UA92622C2 - Genes grg23 and grg51 conferring herbicide resistance - Google Patents

Abstract

An invention relates to the isolated nucleic acids, coding polynucleotides, conferring herbicide resistance or herbicide tolerance to bacteria, plants, plant cells, tissues and seeds. The nucleotide sequences of the invention can be used in DNA constructs or expression cassettes for transformation or expression in organisms, comprising microorganisms and plants. The composition also contains transformed bacteria, plants, plant cells, tissues, and seeds. In particular, the isolated polynucleotides are presented, coding polypeptides of resistance or tolerance towards glyphosate.

Description

The field of technology

The present invention discloses new genes encoding resistance to herbicides, which are applicable in plant biology, in the selection of agricultural crops and for plant cell cultures.

Prior art

M-phosphonomethylglycine, commonly called glyphosate, is an important agronomic chemical.

Glyphosate inhibits the enzyme that converts phosphoenolpyruvic acid (PEP) and 3-phosphoshikimic acid (5Z3P) to 5-enolpyruvyl-3-phosphoshikimic acid. Inhibition of this enzyme (5-enolpyruvylshikimate-3-phosphate synthase; referred to herein as "ERBRB5") destroys plant cells by shutting down the shikimate metabolic pathway, thus suppressing aromatic acid biosynthesis.

Since glyphosate herbicides inhibit the biosynthesis of aromatic amino acids, they not only destroy plant cells, but are also toxic to bacterial cells. Glyphosate inhibits many bacterial ERBR synthases and is thus toxic to these bacteria. However, certain bacterial synthases

ERBRs are highly resistant to glyphosate.

Plant cells resistant to glyphosate toxicity can be obtained by transforming plant cells to express glyphosate-resistant bacterial EPZR synthases. In particular, a bacterial gene from the CPA strain Adhorasiegisht isteiasiep5 was used to render plant cells resistant to herbicides after expression in plants. Mutated ERBR synthase from ST7 strain

Zaitopeiia liurpitigicht confers glyphosate resistance in bacterial cells and confers glyphosate resistance in plant cells (US Patents MoM 4,535,060; 4,769,061 and 5,094,945). However, there is a need for other herbicide resistance genes.

The kinetic activity of ERBRO can be assessed by measuring the release of phosphate.

Phosphate release is determined using a conjugated assay for the fluorescence detection of phosphate based on the formation of M-acetyl-3,7-dihydroxyphenoxacin (Atriehb Kei) as is known in the art (Magdzel et al. (2003) Apaiuiisa! Viospetivighu 320: 292-298) . Published assay conditions may saturate the assay in experiments where phosphate is released very rapidly. Additional methods are needed to measure ERBR5 kinetic activity.

The essence of the invention

Compositions and methods of imparting herbicide resistance or tolerance to bacteria, plants, plant cells, tissues, and seeds are presented. The compositions include nucleic acid molecules that encode herbicide resistance or tolerance polypeptides, vectors that contain such nucleic acid molecules, and host cells that contain the vectors. The compositions also include antibodies to herbicide resistance or tolerance polypeptides. As noted, the nucleotide sequences of the invention can be used in DNA constructs or expression cassettes for transformation and expression in organisms including microorganisms and plants. Compositions also contain transformed bacteria, plants, plant cells, tissues and seeds. In addition, methods of obtaining polypeptides encoded by synthetic nucleotides according to the invention are presented.

Isolated nucleic acid molecules and variants thereof encoding herbicide resistance or tolerance polypeptides are presented. Additionally, amino acid sequences and variants encoded by polynucleotides that confer herbicide resistance or tolerance are encompassed. The present invention presents isolated nucleic acid molecules containing the nucleotide sequence represented in ZEO IU MO':1, C or 5, the nucleotide sequence that encodes the amino acid sequence represented in ZEO IU MO:2, 4 or 6, the nucleotide sequence of resistance to herbicide deposited in the host bacterium in the form of accession numbers MEZHI 8B-30888 or MARY B-30949, as well as variants and fragments thereof. Nucleotide sequences that are complementary to nucleotide sequences of the invention, or those that hybridize to sequences of the invention, are also encompassed.

Methods of measuring enzymatic kinetic activity using fluorogenic substrates are also presented.

Description of drawing figures

Figure 1 shows the amino acid sequence alignment of ZKO23 OKE1 (ZEO IU MO:2) and KO51 (ZEO IO MO:6) from Vasiliiv5 siaschia (ZEO 10 MO:7), Kyrgoraseg huiaporpiina5 (ZEO IO MO:8), Euspegispia soybean ( ZEO

IO 5EO MO:11), strain SRA Adgobrasiegicht 5yr. (ZEO IO MO:10) and 7ea tauz (5EO IO MO:9).

Figure 2 shows a scatterplot of enzymatic activity of KO23 (axis MU) as a function of the concentration of PEP (axis X) at glyphosate concentrations of 0.3.5110 mM.

Figure 3 shows a scatterplot of Kt (arr.) (Y axis) as a function of glyphosate concentration (X axis).

The point of intersection of the X axis represents K; for glyphosate.

Detailed description

The present invention will now be described in more detail with reference to the accompanying drawings in which some, but not all, embodiments of the invention are shown. Indeed, these inventions may be embodied in many different forms and should not be construed as limited to the embodiments presented herein; rather, these embodiments are presented so that this disclosure satisfies applicable legal requirements. Similar numbers throughout the application refer to similar elements.

Many modifications and other embodiments of the inventions presented herein will be apparent to those skilled in the art to which these inventions pertain, taking advantage of the inventive concepts set forth in the foregoing descriptions and accompanying drawings. Therefore, it should be understood that the inventions should not be limited to the specific disclosed embodiments, and that modifications and other embodiments are intended to be included within the scope of the claims. Although certain terms are used herein, they are used only in a typical and descriptive sense and not for the purpose of limitation.

The present invention relates to compositions and methods of regulating herbicide resistance in organisms, especially in plants or plant cells. The methods include the transformation of organisms with nucleotide sequences encoding the glyphosate resistance gene of the invention. Nucleotide sequences according to the invention are suitable for obtaining plants that show increased tolerance to the herbicide glyphosate. Thus, transformed bacteria, plants, plant cells, plant tissues and seeds are presented. The compositions include nucleic acids and proteins relevant to herbicide tolerance in microorganisms and plants, as well as transformed bacteria, plants, plant tissues and seeds. The nucleotide sequences of the glyphosate resistance gene (9d9g923 and dg951) and the amino acid sequences of the proteins encoded by them were revealed. The sequences are used in the construction of expression vectors for subsequent transformation of plants of interest, as probes for the selection of other glyphosate resistance genes, as selection markers, etc. Thus, the "glyphosate resistance gene according to the invention" refers to the nucleotide sequence given in 5EO I MO 1 or 3, and variants and fragments thereof (ZEO IU MO:5, 12, 14, 16, 18, 20, 22 , 24, 26, 28, 30 and 32), which encode a polypeptide of resistance or tolerance to glyphosate. Similarly, a "glyphosate resistance polypeptide of the invention" is a polypeptide having the amino acid sequence set forth in 5EO IU MO:2 or 4, and variants and fragments thereof (ZEO IUO MO:6, 15, 17, 19, 21, 23 , 25, 27, 29, 31 and 33), which confer resistance or tolerance to glyphosate to the host cell.

Plasmids containing the herbicide resistance nucleotide sequences of the invention are deposited in the permanent collection of the Crop Collection of the Agricultural Research Service, Northern Regional

of the Scientific Research Laboratory (MERE) on November 18, 2005 under the MEVI accession number B-30888 (dg923), and on June 26, 2006 under the MERE accession number. B-30949 (dg951). This deposit will be maintained in accordance with

of the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for Patent Purposes

Procedures. This deposition has been made for the convenience of those skilled in the art, and it is not believed that a deposition is required under 35 USC 5112.

By "glirosate" is meant any herbicidal form of M-phosphonomethylglycine (including any salt thereof) and other forms from which the anion of glyphosate ip riapia is obtained. A "herbicide resistance protein" or a protein that is the expression product of a "nucleic acid molecule encoding herbicide resistance" includes proteins that confer the ability of a cell to be tolerant to a higher concentration of herbicide than cells not expressing the protein, or to tolerate a given concentration of herbicide for a longer period of time than cells that do not express the protein. A "glyphosate resistance protein" includes a protein that confers on a cell the ability to remain tolerant to a higher concentration of glyphosate than cells that do not express the protein, or to be tolerant to a certain concentration of glyphosate for a longer period of time than cells that do not express the protein. To be tolerant or tolerable is to either survive or perform essential cellular functions, such as protein synthesis and respiration, in a manner that is indistinguishable from untreated cells.

Isolated nucleic acid molecules and their variants and fragments

One aspect of the invention relates to isolated nucleic acid molecules that contain nucleotide sequences encoding herbicide resistance proteins and polypeptides or biologically active portions thereof, as well as nucleic acid molecules suitable for use as hybridization probes to identify nucleic acids that encode herbicide resistance. As used herein, the term "nucleic acid molecule" is intended to include DNA molecules (eg, cDNA or genomic DNA) and RNA molecules (eg, mRNA) and DNA or RNA analogs obtained using nucleotide analogs. A nucleic acid molecule can be single-stranded or double-stranded.

Nucleotide sequences that encode the proteins of the present invention include the sequences shown in 5EO IUO MO/1, C and 5, the nucleotide sequence of resistance to the herbicide introduced into the bacterial host under accession numbers ICC! B-30888 and MAK. B-30949, and variants, fragments, and complementary ones. By the term "complementary" is meant a nucleotide sequence that is sufficiently complementary to a given nucleotide sequence such that it can hybridize with a given nucleotide sequence, thus forming a stable duplex. The corresponding amino acid sequence for the herbicide resistance protein encoded by these nucleotide sequences is given in 5EO IU MO:2, 4 or 6. The invention also encompasses nucleic acid molecules that contain nucleotide sequences encoding incomplete herbicide resistance proteins and are complementary to such An "isolated" or "purified" nucleic acid or protein molecule, or a biologically active portion thereof, is essentially free from other cellular material or culture medium when produced by recombinant techniques, or is essentially free from chemical precursors or other chemical reagents, if synthesized chemically. Preferably, the "isolated" nucleic acid is free of sequences (preferably protein-coding sequences) that are naturally adjacent to the nucleic acid (ie, sequences located at the 5' and 3' ends of the nucleic acid) in the genomic DNA of the organism from which it is derived nucleic acid. For the purposes of the invention, the term "isolated" as applied to nucleic acid molecules excludes isolated chromosomes. For example, in various embodiments, an isolated nucleic acid molecule that encodes glyphosate resistance may contain less than about 5 kb, 4 kb, C kb, 2 kb .p.n., 1 t.p.n., 0.5 t.p.n. or 0.1 t.p.n. nucleotide sequence that is naturally adjacent to the nucleic acid molecule in the genomic DNA of the cell from which the nucleic acid was obtained. A herbicide resistance protein that is substantially free of cellular material includes producing a protein having less than about 3095, 20905, 1090, or 595 (dry weight) of a non-herbicide resistance protein (also referred to herein as a "contaminant protein" ).

Nucleic acid molecules that are fragments of these nucleotide sequences that encode herbicide resistance are also within the scope of this invention. "Fragment" means a part of a nucleotide sequence that encodes a herbicide resistance protein. A fragment of a nucleotide sequence can encode a biologically active part of a herbicide resistance protein, or it can be a fragment that can be used as a hybridization probe or PCR primer using the methods disclosed below. Nucleic acid molecules that are herbicide resistance nucleotide sequence fragments comprise at least about 15, 20, 50, 75, 100, 200, 300, 350, 400, 450, 500, 550, 600, 650, 700, 750, 800, 850, 900, 950, 1000, 1050, 1100, 1150, 1200, 1250, 1300, 1350, 1400, 1450, 1500, 1550, 1600, 1650, 1700, 1750, 1800, 1850, 1950, or up to 1950 consecutive nucleotides. the number of nucleotides present in the full-length nucleotide sequence that encodes resistance to the herbicide disclosed herein (eg, 1892 nucleotides for 5EO IO MO:1, 1259 nucleotides for 5EO IO MO:3, and 1242 nucleotides for 5EO IU MO:5) . By "consecutive" nucleotides are meant nucleotide residues that are immediately adjacent to each other.

