ID NO. 23: 105 and 179, 137 and 166, 121 and 150, or 137 and 156; a C-terminal fragment of the 25 amino acid sequence of SEQ ID NO. 23 which covers the following g-a-lg-Í-tlliÍ ^ - ---------- L --- ..-- ^, ^ -_. . . . -. . , ..., ^^ v? &amp 119 amino acids of SEQ ID NO. 23: 169 and 403, 210 and 403, 267 and 403, or 343 and 403; a fragment comprising amino acids 190 to 294 of SEQ ID NO. 31; or a fragment comprising the amino acid sequence of SEQ ID NO. 39. 58. A method according to claim 45, characterized in that the protein or polypeptide promoting the hypersensitive response is derived from Erwinia, Pseudomonas s, Xan thomona s, or Phytoph thora. 59. A method according to claim 58, characterized in that the fragment is: an N-terminal fragment of the amino acid sequence of SEQ ID NO. 2. 3; an internal fragment of the amino acid sequence of SEQ ID NO. 23 which encompasses the following amino acids of SEQ ID NO. 23: 105 and 179, 137 and 166, 121 and 150, or 137 and 156; a C-terminal fragment of the amino acid sequence of SEQ ID NO. 23 which encompasses the following amino acids of SEQ ID NO. 23: 169 and 403, 210 and 403, 267 and 403, or 343 and 403; 120 a fragment comprising amino acids 190 to 294 of SEQ ID NO. 31; or a fragment comprising the amino acid sequence of SEQ ID NO. 39 ^ m ^^^^ g ^^ ^ ñ 121 J SUMMARY OF THE INVENTION The present invention is directed to isolated active fragments of a hypersensitive response promoter protein or polypeptide, which fragment does not promote a hypersensitive response in plants. Also described are the isolated DNA molecules, which code for such fragments. The isolated fragments of the proteins or polypeptides promoting the hypersensitive response according to the present invention and the isolated DNA molecules that encode them have the following activities: imparting resistance against diseases to plants, increasing the growth of plants, and / or control of insects on plants. This can be achieved by applying fragments of a hypersensitive response promoter in a non-infectious manner to plants or plant seeds under conditions effective to impart resistance against diseases, to increase plant growth, and / or to control insects on plants or plants developed from the seeds of plants. Alternatively, the transgenic plants or the seeds of plants transformed with a DNA molecule encoding the fragment can be provided, and the transgenic plants or plants resulting from the j "- 122 seeds of transgenic plants are developed under effective conditions to impart resistance against diseases, to increase the growth of the plants, and / or to control insects on the plants or plants developed from the seeds of plants.