Nucleotide sequence fragments of the present invention will primarily encode protein fragments that retain the biological activity of the full-length glyphosate resistance protein; ie, herbicide resistance activity. By "retains herbicide resistance activity" it is meant that the fragment will have at least about 3095, at least about 5095, at least about 70905, or at least about 80905 of the herbicide resistance activity of the full-length glyphosate resistance proteins disclosed herein as ZEOs IO MO:2, 4 or 6. Methods of measuring herbicide resistance activity are known in the art. See, for example, US Patent Nos. 4,535,060 and 5,188,642, each of which is incorporated herein by reference in its entirety.

A fragment of a nucleotide sequence encoding resistance to a herbicide encoding a biologically active portion of a protein of the invention will encode at least about 15, 25, 30, 50, 75, 100, 125, 150, 175, 200, 250, 300, 350, 400 consecutive amino acids, or up to the total number of amino acids in the full-length herbicide resistance protein of the present invention (for example, 436 amino acids for 5ZEO IU MO:2, 413 amino acids for 5EO IU MO 4 and 413 amino acids for ZEO IU MO:6).

The herbicide resistance proteins of the present invention are encoded by a nucleotide sequence sufficiently identical to the nucleotide sequence of BEO I MO:1, C or 5. By "sufficiently identical" is meant an amino acid or nucleotide sequence that has at least about 6095 or 65905 sequence identity, about 7095 or 7595 sequence identity, about 8095 or 8595 sequence identity, about 9095, 9195, 9295, 9395, 94905, 9595, 9695, 9795, 9895, or 99965 sequence identity when aligned with a reference sequence using one of the alignment programs described in this description, using standard parameters. One skilled in the art will recognize that these values can be suitably adjusted to determine the respective identities of the proteins encoded by the two nucleotide sequences by taking into account codon degeneracy, amino acid similarity, reading frame location, and the like.

To determine the percent identity of two amino acid sequences or two nucleic acids, the sequences are aligned for optimal comparison. The percent identity between two sequences is a function of the number of identical positions that the sequences share (ie, percent identity - number of identical positions/total number of positions (eg, overlapping positions) x 100). In one embodiment, the two sequences have the same length. The percentage of identity between two sequences can be determined using techniques similar to those described below, with or without allowance for omissions. When calculating percent identity, as a rule, exact matches are counted.

Determining the percent identity between two sequences can be achieved using a mathematical algorithm. A non-limiting example of a mathematical algorithm that is used to compare two sequences is the algorithm of Kapip apa Ai5spytsi (1990) Rgos. Mai! Asai. 5 OBA 87:2264- 2268, changed to Kaigpip apa Ayb5spy! (1993) Rgos. May Asad from the U.S. BOTH 90:5873-5877. Such an algorithm is included in VABTM and VGABTH programs from Aibspa! oh oh (1990) U. Moi. Vioi 215:403-410. VI A5T nucleotide searches can be performed by the VIA5TM program, the number of points is 100, the word length is 12, to obtain nucleotide sequences homologous to zOS-like nucleic acid molecules according to the invention. VI A5T protein searches can be performed by the VI A5TX program, the number of points "- 50, word length

E 3, to obtain amino acid sequences homologous to the herbicide resistance protein molecules according to the invention. To obtain, for the purpose of comparison, an alignment with gaps, can be used

Surrey VGA5T, as described in Ai5spii ei ai. (1997) Mysiviis Asii Ke5. 25:3389-3402. Alternatively, to perform an iterative search that detects distant similarities between molecules can be applied

RBI-Viavzi. See Aiy5sptsi ei a. (1997) above. When using VGA5T, Surrey VI AZT and RBI-VIA5T programs, you can use the default parameters of the corresponding programs (for example, VGA5TX and VGAZTM).

See mmlu.psbri.pit.piy.dom. Another non-limiting example of a mathematical algorithm used to compare sequences is the SisheiaIMm algorithm (Niddip5ei a. (1994) Mysivs Asia Kev. 22:4673-4680). SiiaMmu compares sequences and aligns amino acid or DNA sequences completely, and thus can provide data on the sequence conservation of the entire amino acid sequence.

The SiviaiiM/ algorithm is used in several commercially available software packages for analysis

DNA/amino acids, such as the AGISMH module of the Mesiog MTI Program Kit (Ipmigodep Corporation, Sagizride, CA).

After alignment of the amino acid sequences of Siviam, the percentage of amino acid identity can be determined. A non-limiting example of a program suitable for alignment analysis

SiiviaMu, is sepebostm, (zepedos"m (Kaig! Mispoiaz) allows to evaluate amino acid similarity (or DNA) and identity between several proteins. Another non-limiting example of a mathematical algorithm used for sequence comparison is the algorithm of Mueg5 and MiShSheg (1988) SAVIO5 4 :11-17. Such an algorithm is included in the ACOM program (version 2.0), which is part of the CO sequence alignment software package (available from Asseigu5, Ips., San Diego, CA). Using the ACOM program to compare amino acid sequences, one can RAM12 residue weight table 0, break length penalty 12 and break penalty 4 are applied.

Unless otherwise noted, Version 10 of SAR, which uses the algorithm of Meedietap and Musp5sp (1970) 9. Mine.

Vioi 48 (3):443-4A53, will be used to determine sequence identity or similarity using the following parameters: 95 identity and 90 similarity for nucleotide sequence using SAR Umeidnpi 50 and Hepdip UUeidpi Z ii pmuzdarapa.str matrix of points; 9o identity or 90 similarity for the amino acid sequence using SAR Uueidni and Hepdip Umeidni 2, and the VHO5BIMb2 scoring program. Equivalent programs may also be used. By "equivalent program" is meant any sequence comparison program that, for any two considered sequences, produces an alignment that has identical nucleotide residue matches and an identical percentage of sequence identity when compared to the corresponding alignment made using SAR Version 10 .

The invention also encompasses nucleic acid variant molecules. "Variants" of nucleotide sequences that encode herbicide resistance include those sequences that encode a herbicide resistance protein disclosed herein but that are conservatively different due to degeneracy of the genetic code, as well as those that are substantially identical as discussed above (for example, ZEO IU MO:5, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30 and 32 are variants of 5EO IU MO:1). Natural allelic variants can be identified using known methods of molecular biology, such as polymerase chain reaction (PCR) and hybridization methods, as outlined in general below. Alternative nucleotide sequences also include synthetically derived nucleotide sequences that have been obtained, for example, using site-directed mutagenesis, but which still encode the herbicide resistance proteins disclosed in the present invention, as discussed below.

Variant proteins covered by the present invention are biologically active if they retain the desired biological activity of the native protein, ie, herbicide resistance activity. By "retains herbicide resistance activity" is meant that the variant will have at least about 3095, at least about 5095, at least about 7095, or at least about 8095 of the herbicide resistance activity of the native protein. Methods for measuring herbicide resistance activity are well known in the art. See, for example,

US Patents MoMe 4,535,060 and 5,188,642, each of which is incorporated herein by reference in its entirety.

A skilled specialist will further appreciate that the nucleotide sequences according to the invention can be changed by mutation, thus leading to changes in the amino acid sequence of the encoded herbicide resistance proteins, without changing the biological activity of the proteins. Thus, isolated variant nucleic acid molecules can be created by introducing one or more nucleotide substitutions, additions, or deletions into the corresponding nucleotide sequence disclosed herein, such that one or more amino acid substitutions, additions, or deletions are introduced into the encoded protein. deletions Mutations can be introduced using standard techniques such as site-directed mutagenesis and PCR-mediated mutagenesis. Such variant nucleotide sequences are also within the scope of this invention.

For example, conservative amino acid substitutions can be made in one or more predicted non-essential amino acid residues. A "non-essential" amino acid residue is a residue that can be changed in the sequence of a wild-type herbicide resistance protein without changing biological activity, while an "essential" amino acid residue is required for biological activity. A "conservative amino acid substitution" is one in which an amino acid residue is replaced by an amino acid residue that has a similar side chain. Families of amino acid residues having similar side chains have been identified in the art. These families include amino acids with basic side chains (eg, lysine, arginine, histidine), acidic side chains (eg, aspartic acid, glutamic acid), uncharged polar side chains (eg, glycine, asparagine, glutamine, serine, threonine, tyrosine, cysteine), non-polar side chains (e.g. alanine, valine, leucine, isolecine, proline, phenylalanine, methionine, tryptophan), beta-branched side chains (e.g. threonine, valine, isoleucine) and aromatic side chains (e.g. tyrosine, phenylalanine , tryptophan, histidine). Amino acid substitutions can be made in non-conservative regions that retain function. In particular, such substitutions would not be made for conserved amino acid residues or for amino acid residues within a conserved motif where such residues are essential for protein activity. However, one skilled in the art would appreciate that functional variants may have small conservative or non-conservative changes in conserved residues.

Guvz-22, Ago-124, Avr-313, Ago-344, Ago-386 and Guz-411 are conserved residues of ERBR synthase from E. soybean (Zepoprhypp ei ai. (2001) Rgos. May). Asad 5 OA 98:1376-1380). Conservative residues important for

ERBR-synthase activity also includes Ag49-100, Avr-242 and Azr-384 (ZeImarapaiuap ei ai. (1995) REV5

Journal of Medicine 374:253-256). Agd-27 binds to ZR (ZPPiyShshShemopin ei a. (1999) Viosnetivighu 38:296-302).

Alternatively, variant nucleotide sequences can be obtained by introducing mutations randomly along all or part of the coding sequence, for example, using saturation mutagenesis, and the resulting mutants can be tested for the ability to confer herbicide resistance activity to identify mutants that retain the activity. After mutagenesis, the encoded protein can be expressed recombinantly, and the activity of the protein can be determined using standard testing methods.

Using methods such as PCR, hybridization, etc., appropriate herbicide resistance sequences can be identified, such sequences having substantial identity to the sequences of the invention. See, for example, Zatyuhook and Kizzei! (2001) MoiIesshag Siopipd: Garogayugu Mapiai! (Soybean 5rhipa

Nagbrog Garogaiogu Rgez5, Soiai Zrgipd Nagrog, MU) and Ippiv, ei a. (1990).

Arriisayopz (Asadetis Rgevv, 5I.-I otsiv, MO).

In the hybridization method, all or part of the herbicide resistance nucleotide sequence can be used to screen cDNA or genomic libraries. Methods for creating such cDNA and genomic libraries are well known in the art and are disclosed in the book of Kizzey (2001) above. The so-called hybridization probes can be genomic DNA fragments, cDNA fragments, RNA fragments, or other oligonucleotides, and can be labeled with a detectable group, such as RP, or any other detectable marker, such as other radioisotopes, a fluorescent compound, an enzyme or enzyme cofactor. Hybridization probes can be obtained by labeling synthetic oligonucleotides based on known nucleotide sequence(s) encoding resistance to the herbicide disclosed herein. In addition, degenerate primers designed on the basis of conservative nucleotides or amino acid residues in the nucleotide sequence or coded amino acid sequence can be used. The probe typically comprises a region of nucleotide sequence that hybridizes under stringent conditions to at least about 12, at least about 25, at least about 50, 75, 100, 125, 150, 175, 200, 250, 300, 350, 400, 500, 600, 700, 800, 900, 1000, 1200, 1400, 1600 or 1800 consecutive nucleotides of the nucleotide sequence(s) encoding resistance to the herbicide of the invention, or a fragment or variant thereof. Methods for obtaining hybridization probes are well known in the art and are disclosed in Kizzea's patent application! (2001) above, and Zatrhook ei ai. (1989)

MoiIesshiag Siopipod: A I arogayugu Maptspai (249 ea., Soia 5riipd Natbog I arogayugu Rgevs, Soia brgipd Nagbog, MU), each of which is included in this description by reference.

For example, the entire herbicide resistance sequence disclosed herein, or one or more parts thereof, can be used as a probe capable of specifically hybridizing to the corresponding herbicide resistance sequences and to template RNAs. To achieve specific hybridization under different conditions, such probes include sequences that are unique and are at least about nucleotides in length and at least about 20 nucleotides in length. Such probes can be used to amplify the corresponding herbicide resistance sequences from the selected organism by PCR. This technique can be used to isolate additional coding sequences from a desired organism or as a diagnostic test to determine the presence of coding sequences in an organism. Hybridization techniques include hybridization screening of plate-plated DNA libraries (or plaques or colonies; see, for example, Zatrgook et al. (1989) MoiIesshag Siopipd: A

And arogayugu Mappai (24 units, Soia Zriipd Nagtog And arogayagu Rgev5, Soia briipd Nagbog, MU).

Hybridization of such sequences can be performed under stringent conditions. By "stringent conditions" or "stringent hybridization conditions" is meant conditions in which the probe hybridizes to its target sequence to a detectably greater extent than to other sequences (eg, at least 2-fold above background). Hard conditions are sequence dependent and will be different under different circumstances. By controlling the stringency of tal hybridization or washing conditions, target sequences that are 10095 complementary to the probe can be identified (potiodoio5rgobipd). Alternatively, the stringency conditions can be adjusted to allow some mismatch in the sequences so that more low degrees of similarity (low sequence similarity) Typically, the probe is less than about 1000 nucleotides in length, or less than about 500 nucleotides in length.

Generally, harsh conditions will be those where the salt concentration is less than about 1.5 M ion

Ma is typically about 0.01 to 1.0 M concentration of Ma ion (or other salts) at a pH of 7.0 to 8.3 and a temperature of at least about 307°C for short probes (eg, 10 to 50 nucleotides) and at least about 60"C for long probes (eg, greater than 50 nucleotides). Rigid conditions can also be achieved by adding destabilizing agents such as formamide. Illustrative low stringency conditions include hybridization in 3095-3595 formamide buffer, 1 M Massey, 195

OB (sodium dodecyl sulfate) at 37°C, and washing in 1X-2X 5Z5O (20X 550 - 3.0 M Mass/0.3 M trisodium citrate) at 50-557C. Illustrative conditions of moderate stringency include hybridization at 4095-4595- formamide, 1.0 M mass, 195th 5O5 at 37"С, and washing in 0.5X-1X 550 at 55-607С. Illustrative high stringency conditions include hybridization in 5095 formamide, 1 M Mass, 1956 505 at 37°C, and washing in 0.1X 55C at 60-657°C. Optionally, wash buffers may contain from about 0.195 to about 195,505. The duration of hybridization is usually less than about 24 hours, usually from about 4 to about 12 hours.

Specificity is generally a function of post-hybridization washes, with critical factors being the ionic strength and temperature of the final wash solution. For DNA-DNA hybrids, Tt can be approximated by the equation of Meipkoip apa Umapi (1984) Apai!. Viospet. 138:267-284: Tya - 81.57C and 16.6 (109 M), and 0.41 (95655) - 0.61 (96 forms) - 500/I; where M is the molarity of monovalent cations, 9005 is the percentage of guanosine and cytosine nucleotides in DNA, 95 forms. is the percentage of formamide in the hybridization solution, and Her is the length of the hybrid in pairs of nitrogenous bases. Tt is the temperature (at a given ionic strength and pH) at which 50906 complementary target sequences hybridize to a perfectly matched probe. Tt decreases by about 17C with each 1905 inconsistencies; thus, Tt, hybridization and/or washing conditions can be adjusted to hybridize to sequences of the desired identity. For example, if sequences with "9095th identity" are to be found, Tt may be reduced by 10"C. Typically, stringent conditions are chosen to be about 5"C lower than the melting point temperature (Tt) of the specific sequence and its complement at a certain ionic strength and pH. However, under very stringent conditions, hybridization and/or washing can be performed at 1, 2, 3, or 4°C below the melting point (Tt); under moderately stringent conditions, hybridization and/or washing can be performed at 6, 7, 8 , 9, or 10"C lower than the melting point temperature (Тt); under low stringency conditions, hybridization and/or washes can be performed at 11, 12, 13, 14, 15, or 20°C below the melting point (Tt). variations in stringency of hybridization and/or wash solutions are essentially described. If the desired degree of mismatch results in a T less than 457°C (aqueous solution) or 327°C (formamide solution), it is preferable to increase the 55°C concentration so that a higher temperature can be used . An extensive guide to nucleic acid hybridization is found in Tid55ep (1993) I arogayug

Tesppidtsev ip Viospetivighu apa Moiiesshag Vioiodu - Nubgiaigaiop my Misieis Asii Rgobez, Raigi I, SNarieg 2 (Eivemieg, Mem MogK); and A!,yzibei ei ai., ed5. (1995).

Rybiivpipd apa UmMieu-Ipiegzsiepse, Mem Mogk). See zagargook her aI. (1989) MoiIesshag Siopipd: A Garogayugu

Maptsmai (249 units, Soii 5riipd Natbog I arogaiyugu Rgezz, Soia brgipd Nagbog, MU).

Isolated proteins and their variants and fragments

Herbicide resistance proteins are also within the scope of this invention. By "herbicide resistance protein" or "herbicide tolerance protein" is meant a protein having the amino acid sequence represented in 5EO IU MO:2, 4 or 6. Fragments, biologically active parts and variants thereof are also provided and may be used for the practical implementation of the methods according to the present invention. "Fragments" or "biologically active parts" include polypeptide fragments containing a portion of the amino acid sequence that encodes a herbicide resistance protein as set forth in 5EO IO MO2, 4, or or, and which retain herbicide resistance activity. The biologically active part of the herbicide resistance protein can be a polypeptide, for example, having 10, 25, 50, 100 or more amino acids in length. Such biologically active parts can be obtained using recombinant techniques and evaluated for herbicide resistance activity. Methods for measuring herbicide resistance activity are well known in the art. See, for example, US Patent Nos. 4,535,060 and 5,188,642, each of which is incorporated herein by reference in its entirety. As used herein, a fragment contains at least 8 consecutive amino acids 5EO IO MO:2, 4 or b. However, the invention encompasses other fragments, such as, for example, any fragment in a protein greater than about 10, 20, 30, 50, 100, 150, 200, 250, 300, 350, or 400 amino acids.

By "variants" is meant proteins or polypeptides having an amino acid sequence that is at least about 6095, 6595, at least about 7095, 7595, at least about 8095, 8595, 9095, 9195, 9295, 93905, 94905, 9595, 9695, 97905, 9895 or 9995, identical to the amino acid sequence of ZEO

IO MO:2, 4, or b (for example, ZEO IO MO:6, 15, 17, 19, 21, 23, 25, 27, 29, 31 and 33 are variants of 5EO IU MO:2).

Variants also include polypeptides that are encoded by a nucleic acid molecule that hybridizes to, or is complementary to, a nucleic acid molecule of ZEO IJUO MO:1, C or 5 under stringent conditions.

Variants include polypeptides that differ in amino acid sequence due to mutagenesis.

The variant proteins encompassed by the present invention are biologically active such that they continue to have the desired biological activity of the parent protein, ie, retain herbicide resistance activity. Methods for measuring herbicide resistance activity are well known in the art. See, e.g., U.S. Pat

Nos. 4535060 and 5188642, each of which is incorporated herein by reference in its entirety.

Bacterial genes, such as gene 9923 or dg9451 of the present invention, quite often have multiple methionine initiation codons near the beginning of the open reading frame. Frequent initiation of translation at one or more of these start codons will result in the formation of a functional protein. These start codons may include ATO codons. However, bacteria such as Vasiyi5 5r. also recognize the STO codon as a start codon, and proteins that begin translation at STO codons contain methionine in the first amino acid. Furthermore, it is not often determined which of these codons are used naturally in the bacterium. Thus, it is clear that the use of one of the additional methionine codons can lead to the formation of variants dgd23 or dg951, which have resistance to the herbicide. These herbicide resistance proteins are within the scope of this invention and can be used in the methods of this invention.

Antibodies to polypeptides of the present invention, or to variants or fragments thereof, are also encompassed.

Methods for obtaining antibodies are well known in the art (see, for example, Nagomzh/apa Gape (1988)

Apiirodiev: And Aroghaiogu Mapiai! (Soy Zrgipd Nagrog Garogaiogu, Soy Zrgipd Nagrog, MU); US Patent Mo 4196265).

Changed or improved options

It is recognized that the DNA sequence of 9gd23 or dgd51 can be changed using various methods, and that these changes can lead to DNA sequences that encode proteins with amino acid sequences different from those encoded by 9dgd23 or 9g951. This protein can be modified in a variety of ways, including amino acid substitutions, deletions, truncations, and insertions. Methods of such manipulation are well known in the art. For example, variants of the amino acid sequence of SKO23 or

OO51 can be obtained with the help of mutations in DNA. This can also be achieved by one of several forms of mutagenesis and/or by directed evolution. In some aspects, changes that are encoded in the amino acid sequence will not substantially affect the function of the protein. Such variants will have the desired herbicide resistance activity. However, it is clear that the ability of OKO23 or SKO51 to confer herbicide resistance can be improved using such techniques in the compositions of the present invention. For example, 523 or AZKO51 can be expressed in host cells that exhibit high levels of misincorporation during DNA replication, such as XI-1 Nei (Zigagadepe, Gadoia, CA). After reproduction in such strains, the 9gd23 or 49gd51 DNA can be isolated (eg, by obtaining plasmid DNA or by PCR amplification and cloning

of the resulting PCR fragment into a vector) and cultivated in non-mutagenic strains. Clones containing mutations in dg(d23 or adg951) can be identified by measuring improved resistance to a herbicide such as glyphosate, for example by growing cells on increasing concentrations of glyphosate and testing for clones that have tolerance to increasing concentrations of glyphosate .

Alternatively, changes can be made to the protein sequence of many proteins at the amino- or carboxy-terminus, essentially without affecting activity. These changes may include insertions, deletions or changes introduced by modern molecular methods such as PCR, including PCR amplification, which alter or extend the sequence that codes for the protein by incorporating sequences that code for amino acids in oligonucleotides that use during PCR amplification. Alternatively, added protein sequences may include complete protein-coding sequences, such as those commonly used in the art to produce hybrid proteins. Such hybrid proteins are often used to (1) increase expression of the protein of interest; (2) introducing a binding domain, enzymatic activity, or epitope to facilitate or purify the protein, or detect the protein, or other experimental applications known in the art; or, (3) targeted secretion or translation of the protein into a subcellular organelle, such as the periplasmic space of Gram-negative bacteria or the endoplasmic reticulum of eukaryotic cells, the latter of which often results in protein glycosylation.

Variant nucleotide and amino acid sequences of the present invention also encompass sequences obtained by mutagenic and recombinant procedures, such as DNA shuffling.

Using this procedure, one or more different coding regions of herbicide resistance proteins can be used to create a new herbicide resistance protein that has the desired properties.

Thus, libraries of recombinant polynucleotides are formed from a number of related polynucleotide sequences, including sections of the sequence that have substantial sequence identity and can be homologously recombined by ip migo or ip mmo. For example, using this approach, fragments of a sequence encoding a domain of interest can be shuffled between a herbicide resistance gene of the invention and other known herbicide resistance genes to produce a new gene encoding a protein with an improved property of interest. such as increased glyphosate resistance activity. Strategies for such DNA shuffling are known in the art. See, for example, 5ietteg (1994) Rhos. May Asai. si. BOTH 91:10747-10751; Zietteg (1994) Maishtge 370:389-391;

Strategies and strategies. (1997) Mashge Vioyesp. 15:436-438; Mooge ey a. (1997) 9. Mine. VioI. 272:336-347; 7 Napo ei ai. (1997) Rhos. May). Asai. 5 BOTH 94:4504-4509; Articles of hers. (1998) Maishge 391:288-291; and US Patents Memo 5,605,793 and 5,837,458.

Transformation of bacterial or plant cells

Presented herein are novel isolated genes that confer herbicide resistance. Also presented are the amino acid sequences of SBOS23 and 5KO51 proteins. The protein produced when this gene is translated allows cells to function in the presence of concentrations of the herbicide that would otherwise be toxic to cells, including plant cells and bacterial cells.

In one aspect of the invention, the gene 9g923 or d9g951 is useful as a marker gene for evaluating the transformation of bacterial or plant cells.

By engineering 9g9d23 or dg951 for (1) expression from a bacterial promoter that drives transcription in the test organism, (2) correct translation to produce an unaltered OKO23 or OKO51 peptide, and (3) transfer of cells to a different toxic concentration of herbicide can be identified cells that have been DNA transformed by their herbicide resistance. By "promoter" is meant a nucleic acid sequence that functions to direct the transcription of a downstream coding sequence. The promoter, along with other nucleic acid sequences that regulate transcription and translation (also called "regulatory sequences"), is necessary for the expression of the DNA sequence of interest.

Transformation of bacterial cells is accomplished by one of several techniques known in the art, including, but not limited to, electroporation or chemical transformation (See, e.g., A!zibei (ea.) (1994) Sigtepi Rgoiosoi5 ip MoiIesshag Vioiodu (opp Um/ ieu apa 5opv, Ips., Ipaiaparoi 5,

IM)). Markers that carry resistance to toxic substances are used to identify transformed cells (which have taken up and express the tested DNA) from non-transformed cells (those that do not contain or do not express the tested DNA). In one aspect of the invention, the gene 9gd23 or ag951 is used as a marker gene to evaluate the transformation of bacterial or plant cells.

The transformation of plant cells can be carried out in a similar way. By "plant" we mean whole plants, plant organs (for example, leaves, stems, roots, etc.), seeds, plant cells, shoots, embryos and offspring thereof. Plant cells can be differentiated or undifferentiated (eg, callus, suspension cell cultures, protoplasts, leaf cells, root cells, phloem cells, pollen). "Transgenic plants" or "transformed plants" or "stably transformed" plants, cells or tissues refer to plants that have absorbed or integrated exogenous nucleic acid sequences or DNA fragments into the plant cell. By "stable transformation" is meant that the nucleotide construct introduced into the plant integrates into the plant's genome and is capable of being inherited by its offspring.

The dgd23 or dgd51 gene according to the invention can be modified to obtain or enhance expression in plant cells. The herbicide resistance sequences of the invention can be represented in expression cassettes for expression in a plant of interest. "Cassette for expression in a plant" includes DNA constructs that are capable of leading to the expression of a protein from an open reading frame in a plant cell. The cassette will include, in the 5-3 direction of transcription, a transcription initiation site (ie, promoter) operably linked to the DNA sequence of the invention, and a transcription and translation termination site (ie, termination site) that function in plants. The cassette may additionally contain at least one additional gene for cotransformation into the organism, such as a selection marker gene. Alternatively, the additional gene(s) can be represented in multiple cassettes for expression. Such an expression cassette is provided with multiple restriction sites for insertion of the herbicide resistance sequence under the transcriptional regulation of the regulatory regions.

The promoter may be native or homologous, or foreign or heterologous, to the host plant and/or to the DNA sequence of the invention. Additionally, the promoter may be a naturally occurring sequence or, alternatively, a synthetic sequence. If the promoter is "native" or "homologous" to the host plant, this means that the promoter is derived from the native plant into which the promoter is introduced. If a promoter is "foreign" or "heterologous" to a DNA sequence of the invention, it means that the promoter is not derived from or is not a naturally occurring promoter functionally linked to the DNA sequence of the invention. "Heterologous" usually refers to nucleic acid sequences that are not endogenous to the cell or part of the native genome in which they reside and have been added to the cell by infection, transfection, microinjection, electroporation, microprojection, or the like. By "operably linked" is meant a functional relationship between the promoter and the second sequence, if the promoter sequence initiates and mediates transcription from the DNA sequence corresponding to the second sequence. Of course, "operably linked" means that the linked nucleic acid sequences are contiguous and, where necessary to join two contiguous protein-coding regions, contiguous in the same reading frame.

Often such constructs will also contain 5' and 3' untranslated regions. Such constructs may contain a "signal sequence" or "leader sequence" to facilitate co-translational or post-translational transport of the peptide of interest into certain intracellular structures such as the chloroplast (or other plastid), endoplasmic reticulum or Golgi apparatus, or to be secreted.

For example, a gene can be designed to contain a signal peptide to facilitate transfer of the peptide to the endoplasmic reticulum. By "signal sequence" is meant a sequence that is known or believed to lead to co-translational or post-translational transport of the peptide across the cell membrane. In eukaryotes, this transport usually involves secretion into the Golgi apparatus, with some glycosylation. "Leader sequence" means any sequence that, upon translation, leads to an amino acid sequence sufficient to initiate co-translational transport of a peptide chain into a subcellular organelle. Thus, the above includes leader sequence-directed transport and/or glycosylation via passage into the endoplasmic reticulum, passages to vacuoles, plastids including chloroplasts, mitochondria, and the like. A cassette for expression in a plant can also be designed to contain an intron whose mRNA processing is necessary for expression.

By "3" untranslated region" is meant the nucleotide sequence located downstream of the transcription of the coding sequence. Polyadenylation signal sequences and other sequences encoding regulatory signals capable of affecting the addition of polyadenylic acid tails to the 33-end of the precursor mRNA are 3 untranslated regions. "Untranslated region 5" means a nucleotide sequence located upstream of the transcription of the coding sequence.

Other upstream or downstream untranslated elements include enhancers. Enhancers are nucleotide sequences that lead to increased expression of the promoter region. Enhancers are known in the art and include, but are not limited to, an enhancer site

ZM40 and enhancer element 355.

The termination site may be native to the transcription initiation site, may be native to the herbicide resistance sequence of the present invention, or may be derived from another source. Convenient termination sites are available from the A. Stetiasiep5 Ti plasmid, such as the octopine synthase and nopaline synthase termination sites. See also Spegipeai ei a!. (1991) Mine. Sept. sepia 262:141-144;

Rgotsaigooi (1991) Say! 64:671-674; Zapiasop eyi a. (1991) Sepev Oeu. 5:141-149; Modep ei a)i. (1990) Riapi Sei 2:1261-1272; Mypgoe her a. (1990) Sep 91:151-158; VaiPaz her ai. (1989) Mysieis Asiaz Nev. 17:7891-7903; and dov5pi her ai. (1987) Mysieis Asia Nez. 25 15:9627-9639.

If necessary, the gene(s) can be optimized for increased expression in the transformed host cell. Thus, genes can be synthesized using host-preferred codons for improved expression, or can be synthesized using host-preferred codons using repeats. Of course, C gene content will be increased. See, for example, Satrbrei! apa sSougi (1990) Riapi Rpuvzioi!. 92:1-11 for a discussion of host preferred codons. Methods of synthesizing host preferred genes are well known in the art. See, for example, US Patent MoMe 6320100; 6075185; 5380831 and 5436391, US MoM Published Applications 20040005600 and 20010003849, and Mygau et al. (1989) Mysieis Asiav Nev. 17:477-498, incorporated herein by reference.

In one embodiment, the nucleic acids of interest are targeted for expression in the chloroplast. In this method, if the nucleic acid of interest is not directly inserted into the chloroplast, the expression cassette will additionally contain a nucleic acid that encodes a transit peptide to direct the gene product of interest into the chloroplast. Such transit peptides are known in the art. See, for example, Mop Neyi|)pe ei a. (1991) Riapi Moi. Axes Sept. 9:104-126; Spiaik her ai. (1989) 9. Vioi. Spent 264:17544-17550; OePa-Siorra ei ai. (1987) Riapi Rpuzioi. 84:965-968;

Voteg" ei a!. (1993) Viospet. Viorpuvz. Nez. Sottyp. 196:1414-1421; and Zpapy ei a). (1986) 5siepse 233:478-481.

Nucleic acids of interest to be targeted to the chloroplast can be optimized for expression in the chloroplast, taking into account the differences in codon usage between the plant nucleus and this organelle. Thus, nucleic acids of interest can be synthesized using chloroplast preferred codons. See, for example, US Patent No. 5,380,831, incorporated herein by reference.

Typically, a given "cassette for expression in a plant" will be inserted into a "vector for plant transformation". "Transformation vector" refers to a DNA molecule that is necessary for effective cell transformation. Such a molecule may consist of one or more cassettes for expression, and may be organized into more than one "vector" DNA molecule. For example, dual vectors are plant transformation vectors that use two non-sequential DNA vectors to encode all the necessary cis- and trans-acting functions for the transformation of plant cells (NePep5 apa Miiiipeaiykh (2000)

Tgepavz ip Riapi 5siepse 5:446-451). "Vector" refers to a nucleic acid construct engineered for transfer between different host cells. An "expression vector" refers to a vector that is capable of internalizing, integrating, and expressing heterologous DNA sequences or fragments in a foreign cell.

This plant transformation vector may include one or more DNA vectors necessary to achieve plant transformation. For example, it is common practice in the art to use plant transformation vectors that consist of more than one sequenced DNA segment. These vectors are often referred to in the art as "dual vectors". Double vectors, as well as vectors with helper plasmids, are most often used for Adhorasiegisht-mediated transformation, when a sufficiently large size and complexity of DNA segments are required to achieve efficient transformation, and it is advantageous to divide functions between individual DNA molecules. Binary vectors typically contain a plasmid vector containing cis-acting sequences required for T-DNA movement (such as left border and right border), a selection marker engineered to be capable of expression in a plant cell , and the gene of interest (a gene engineered to be capable of expression in a plant cell for which the formation of transgenic plants is desired). This plasmid vector also contains sequences necessary for replication in bacteria. The cis-acting sequences are arranged in such a way as to ensure efficient transfer into and expression in plant cells.

For example, the selection marker gene and the gene of interest are located between the left and right borders. Often, the second plasmid vector contains trans-acting factors that mediate T-DNA transfer from Adhorasiegisht to plant cells. This plasmid often contains virulence factors (mig genes) that allow infection of plant cells by Adhorasiegisht, and DNA transfer by cutting in the border sequences and mig-mediated DNA transfer, as it is understood in the art (NePep5 apa Mijpeaih (2000 ) Tgepa5 ip Riapi Zsiepse, 5:446-451). Several types of strains

Adhorase genes (e.g., I! BA4404, (zM3101, ENATO1, ENAT1O5, etc.) can be used for plant transformation. A second plasmid vector is not necessary for plant transformation by other methods such as microengineering, microinjection , electroporation, polyethylene glycol, etc.

Plant transformation

The methods of the invention relate to the introduction of a nucleotide construct into a plant. By "introducing" is meant providing a plant with a nucleotide construct in such a way that the construct gains access to the interior of the plant cell. The methods according to the invention do not require the use of a specific method of introducing a nucleotide construct to a plant if the nucleotide construct gains access to at least one cell of the plant. Methods of introducing nucleotide constructs into plants are known in the art, including, but not limited to, stable transformation methods, transient transformation methods, and virus-mediated methods.

In general, plant transformation methods involve the transfer of heterologous DNA into target plant cells (eg, immature or mature embryos, suspension cultures, undifferentiated callus, protoplasts, etc.), followed by the application of the maximum threshold level of suitable selection (depending on selection marker gene and in this case "glyphosate") regenerate transformed plant cells from the group of untransformed cell mass. Explants are usually transferred for fresh access to the same medium and cultured in the usual manner. Subsequently, the transformed cells differentiate into shoots after being transferred to a medium for regeneration supplemented with the maximum limiting level of the selection substance (for example, "glyphosate"). The shoots are then transferred to a selective plant growth medium to regenerate root shoots or seedlings.

The transgenic seedling then grows into mature plants and produces fertile seeds (for example, Nieyi ei ai. (1994)

Tne Riapi uoshtai 6:271-282; Ivpida her ai. (1996) Mashge Viosiesppoiodu 14:745-750). Explants, as a rule, are transferred fresh to the same medium and cultured in the usual way. A general description of the methods and methods of obtaining transgenic plants is found in Auga5 apa Ragk (1994) Spiisa! Nemiemv ip Riapi Zsiepse 13:219-239 and Vottipepi apa dashnag (1997) Maudisa 42:107-120. Since the transformed material contains many cells; and transformed and non-transformed cells are present in any part of the treated target callus or tissue or group of cells. The ability to destroy non-transformed cells and allow transformed cells to reproduce yields transformed plant cultures. Often, the ability to remove untransformed cells is a limitation for rapid recovery of transformed plant cells and successful generation of transgenic plants. Molecular and biochemical methods can be used to confirm the presence of an integrated heterologous gene of interest in the genome of a transgenic plant.

Production of transgenic plants can be accomplished by one of several methods, including, but not limited to, introduction of heterologous DNA by Adhorasiegist into plant cells (Adgorasiegiit-mediated transformation), bombardment of plant cells with particle-attached heterologous foreign DNA, and various other targeted methods without particles (e.g. Niei ei ai. (1994) Te Riapi mahtpai 6:271-282; Ivpida ei ai. (1996) Mashge Viotesppoiodu 14:745-750;

Auge5 apa Raik (1994) Spiysa! Nemiemuv ip Riapi bsiepse 13:219-239; Wottipepi apa dashnag (1997) Mauaisa 42:107-120), for DNA transfer.

Methods of chloroplast transformation are well known in the art. See, for example, Zmab eyi a. (1990)

Rgos. Mai). Asad 5 BOTH 87:8526-8530; mar apa Mayida (1993) Rhos. Mai). Asad si. BOTH 90:913-917; mar apa Mayida (1993) EMVO 3. 12:601-606. The method is based on the delivery by means of a "gun" of DNA particles containing a selection marker, which addresses the DNA to the plastid genome by means of homologous recombination. In addition, plastid transformation can be achieved by transactivation of a silent transgene in the plastid by tissue-predominant expression of nuclear-encoded and plastid-directed RNA polymerase. Such a system was mentioned in MevVgide ei ai. (1994) Rgos. May). Asad 5 BOTH 90:5873-5877.

Cells that have been transformed can be grown into plants according to conventional methods. See, for example, MeSogtisk ei a!. (1986) Riapi Sei! Kerogov 5:81-84. These plants can then be grown and pollinated with either the same transformed strain or different strains, and the resulting hybrid has constitutive expression of the desired identified phenotypic trait. Two or more generations can be grown to ensure that expression of the desired phenotypic feature is stably maintained and inherited, and then seeds are harvested to confirm that expression of the desired phenotypic feature has been achieved. Thus, the present invention provides transformed seeds (which are also called "transgenic seeds") that have a nucleotide construct of the invention, for example, an expression cassette of the invention, stably incorporated into their genome.

Measurement of ERBR5 activity

In one embodiment of the present invention, the EPZR3 glyphosate resistance enzyme has a Kt for phosphoenolpyruvate (PEP) between about 1 and about 150 µM, including about 2 µM, about 3.4, 5.6, 7.8, 9, 10, 20 , 30, 40, 50, 60, 70, 80, 90, 100, 110, 120, 130 or about 140 µM, and K; (glyphosate)/Kt (PEP) between about 500 and about 1000, about 550, about 600, 650, 700, 750, 800, 850, 900, 950, or up to about 1000. As used herein, Kt and K; measured under conditions in which the enzyme obeys Michaelis-Menten kinetics, a pH of approximately 7. One non-limiting measurement technique uses purified enzyme in potassium chloride and HERE5 buffer at pH 7 at room temperature and uses 0 to 10 mM glyphosate concentrations.

Kinetic activity of EPOR5 can be measured, for example, by measuring the release of phosphate that is formed during catalysis of an EPOR5 substrate (e.g., PEP and 53P) to the next reaction product (e.g., 5-enolpyruvyl-3-phosphoshikimic acid) using a fluorescence assay , described by Ma?dpe? hey ayy!. (2003) Apai. Viospet. 320 (2):292-298. This test is based on the oxidation of the non-fluorescent compound M-acetyl-3,7-dihydroxyphenoxacin (AtriehF Neai, Ipmigodep,

Saghizrad, SA) into the fluorescent compound resorufin with the help of hydrogen peroxide (2potsi and Rapspik-

Moiospipa (1997) Apai). Viospet. 253:169-174). The reaction is based on the use of phosphate purine nucleoside phosphorylase (PMP), xanthine oxidase (XOO) and horseradish peroxidase (NKR). Is the release of phosphate related to the level of fluorescence produced by the conversion of Atriech? Kea u resorufin.

Fluorescence can be measured, for example, using a fluorimeter filter, a spectrophotometer for plate reading, a spectrofluorimeter, a spectrophotometer, or the like, using methods well known in the art. Fluorescence produced by the reaction can be detected using a fluorometric setup with excitation in the range of about 530 to about 560 nm and emission at about 590 nm. The absorbance can be measured (eg, using a spectrophotometer or plate reading spectrophotometer) at about 565 nm.

In one embodiment, the present invention encompasses changing the previously specified test conditions to expand the dynamic range of the test to accommodate a wider range of substrate concentrations.

The variation includes an HOO concentration of at least 1 U/mL, about 1 to about 1.25 U/mL, about 1.25 to about 1.5 U/mL, about 1.5 to about 2 U/mL, or greater than 2 O/ml; concentration

PP greater than 0.1 U/ml, from about 0.1 to about 0.5 U/ml, from about 0.5 to about 1 U/ml, from about 1 to about 1.5 U/ml, from about 1.5 to about 2 O/ml, or greater than 2 O/ml; and the concentration of Atrieh? Ke greater than 100 µM, from about 100 to about 200 µM, from about 200 to about 300 µM, from about 300 to about 400 µM, from about 400 to about 500

MKM, from about 500 to about 600 µM, from about 700 to about 800 µM, from about 800 to about 900 µM, from about 900 to about 1000 µM, or greater than about 1000 µM.

This modification can be applied to assays measuring the kinetic activity of any enzyme in which phosphate is released during an enzyme-catalyzed reaction.

Plants

The present invention can be used to transform any variety of plants, including but not limited to monocots and dicots. Examples of plants of interest include, but are not limited to, cereals (corn), sorghum, wheat, sunflower, tomato, cruciferous, pepper, potato, cotton, rice, soybean, sugar beet, sugar cane, tobacco, barley, and oilseeds, Vgazzisa 5 years, alfalfa, rye, millet, safflower, peanut, sweet potato, cassava, coffee, coconut, pineapple, citrus trees, cocoa, tea, banana, avocado, fig, guava, mango, olive, papaya, cashew nut, macadamia , almonds, oats, vegetables, decorative plants and conifers.

Vegetables include, but are not limited to, tomatoes, lettuce, green beans, lima beans, peas, and members of the Sigsit family such as cucumber, muskmelon, and muskmelon. Ornamental plants include, but are not limited to, azaleas, hydrangea, hibiscus, roses, tulips, daffodils, petunias, carnations, buttercups, and chrysanthemums. Preferably, the plants of the present invention are cereals (for example, corn, sorghum, wheat, sunflower, tomato, cruciferous, peppers, potatoes, cotton, rice, soybean, sugar beet, sugar cane, tobacco, barley, oil crops, etc. d.).

The present invention is particularly suitable for any member of the monocot plant family, including but not limited to corn, rice, barley, oats, wheat, sorghum, rye, sugar cane, pineapple, sweet potato, onion, banana, coconut and dates.

Assessment of plant transformation

After the introduction of heterologous foreign DNA into plant cells, the transformation or integration of the heterologous gene into the plant genome is confirmed by various methods, such as the analysis of nucleic acids, proteins and metabolites associated with the integrated gene.

PCR analysis is a rapid method for screening transformed cells, tissue or shoots for the presence of the introduced gene at an earlier stage before transplanting into the soil (Zatrgook apa Kizzei (2001) MoIesshag Siopippo: A I arogayugu Mapiai! briipd Nabog, MU)).

PCR is performed using oligonucleotide primers specific for the gene of interest or for the Adgobasiegicht vector as a background, etc.

Plant transformation can be confirmed by Southern blot analysis of genomic DNA (ZBatrgook apa Kyvze! (2001) above). In general, total DNA is extracted from the transformant, digested with appropriate restriction enzymes, fractionated in an agarose gel, and transferred to a nylon membrane or nitrocellulose. The membrane or "blot" can be further probed, for example, with a fragment of the target DNA labeled with a radioactive isotope ZR, to confirm the integration of the introduced gene into the plant genome according to standard techniques (Zatbgook and Kizzei!, 2001, supra).

In Northern analysis, RNA is isolated from certain transformant tissues, fractionated in an agarose formaldehyde gel, and transferred to a nylon filter according to standard techniques commonly used in the art (Zatgook apa Kizzei! (2001) above). The expression of RNA encoded by 9gd23 or d9gd51 is tested by hybridization of the filter with a radioactive probe obtained from 5OS using methods known in the art (Zatbgook apa Kizzei! (2001) above).

Western blotting and biochemical tests, etc., can be performed on transgenic plants to determine the presence of the protein encoded by the herbicide resistance gene using standard methods. (Zatogook apa Kivzzei (2001) above), using antibodies that bind to one or more epitopes present in the herbicide resistance protein.

The following examples are offered by way of illustration and not limitation.

Experimental part

Example 1: Obtaining ATX213 0 8

ATX 21308 was isolated by inoculating soil samples on Enriched Minimum Nutrient C medium (EMM3) containing phosphates and 50 mM glyphosate. Since EMMZ does not contain any aromatic amino acids, the strain must be resistant to glyphosate to grow on this medium.

Approximately one gram of soil was dissolved in approximately 10 mL of water and vortexed for 5 seconds. 100 μl of this suspension was added to 1 ml of EMMZ3 with phosphate, but without glyphosate. EMMZ3 contains (per liter, pH 7.0): 10 g sucrose, 1 g MNACI, 0.2 g Ma5O4:7HgO, 0.01 g RevO4:7HgO, 0.007 g MazO:HgO and 10 ml of a phosphate solution containing ( per liter, pH 7.0) 210 g of Mag2HRO" and 90 g of Mane" RoOx"x. The culture is shaken in a rotating tissue culture drum at 217C overnight and then plated on EMM3 agar containing 50 mM glyphosate. After three days, the isolate is plated on Ihia Vepapi (IV) agar to confirm the unity of morphology. After six days, a single colony is transferred to EMM3Z agar containing 50 mM glyphosate. The isolate was grown overnight on plates with 50 mM glyphosate. One specific strain, designated ATX21308, was selected due to its ability to grow in the presence of high concentrations of glyphosate. This strain has been tested for growth in the presence of glyphosate in liquid culture and is capable of growing at approximately 300 mM glyphosate under controlled conditions.

Example 2. Preparation and screening of cosmid libraries

Total DNA was obtained from the ATX21308 culture using methods well known in the art. The DNA was partially cleaved with the restriction enzyme ZaizA!1 and ligated with the vector fragment

ByregSboz (Zigaiadepe) according to the manufacturer's instructions. The lithiation products were packaged into phage particles using the SidaRask X/ packaging extract. (5iga(adepe) transfected into E. soybean cells were sown on IV agar containing 50 μg/ml kanamycin for selection of colonies containing cosmids.

Individual colonies were plated into 384-well plates containing IV broth and 50 μg/ml kanamycin and grown to saturation. Cells from these cultures were diluted 1:10, then plated on Mb63 agar plates containing 50 μg/ml kanamycin and either 0 mM, 10 mM, 20 mM, or 50 mM glyphosate.

IAgar medium Mb3 100 mM KNeRO»x, 15 mM (MNag)250x, 50 μM Sasi», 1 μM Reso», 50 μM Masi», 55

MM of glucose, 25 mg/liter of I-proline, 10 mg/liter of thiamine NCI, enough to bring the pH to 7.0, and 15 g/liter of agar! Transformants with faster growth at higher concentrations of glyphosate were isolated and digested with the restriction enzyme Esogi. to identify cosmids with a similar restriction pattern. Several clones have been identified that grow in the presence of glyphosate and have similar Esogie restriction patterns. One of these cosmid clones, pAX1924, was selected for further experiments.

Example 3. Identification of dgd23 in cosmid pAX1924

To identify the gene(s) responsible for the glyphosate resistance demonstrated by cosmid pAX1924, DNA from this clone was mutagenized with mobile elements. This method identified clones that underwent transposon insertions and lost the ability to confer resistance to glyphosate. The location of transposon insertions establishes an open reading frame responsible for the glyphosate resistance phenotype.

Cosmid pAHI924 of ip migo was subjected to transposon mutagenesis using E2::TM Ipsepiop Kii (Erisepige, Madizop, MU) according to the manufacturer's protocol. According to this method, a fragment of a transposon is randomly inserted into the cosmid DNA and thus randomly destroys the function of the genes in the cosmid.

This transposon contains a gene encoding resistance to trimethoprim, so clones with the transposon insertion can be selected for their ability to grow in the presence of this antibiotic. The locations of transposon insertions can be determined by constructing a genetic map of the restriction fragment or by sequencing from primers that anneal to the transposon. Clones pAX1924 with transposon inserts were sown on Mb3 medium containing glyphosate. Many clones containing the transposon were identified that lost the ability to grow in the presence of glyphosate, indicating that the transposon had disrupted the gene responsible for resistance.

The DNA sequence was determined for the region of rakh1!924 containing transposon insertions using sequencing methods well known in the art. Using this sequence information, DNA primers were synthesized and used to determine the pAX1924 DNA sequence of the region containing the transposon insertion. Analysis of the obtained DNA sequences shows that this section contains a binding gene. This gene is designated as dgd23 in this description. Analysis of dgd23 shows that it is capable of producing two possible proteins in bacterial cells due to the presence of potential additional translation start sites. The first OKE (OKR) begins with the TO start codon in positions 109-111 with 5EO I

MO:1, and ends with a TAS stop code near nucleotides 1417-1419 of 5EO IU MO:1. The second OBE (ОБег2) begins with the ATO start codon near nucleotides 178-180 of the 5EO IYU MO/1, and ends with the TAS stop codon near nucleotides 1417-1419 with the BEO IYU MO:1. Translation of OKE1 leads to the amino acid sequence given in ZEO IYUO MO:2. Translation of OKE2 results in the amino acid sequence given in ZEO

IO MO4.

Analysis of the DNA region surrounding dgd23 suggests that OKE2 precedes the ribosome-binding site, whereas it is not clear that the ribosome-binding site precedes the start of OBE1 translation. In addition, alignment of both open reading frames with representative ERBRO enzymes shows that some ERBRO enzymes contain this M-terminal extension encoded within OKE1. Thus, the functional OKR encoded by 9gd23 in bacteria is OKE2. Therefore, as used herein, okOo23 refers to what is encoded by OKE2 (nucleotides 178-1419 5EO IO MO:1). However, it is known in the art that ERBROZ enzymes are quite tolerant to additional amino acids at their M-terminus. Therefore, expression of OKE1 (nucleotides 109-1419 from BEO IO MO 1) should also lead to glyphosate-resistant ERBR5.

To test the ability of OKE2 to function as ERBRB and confer glyphosate resistance in the cell, this open reading frame could be subcloned and expressed in E. soya.

Example 4. Subcloning of adgd23 into vectors for expression in E. soya.

The gene encoding ZKO23 OMKE2 (which starts with ATO (positions 178-180 of 5EO IO MO), which expresses a protein of 413 amino acids), was subcloned into ryC18 and reEB5E1pb using the same cloning strategy outlined above in general. IB PCR primer was synthesized"

САСОССАТССОСАТОСАААСТОАТСОСАСАСТАСТО 3), which adds a Watney site, after which is located a SOC (5'- сОсАТССО(ОС-3) directly from 5 from the start site. The 2nd primer was synthesized

ITATTOaSOSOSSssSTAoSSOoOOSASSOTAAS 3, which added the AusI site directly from 3 from the stop sequence (5-s(0(0(0300-3). The coding region of 9g923 was amplified by PCR using the GRID tm DNA polymerase (5igai(adepe)). After PCR amplification of dgd23, using these primers and cleavage with Watni/AzsiI restriction enzymes, the PCR product was ligated into ryC19 (cleaved

Watni and AzvsiI) and reE5ETr (cleaved by Watni and Avsi), and colonies containing the insert were obtained. Clone risC18-9gd23 (designated herein as pAX1927) was confirmed by restriction enzyme digestion and DNA sequencing.

Similarly, the vector for the expression of pAX1909 was cleaved by Watney and Avsi, and the vector containing the fragment was isolated from the gel using methods well known in the art. pAX1909 is a derivative of REBE-1p6 (Momadep, Zap-Oiedo, SA) modified to contain a VatNi site immediately 3" from the histidine-enriched "Niz-Tad" coding region. Thus, the proteins cloned in pAX1909 are hybrids in-frame containing the additional amino acids MANNNNNNOZO.Vectors such as pAX1909 typically

have been developed for the expression and purification of proteins, and these methods are well known in the art.

The cleaved PCR product obtained above was ligated into the cleaved pAX1909 vector, and colonies containing the insert were obtained. Clone pAX1909-dgd23 (designated herein as pAXI926) was confirmed by restriction enzyme digestion and DNA sequencing. A feature of the pAX1926 construct is that the predicted OKO23 translation product contains an amino-terminal extension consisting of MANNNNNNN. This M-terminal extension includes a "histidine tag" or "5h-Niv" tag, which is used to facilitate purification of the SKO23 protein, which is also well known in the art.

Plasmid rAHI1926, containing 9gd23 OMKE2, was deposited in the Agricultural Research Service (ASR!) Culture Collection on November 18, 2005, and has been assigned an ASR accession number. B-30888.

Example 5. dg523 confers resistance to high levels of glyphosate

The construct pОС18-5гд23 (pАХ1927) was transformed into E. soya strain ОНбо.: and sown on agar plates

And B, supplemented with carbenicillin (0.1 mg/ml). Two colonies were picked, resuspended in sterilized water and plated onto Mb63 plates containing either 0 mM, 25 mM, 50 mM or 100 mM glyphosate. Isopropyl-B-O-thiogalactopyranoside (IPTO; 0.1 mM) was also added to the dishes. As a control, cells containing only one rysC18 vector were transformed and plated on glyphosate plates. After 2 days of growth, these plates were tested for growth (Table 1).

Table 1

PRTYTo PNYA NO ON KON KO NNYA KOKO

This result confirms that the expression of dg9d23 with the formation of 5KO23-OKE2 confers resistance to glyphosate in E. soybean up to at least 100 mm. Additionally, the growth of E. soybeans containing pAX1927 was more pronounced in the presence of glyphosate than in the absence of glyphosate.

Example 6. Homology of OB O23 with other proteins

The deduced amino acid sequence of 5KO23 has homology with ERBR3 enzymes, indicating that dgd23 encodes ERBR5B.

Study of the deduced amino acid sequence of SVO-OKE2 (5EO IU MO:4) shows that it does not contain the four domains typical for Class II EPZR5Z enzymes. In this way, it is a new, non-class II, ERBR5 glyphosate resistance.

A search of publicly available protein databases, such as 5UMZ5RKOT, shows that oKO23 has amino acid similarity to a wide class of EPZR5Z enzymes. However, no protein in all databases has more than 5095 homology with the amino acid sequence C2C23. A representative alignment of okog23 with other EPZRZ enzymes is shown in Figure 1.

Example 7. Purification of KO23

The construct pKZE1p-dgd23 (pAX1926) was expressed in E. soybean after IRTO induction and purified in one step using a cobalt chromatographic column as known in the art. After elution from the column, purified SKO23 was dialyzed against 50 mM HERE5Z/100 mM KS, pH 7.0. The protein was more than 9595 pure as estimated by RACE. The amount of SOKO23 was quantified using the method

Bradford, as known in the art (Vhaagtoga (1976) Apa!. Viospet. 72:248-254).

Example 8 Kinetic tests for OKO23 activity

Purified protein samples were assayed for ЕР5Р5 activity using a kinetic assay involving incubation of РЕР (Zidta, 5. Gotsi5, MO) and 53Р in a buffer containing potassium chloride and НЕРЕ5 at pH 7.0.

The release of phosphate was detected using a double test for fluorescence detection of phosphate based on the formation of Atrieh Kei, as known in the art (Magdpe? ei ai., (2003) Apa!. Biospet. 320:292-298). Published assay conditions may lead to saturation of the analyte in experiments in which phosphate is released very quickly. This saturation slightly limits the dynamic range of the analyte, and requires a certain range of enzyme concentrations. It was determined that the kinetic limitation of the fluorescence assay for phosphate is apparently due to a combination of factors, including limitation of inosine and

RMER. In the present invention, the test conditions were designed in such a way that they led to a significant improvement in the dynamic range and allow a wider range of enzyme and substrate concentrations to be used. Assay conditions that have been significantly changed include concentrations of purine nucleoside phosphorylase (PMP), xanthine oxidase (XOO), AMRIEHP Kea, and inosine, for each of which the assay concentrations were increased to accommodate the higher phosphate turnover rate. This assay was applied to measure ERBR5 activity in a 96-well format with the following improvements:

Table 2

Improved fluorescence test

Improved | Ma?dpne? you ai., y

From news units 225 | 15 | mm

AtrNei| 1100 | 50 | µm

Nerev | 2625 | - | mm ks | 2625 | - | mm pH HH 7 | 74 yav | - | 50 | mm

Enzymatic tests were performed in 9b-well tablets in a total volume of 50 μl. The reactions were carried out at room temperature at pH 7.0. All test components except PEP, ERBRB and 53P were combined in Mawsieg Mich and packaged in separate tubes in a 9b-well plate using a multichannel pipette. Appropriate concentrations of PEP were then added to each well. Fresh breeding

ERBRBs were prepared and added to the corresponding wells. Each test was started with the addition of 5ZR.

The velocity data were plotted and the kinetic parameters Kt and Ksa were determined by applying the Michaelis-Menten Equation using a nonlinear curve processing program (KAGEIU

ASVAARNF, Zupegdu Zoymage). Ki values were determined by measuring Kt (appr) at multiple concentrations of glyphosate, and a plot of Ki (appr) as a function of inhibitor concentration was plotted.

Table C

The influence of glyphosate on the Kp (arr) of ХО2З ny sy sy

By plotting the graph of Kt (arr) as a function of glyphosate concentration, a linear representation of З2О23 resistance to glyphosate can be obtained. The point of intersection of the resulting line with the X axis is -Ki. Construction of this line according to the data from Table C leads to the following values:

Table 4

Kinetic values for OKO23

Ooo23 is very resistant to glyphosate, with K; more than 9 mM, and the K/iKt ratio is more than 800.

Example 9: Isolation of ATX21308

For strain ATX 21313, approximately one gram of soil was suspended in 10 ml of water, and 100 μl of inoculation of 1 ml of culture in mineral nutrient salts medium A (M5MA) without glyphosate was used. MYOMA contains (per 1 liter, pH 7.0) 1 g of MNASI, 10 g of sucrose, 0.2 g of Ma5O4:7 HO, 0.01 g of RebO4:7HgO, 0.007 g of Mpy5O.: HO, supplemented with phosphates. After overnight incubation, the culture was inoculated onto a solid medium containing

M5MA and 50 mM glyphosate, incubated for several days, and inoculated onto Hygia agar plates

Vepapi to confirm a single colony type. Growth in the presence of 50 mM glyphosate was recommended after re-growing on MOMA, 50 mM agar plates. This method of selection led to the strain

ATX21313, which was able to grow well in such conditions.

Example 10. Cloning of glyphosate-resistant EPZR synthases

Genomic DNA was obtained from strain ATX21313, and the obtained DNA was partially digested with the restriction enzyme Zap3zAi to obtain DNA fragments with a size of approximately 5 thousand nucleotide pairs. These DNA molecules were selected by size on an agarose gel, isolated and ligated into "arms"

IAMVOA 2ARF vector, which was previously cleaved by VatNi. The ligated "arms" were then packaged into phage particles, and bacteriophage titers were determined as known in the art. The resulting libraries were amplified using methods known in the art to obtain a library titer between

Zh107 and Zh108 IU/ml. For each independent library, E. soii (X/1 Vipe MER) was then cotransfected with bacteriophage from the amplified library in the same way as M133 with a helper phage to ensure mass excision of the library as infectious, circular olDNA as known in the art (Zpogi her a). (1988) Mysieis Acid5 Nezeagsi 16:7583-7600). After centrifugation of the co-infected cells, the supernatant containing the bacteriophage was heated to 65-707C for 15-20 minutes to inactivate the remaining particles of the lambda phage. Dilution of the obtained old DNA plasmid library was transfected into a fresh competent culture

B. soy cells of HIT Vise MER", as well as X--Vipe MAR (Lago) cells (HIT Vise MKR). The resulting transfected cells were plated on Mb3 dishes containing kanamycin, 0.1 μM IRTO and or 0 mM, 20 mm or 50 mM glyphosate.

This method of screening allows the identification of clones containing glyphosate-tolerant ERBR-synthase, as well as clones carrying tolerance to glyphosate. Colonies growing on 20 mM or 50 mM glyphosate in lago or XI-Vice MER" strains were subcultured and their plasmids were analyzed by restriction digestion to identify plasmids with a common restriction pattern. Individual plasmids were sequenced using methods known in the art technique, with preference given to plasmids that showed resistance to 50 mM glyphosate.

Using this approach, sometimes modified for each library, as is known and appreciated in the art, library clones containing EPZP synthase genes were identified.

The sequences of the regions of the obtained clones were identified as regions of EPOR-synthase.

Example 11. DNA and protein sequences of EPZR-synthase

The DNA sequence of glyphosate-resistant ERBR synthase was determined for pAX1967 using methods known in the art. The DNA sequence of 9g951 is presented in this description as ZEO IU MO:5.

The predicted translation product 9g951 (z3KO51) is presented in this description as ZEO IU MO:6. oKO51 shows 97905 amino acid identity out of 523 (ZEO IO MO:2).

Plasmid pAX1926, containing 9gd23 OMKE2, was deposited in the Agricultural Research Service (ASR!) Culture Collection on November 18, 2005, and has been assigned an IAC accession number. B-30949.

Table 5 summarizes the homology of KO23 and KO51 with other EPZR synthase enzymes.

Table 5

Amino acid identity of ZSKO23-OKE1 and OKO51 with representative Enzyme-EROR5O-enzymes

Fo of identity with | 95 identities from a dream | 7777-7779 dream | 926 02 | 7-2

Example 12. Cloning of new glirosate-resistant EP5P synthases into an E. soybean expression vector

The a9g951 gene contained in pAX1967 was subcloned into the E. soya vector for the expression of reE5E1p (Ipmigodep). The resulting clones were confirmed by DNA sequencing and used to induce dg951 expression in E. soya. The expressed Niv-tagged protein was then purified as known in the art.

Example 13. Resistance to glyphosate EPZR-synthase

Cells containing pAX1967 were plated on Mb3 plates containing antibiotic and either 0 mM or 20 mM glyphosate. Growth was assessed after two days of cultivation at 37°C. It was observed that SKO51 gave E. soybean cells resistance to 20 mM glyphosate (Table 6).

Table 6

Glyphosate screening

Evening! ///-/ HER

Example 14. Construction of 5upagd23 and expression

The sequence of a new gene encoding the OKO23 protein (ZEO IO MO:2; US Patent Application Mo 60/741166, registered December 1, 2005) was designed and synthesized. This sequence is represented as ZEO

IO MO:12. This open reading frame, designated herein as "zupdgd23", was cloned into the PE5E16B expression vector (Ipmigodep) using methods known in the art.

The BZupog9d23 gene encoding OMO23 was cloned into the рыС19 vector to create pАХ748. For amplification of zupdgd23 from pAX748 using MOTA2UMMEF || system (Zigaiadepe) to introduce random mutations into the zupagd23 coding region, PCR primers were used that flanked zupagd23 in this vector. The template was diluted 1:50 in an error-prone PCR reaction, and amplification was performed for 30 cycles. The resulting PCR product was cleaved with WatNi and 595I restriction enzymes, purified from the gel and ligated into the PE5ETB vector to create a library of mutated zupdgd23.

Libraries of mutated zupagd23 were transformed into E. Soya strain VI 217"0OEZ "ag (Ipmigodep). After transformation, individual colonies were sown on 1x Mb63 medium containing 150 mM glyphosate to select clones that retained enzymatic activity and growth stability.

Example 15. Screening for resistance to glyphosate on cups

Library lithiations were transformed into competent cells of E. soybean VI 21" OEZ (Ipmigodep).

Transformations were performed according to the manufacturer's instructions with the following modifications. After incubation for 1 hour at 37"C in BOS medium, the cells were precipitated by centrifugation (5 minutes, 1000x9, 4"C). The cells were washed with 1 ml of Mb3-, centrifuged again, and the supernatant was removed.

The cells were washed a second time with 1 ml of Mb3-- and resuspended in 200 μl of MbZk.

To select mutant SKO23 enzymes conferring resistance to glyphosate in E. soybean, cells were seeded on agar plates with Mb3 medium containing 150 mM glyphosate, 0.05 mM IRTO (isopropyl-beta-

O-thiogalactopyranoside) and 50 μg/ml of kanamycin. Medium Mb3-- 100 mM KNegRO»x, 15 mm (MH.g)250»5, 50 μm

Sasi", 1 µM RebzoO", 50 µM Masi", 55 mM glucose, 25 mg/liter I-proline, 10 mg/liter thiamine NSI, enough

Mahon to bring the pH to 7.0, and 15 g/l agar. Cups were incubated for 36 hours at 37"C.

Individual colonies were transplanted and seeded into 384-well plates. Thus, two 384-well plates were created. A third plate with 384 clones was collected from colonies grown on plates without glyphosate.

Example 16. Isolation and analysis of ZKO23 variants resistant to glyphosate

VI21"0EZ cells transformed with mutagenized 5upgd23 and/or ad9g923 variants were identified by growth on glyphosate plates. Extracts of mutagenized 5updgd23 and dgag23 variants were prepared and tested for improved enzymatic activity. Colonies identified on glyphosate plates were attached to 96-well blocks containing medium II B and were grown to 0.0. about 0.6. IRTO (0.5 mm) was then added and the blocks were incubated overnight at 20°C to induce protein expression. Protein extracts were prepared from cell pellets using POR (Momadep) and Guzopase (Momadep) culture reagents, and enzyme activity in crude lysates was measured after heating the extracts for 30 minutes at 37°C. Extracts with activities greater than two standard deviations above the mean from a series of extracts containing the corresponding control protein (eg, OKO23) were selected for further analysis.

Clones showing increased activity after incubation as crude extracts were grown in 250 ml culture IV and protein expression was induced by IRTO. After induction, mutant ZKO23 protein was purified from each culture by affinity chromatography using cobalt resin (Momadep). Next, the purified proteins were tested for enzymatic activity after heating for 0, 2, 4, and approximately 16 hours at 3776.

Example 17. Improved variants of SKO23

Several clones with improved activity were identified from the DNA library of mutagenized zupdgd23. DNA sequences of clones corresponding to these extracts were determined. Table 7 shows the amino acid substitutions identified in six variants of SKO23 that retained resistance to glyphosate: dg923 (-ЗР1.820) (ZEO IO MO:26) encoding the amino acid sequence OKO23 (IZR1.820) (5EO I MO:27 ); dgd23 (3РИ1Т.В83) (ZEO IU MO:28) encoding the amino acid sequence OKO23 (I ZRI1.83) (ZEO IU MO:29); dagd23 (ZRI.P18) (ZEO IO MO:30), which encodes the amino acid sequence 5KO23 (IZRI1.E18) (ZEO IO MO:31); and dgd23 (-3РИ1.023) 5EO OO MO:31 5EO, which encodes the amino acid sequence of SMKO23 (I ЗР1.023) 5EO I

MO:Z2).

Table 7

Mutations identified in glyphosate-resistant variants of SOKOS23

Clones were grown in 250 ml of culture I B, and protein expression was induced, and the protein was isolated as described above. The purified proteins were then tested for enzymatic activity after heating for 0, 2, and 4 and approximately 16 hours at 37°C. One of the clones, designated "M5", was found to have an increased ratio of its enzymatic activity after prolonged incubation at 37°C ( Table 8). The DNA sequence of this clone was determined, and the gene is defined in this description as 9923 (ase!) (ZEO IO

MO:14). The protein expressed from dgd23 (asei) is labeled CO23 (ACE!1) (ZEO IU MO:15).

Table 8

Half-life of OKO23 (ACE1) compared to OKO23 at elevated temperature

Protein | The half-life at 37"C (hours) oko23 (ACEIT) contains 2 amino acid substitutions compared to the wild-type bileuome of SKO23: A49-1 and 5276-T. The rEBETB vector containing this gene is designated pAX3801. Figure 1 shows the relative resistance OKO23 (ACET) compared to OKO23 at elevated temperatures.

Example 18. Determination of EP5P5 activity of OKO-23 variants

Extracts containing variant white 5023 were tested for EP5P synthase activity as described in US Patent Application Mo. 60/741166, filed December 1, 2005, incorporated herein by reference in its entirety. The tests were carried out in a total volume of 50 μl containing 0.5

MM shikimate-Z-phosphate, 200 μM phosphoenolpyruvate (PEP), 1 U/ml xanthine oxidase, 2 U/ml nucleoside phosphorylase, 2.25 mM inosine, 1 U/ml horseradish peroxidase, 0-2 mM glyphosate, 50 MM NEREZ/JOHN pH 7.0, 100 mm KSI and АМР'ЭФ Ray (Ipmigodep) according to the manufacturer's instructions. Extracts were incubated with all test components except shikimate-3-phosphate for 5 minutes at room temperature, and testing was initiated by adding shikimate-33-phosphate. EP5P-synthase activity was measured using a Zresigat Setipi XP5 fluorescence spectrometer (MoIesshag bupatisv, excitation: 555 nm; emission: 590 nm).

Following complete determination, kinetic parameters were performed on purified protein as previously described (US Patent Application Me 60/741166, filed December 1, 2005), proving the amount of protein determined using the Bradford method as known in the art. For any one concentration of glyphosate, EPOR synthase activity was measured as a function of a wide range of EPOR concentrations. The data were fitted into the Michaelis-Menten equation using the KAGEIJUSASKARNFO software (Bupegdu Zoimage) to determine the Kt (guessed Kt) of EP5P synthase at that concentration of glyphosate. Apparent Kt values were determined at at least 4 concentrations of glyphosate, and Ki EPPR5 for glyphosate were calculated from a plot of apparent Kt versus glyphosate concentration using Eq.

(mlyu(takh); t!-1; t2-1), as is known in the art.

Table 9

Kinetics of OKO23 (ACEIT) in comparison with OKO23 sec Dnyu Gena nu (nM/min/μg)

Example 19. Identification of dgd23 (aseg). otos23 (ACET) contains two amino acid substitutions compared to 523. To determine whether additional substitutions at these positions could further improve activity, a DNA library was obtained, resulting in clones expressing proteins that were preferentially mutated at both positions 49 and 276 023. Glyphosate-resistant clones were selected by growth on glyphosate plates and grown and tested for kinetic properties as described.

Surprisingly, one clone designated herein as agd23 (ace2) (ZEO IO MO:16) encoding the OKO23 (ACE2) protein (ZEO IU MO:17) was identified as having improved thermostability. Sequence

The DNA of 9gd23 (ACE2) showed that OKO23 (ACE2g2) contains a single amino acid substitution (residue 276 of 5KO23 for arginine).

Example 20. Comparison of KO23 and OKOZ51, and mutagenesis of various residues

To evaluate permutations of amino acid sequences, probable from the comparison of amino acid sequences of 5KO23 and OKO51, two libraries were obtained. The first library introduced diversity from the amino acid sequence of 5MKO51 into the coding region of 9gd23 (ase2). The second library introduced diversity from the amino acid sequence of OKO23 (ACE2) into the coding region of agd51.

Clones from the resulting libraries were tested for (1) the ability to confer glyphosate resistance to the cell, and (2) activity after prolonged incubation at 37°C. A total of ten clones were sequenced and analyzed in more detail. One particular clone, identified herein as 9g951.4 (ZEO IU MO:18), which encodes protein 551.4 (5EO IU MO:19), contains several amino acid substitutions relative to KO23 (ACEZ) and relative to 5KO51. Amino acid substitutions present in ZKO51.4 relative to 523 (ACE2 ), were subsequently inserted into the dgd23 (ase2) gene to obtain 9g923 (ase3) (ZEO IU MO:20), which encodes the protein OSKO23 (ASEZ) (ZEO

IO MO:21). OKO23 (ACEZ) shows the highest activity and thermostability compared to OKO23 and oKo23 (ACE2).

Oo23 (ase1) was mutagenized and clones were tested to identify clones expressing variants with improved thermostability and/or activity. One clone, a9gd23 (H5P2.92) (ZEO IU MO:22), encoding OKO23 (I5P2.92) (ZEO IU MO:23), was identified based on its improved kinetic properties. OKO23 (I 5P2. 92), contains three amino acid substitutions relative to zKO23 (ACEI), as shown in the following Table 10.

Table 10

Amino acid substitutions in OKO23 (I 5P2.92)

Amino acid (AA) in oKO23 (I 5P2. 92) relative to aOagZ3 (ACE1

Mutagenesis with oligonucleotides was used to create clones that contain each identified amino acid substitution of OKO23 (I5P2.92) in the coding region of d9gd23 (asez3). The clone was identified as a clone encoding a protein that has improved kinetic properties compared to 5Co23 (ACEZ) and was designated 9gd23 (ACE4) (5EO IO MO:24). The protein encoded by dgd23 (ACE4), designated as SKO23 (ACE4) (5EO IO MO:25), contains a single amino acid substitution relative to O23 (ACEZ) (Valine 101 to phenylalanine). Based on these results, separate oligonucleotide mutagenesis was performed to analyze the kinetics of each possible amino acid substitution at position 101. None of the amino acid substitutions led to additional improvements in kinetic properties compared to 5KO23(ACEZ).

Table 11

Kinetics of improved versions of silver, (nM/min/μg)

Example 21. Construction of d9gd23 or dg951 for plant transformation

The open reading frame (OPEF) of 9gd23 or 9g951 was amplified by PCR from a full-length cDNA template. Nipai restriction sites were added to each end of the OBKE during PCR.

Additionally, the ACC nucleotide sequence was added immediately 5' from the start codon of the gene to increase translation efficiency (Kogak (1987) Mysieis Asii Nezeagsi 15:8125-8148; uovni (1987) Mysieis Asii

Veseagsy 15:6643-6653). The PCR product was cloned and sequenced using methods known in the art to confirm that no mutations were introduced during PCR.

The plasmid containing the dgd23 or dgd51 PCR product was digested with Nipai!, and the fragment containing the intact ORE was isolated. This fragment was cloned into the restriction sites of the NipaiII plasmid pAX200, a vector for expression in plants containing the rice actin promoter (Meigou et al. (1991) Moyes. Sep. Sep. 231:150-160) and the Ripi! terminator. (Ap ei a. (1989) Te Riapi Sei! 1:115-122). The promoter-gene-terminator fragment from this intermediate plasmid was subcloned into plasmid pOV11 (Darap Tobrasso, Ips) to form the final plasmid, for example, pOV11oKko23. rovВ110023 was organized in such a way that 3.91 t.p.n. fragment

DNA containing the construct promoter-dgd23-terminator can be cleaved using the double cleavage of Krpi and Ripei! and used to transform plants by means of aerosol beam injection. The structure of РУОВИ1ОКО23 was verified by restriction digestion and gel electrophoresis, and by sequencing through different cloning linkages.

The plasmid was transferred to Adgobrasiegisht isteiasiep5, strain I BA4404, which also carries the plasmid rev! (Charap Torasso, Ips) using triparental crossing procedures well known in the art and plating in medium containing spectinomycin. Plasmid reVI11oKOo23 carries resistance to sectinomycin, but is a plasmid of a narrow range of hosts and cannot reproduce in Adgobasiegit. Colonies resistant to spectinomycin appear when pOV115O23 is integrated into a plasmid of a wide range of rZVI hosts by homologous recombination. The co-integrated product of reB1 and rev110Ko23 was verified by Southern hybridization. The Adhorasiegisht strain, which carries the co-integrate, is used for the transformation of corn using the RigeiIpigo method (Darap Torasso).

Example 22. Transformation of dg523 or 9g9d51 into plant cells

Corn cobs were harvested 8-12 days after pollination. Embryos were isolated from the cobs, and these embryos, 0.8-1.5 mm in size, were used for transformation. Embryos were plated with the cervical shield side up in a suitable incubation medium, such as YuOM62A55 medium (3.98 g/L

Solfi Mb; 1 ml/l (1000x base solution) Vitamins Mb; 800 mg/l I - asparagine; 100 mg/l Muo-inositol 1.4 g/l I-proline; 100 mg/l of casamic acids; 50 g/l sucrose; 1 ml/l (1 mg/ml of base solution) 2.4-0). However, media and salts other than OMb2A55 are suitable and well known in the art. Embryos were incubated overnight at 25°C in the dark.

The resulting explants were transferred to square wells (30-40 per dish), transferred to osmotic media for 30-45 minutes, then transferred to a radiation dish (see, for example, Publication

PCT Mo MU/O/0138514 and US Patent Mo 5240842).

DNA constructs engineered to express 5KO23 in plant cells were transferred into plant tissue using an aerosol beam catalyst using conditions essentially as described in

Publications PCT Mo M/O/0138514. After irradiation, the embryos were incubated for 30 minutes in osmotic media and placed in incubation media overnight at 257C in the dark. In order to avoid excessive damage to the irradiated explants, they were incubated for at least 24 hours before transfer to recovery medium. The embryos were then distributed in the recovery medium for 5 days at 25"C in the dark, then transferred to the selection medium. The explants were cultured in the selective medium for up to eight weeks, depending on the nature and specifics of the specifically applied selection. After the selection period, the obtained callus was transferred to the medium to mature the embryos until the formation of mature somatic embryos was observed. The resulting mature somatic embryos were then placed under low light, and the regeneration process was initiated using methods known in the art. The resulting shoots were allowed to root in a plant growth medium, and the resulting plants were transferred in nursery pots and propagated as transgenic plants.

Materials

Environment OM62A55

Adjust the pH of the solution to pH 5.8 IM KOH/1M KSI, add sSeigye (Zidta) to 3 g/l and autoclave. After cooling to 50"C, bring to 2 ml/l with a 5 m/ml base solution of silver nitrate (Rpuioespoiodu I arz).

The recipe makes about 20 cups.

Example 23. Transformation of di523 or dg951 into plant cells of corn by means of Adgobracyegiit-mediated transformation.

Heads were harvested 8-12 days after pollination. Embryos were isolated from the cobs, and these embryos, 0.8-1.5 mm in size, were used for transformation. Embryos were plated with the carotid side up in a suitable medium for overnight incubation at 25°C in the dark. However, it is not necessary to culture the embryos overnight. -mediated transmission for 5-10 minutes, then sown on cups with medium for co-cultivation for 3 days (at 25"C in the dark). After co-cultivation, the explants were transferred to medium for a recovery period for five days (at 2570 in the dark). The explants were incubated on a selective medium for up to eight weeks, depending on the nature and specifics of the particular method of selection.

After the selection period, the obtained callus was transferred to the environment for embryo maturation until the formation of mature somatic embryos is observed. The resulting mature somatic embryos were then placed under low light, and the regeneration process was initiated using methods known in the art. The resulting shoots were allowed to root in a plant growth medium, and the resulting plants were transferred to nursery pots and propagated as transgenic plants.

All publications and patent applications mentioned in the description indicate the level of expertise of specialists in the field of technology to which this invention belongs. All publications and patent applications are incorporated herein by reference to the extent that each individual publication or patent application is specifically and individually indicated to be incorporated by reference.

Although the foregoing invention has been described in detail by way of illustration and example for the sake of preferred understanding, it will be apparent that certain changes and modifications may be made within the scope of the appended claims.

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Claims (14)

1. An isolated nucleic acid molecule selected from the group consisting of: a) a nucleic acid molecule that contains the nucleotide sequence 5EO IU MO: 1, 3 or 5, or complementary to it; b) a nucleic acid molecule that contains a nucleotide sequence that has at least 80 9o sequence identity with the nucleotide sequence 5EO IU MO: 1, C or 5, or complementary to such; c) the nucleotide sequence of the herbicide resistance insertion of the plasmid DNA deposited under the ICRC Accession Number B-30888 or B-30949, or complementary to it; 4) a nucleic acid molecule that encodes a polypeptide containing the amino acid sequence 5ХЕО ИЮ МО: 2, 4 or 6; 1 e) a nucleic acid molecule that contains a nucleotide sequence that encodes a polypeptide that has at least 80 90 amino acid sequence identity with the amino acid sequence 5EO IU MO: 2, 4 or 6. 2. An isolated nucleic acid molecule according to item I, where the specified nucleotide sequence is a synthetic sequence designed for expression in a plant. 3. A host cell containing a vector containing a nucleic acid molecule according to claim 1. 4. The host cell according to claim 3, which is a bacterial host cell. 5. The host cell according to claim 3, which is a plant cell. 6. Transformed seed of a plant containing the host cell of claim 5. 7. An isolated polypeptide selected from the group consisting of: a) a polypeptide containing the amino acid sequence 5EO IU MO: 2, 4 or 6; b) polypeptide encoded by the nucleotide sequence 5EO IU MO: 1, 3 or 5; c) a polypeptide containing an amino acid sequence that has at least 80 95 sequence identity with the amino acid sequence 5EBO IU MO: 2, 4 or 6, where the specified polypeptide has herbicide resistance activity; 4) a polypeptide encoded by a nucleotide sequence that is at least 80,905 identical to the nucleotide sequence of 5EO IU MO: 1, C or 5, where the specified polypeptide has herbicide resistance activity; 1, e) of the polypeptide encoded by the nucleotide sequence of the herbicide resistance insertion of the plasmid DNA, deposited under Accession No. ICKI, B-30888 or MEKI, B-30949. 8. Polypeptide according to claim 7, which additionally contains a heterologous amino acid sequence. 9, A plant having a DNA construct stably integrated into its genome containing a nucleotide sequence that encodes a protein having herbicide resistance activity, wherein said nucleotide sequence is selected from the group consisting of: a) a 520 IU MO nucleotide sequence : 1, 3 or 5; b) a nucleotide sequence that has at least 80 90 sequence identity with the nucleotide sequence of 5EO IU MO: 1, 3 or 5, where the specified nucleotide sequence encodes a polypeptide that has herbicide resistance activity; c) a nucleotide sequence that encodes a polypeptide containing the amino acid sequence 5EO IU MO: 2, 4 or 6; 4) a nucleotide sequence that encodes a polypeptide having at least 80 to 90 amino acid sequence identity with the amino acid sequence of 5EO IU MO: 2, 4 or 6, where the specified polypeptide has herbicide resistance activity; 1, e) of the nucleotide sequence of the herbicide resistance insertion of the plasmid DNA deposited under Accession Number MEKI, B-30888 or MEKI, B-30949; where the indicated nucleotide sequence is operably linked to a promoter controlling the expression of the coding sequence in a plant cell. 10. The plant according to claim 9, where the specified plant is a plant cell. 11. A plant having a DNA construct stably integrated into its genome comprising a nucleotide sequence encoding an EP5P5 polypeptide, wherein said EP5P5 polypeptide has a Kt to PEP ratio of from about 1 to about 150 µ, 1 Ki (glyphosate)/Kt ( PEP) from about 500 to about 1000, where said plant exhibits resistance to glyphosate herbicide. 12. The plant according to claim 11, wherein said plant is a soybean plant. 13. The plant according to claim 11, where the specified plant is a grain plant. 14. The plant according to claim 11, where said plant is selected from the group consisting of corn, sorghum, wheat, sunflower, tomato, cruciferous, peppers, potato, cotton, rice, soybean, sugar beet, sugar cane, tobacco, barley and oil crops.