Europe PMC
Nothing Special   »   [go: up one dir, main page]

Europe PMC requires Javascript to function effectively.

Either your web browser doesn't support Javascript or it is currently turned off. In the latter case, please turn on Javascript support in your web browser and reload this page.

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our privacy notice and cookie policy.

Proposed acquisition of an animal protein domain by bacteria.

Author information

Affiliations

  • 1. European Molecular Biology Laboratory, Heidelberg, Federal Republic of Germany.
      Authors
    • Bork P 1
    (1 author)

ORCIDs linked to this article

Proceedings of the National Academy of Sciences of the United States of America, 01 Oct 1992, 89(19):8990-8994
https://doi.org/10.1073/pnas.89.19.8990 PMID: 1409594 PMCID: PMC50050

Free full text in Europe PMC

Abstract 

A systematic screen of a protein sequence data base confirms that the fibronectin type III (Fn3) domain is widely distributed among animal proteins and occurs also in several bacterial carbohydrate-splitting enzymes. The motif has yet to be identified in proteins from plants or fungi. All indications are that the bacterial sequences are much too similar to the animal type to be the result of conventional vertical descent. Rather, it is likely that the bacterial units were initially acquired from an animal source and are being spread further by horizontal transfers between distantly related bacteria.

Free full text 

Logo of pnasLink to Publisher's site
Proc Natl Acad Sci U S A. 1992 Oct 1; 89(19): 8990–8994.
PMCID: PMC50050
PMID: 1409594

Proposed acquisition of an animal protein domain by bacteria.

P Bork and R F Doolittle
Author information Copyright and License information Disclaimer

Abstract

A systematic screen of a protein sequence data base confirms that the fibronectin type III (Fn3) domain is widely distributed among animal proteins and occurs also in several bacterial carbohydrate-splitting enzymes. The motif has yet to be identified in proteins from plants or fungi. All indications are that the bacterial sequences are much too similar to the animal type to be the result of conventional vertical descent. Rather, it is likely that the bacterial units were initially acquired from an animal source and are being spread further by horizontal transfers between distantly related bacteria.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (1.0M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.
 
icon of scanned page 8990
8990
icon of scanned page 8991
8991
icon of scanned page 8992
8992
icon of scanned page 8993
8993
icon of scanned page 8994
8994
 

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Bork P. Shuffled domains in extracellular proteins. FEBS Lett. 1991 Jul 29;286(1-2):47–54. [Abstract] [Google Scholar]
  • Patthy L. Homology of a domain of the growth hormone/prolactin receptor family with type III modules of fibronectin. Cell. 1990 Apr 6;61(1):13–14. [Abstract] [Google Scholar]
  • Bazan JF. Structural design and molecular evolution of a cytokine receptor superfamily. Proc Natl Acad Sci U S A. 1990 Sep;87(18):6934–6938. [Europe PMC free article] [Abstract] [Google Scholar]
  • Watanabe T, Suzuki K, Oyanagi W, Ohnishi K, Tanaka H. Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its evolutionary relationship to Serratia chitinase and to the type III homology units of fibronectin. J Biol Chem. 1990 Sep 15;265(26):15659–15665. [Abstract] [Google Scholar]
  • Gilkes NR, Henrissat B, Kilburn DG, Miller RC, Jr, Warren RA. Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families. Microbiol Rev. 1991 Jun;55(2):303–315. [Europe PMC free article] [Abstract] [Google Scholar]
  • Bairoch A, Boeckmann B. The SWISS-PROT protein sequence data bank. Nucleic Acids Res. 1991 Apr 25;19 (Suppl):2247–2249. [Europe PMC free article] [Abstract] [Google Scholar]
  • Bork P, Grunwald C. Recognition of different nucleotide-binding sites in primary structures using a property-pattern approach. Eur J Biochem. 1990 Jul 31;191(2):347–358. [Abstract] [Google Scholar]
  • Bork P, Sander C, Valencia A. An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7290–7294. [Europe PMC free article] [Abstract] [Google Scholar]
  • Gribskov M, McLachlan AD, Eisenberg D. Profile analysis: detection of distantly related proteins. Proc Natl Acad Sci U S A. 1987 Jul;84(13):4355–4358. [Europe PMC free article] [Abstract] [Google Scholar]
  • Lasters I, Wodak SJ, Alard P, van Cutsem E. Structural principles of parallel beta-barrels in proteins. Proc Natl Acad Sci U S A. 1988 May;85(10):3338–3342. [Europe PMC free article] [Abstract] [Google Scholar]
  • Sander C, Schneider R. Database of homology-derived protein structures and the structural meaning of sequence alignment. Proteins. 1991;9(1):56–68. [Abstract] [Google Scholar]
  • Feng DF, Doolittle RF. Progressive sequence alignment as a prerequisite to correct phylogenetic trees. J Mol Evol. 1987;25(4):351–360. [Abstract] [Google Scholar]
  • Needleman SB, Wunsch CD. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J Mol Biol. 1970 Mar;48(3):443–453. [Abstract] [Google Scholar]
  • Doolittle RF. Stein and Moore Award address. Reconstructing history with amino acid sequences. Protein Sci. 1992 Feb;1(2):191–200. [Europe PMC free article] [Abstract] [Google Scholar]
  • Feng DF, Doolittle RF. Progressive alignment and phylogenetic tree construction of protein sequences. Methods Enzymol. 1990;183:375–387. [Abstract] [Google Scholar]
  • Doolittle RF, Feng DF. Nearest neighbor procedure for relating progressively aligned amino acid sequences. Methods Enzymol. 1990;183:659–669. [Abstract] [Google Scholar]
  • Fitch WM. Distinguishing homologous from analogous proteins. Syst Zool. 1970 Jun;19(2):99–113. [Abstract] [Google Scholar]
  • Meinke A, Braun C, Gilkes NR, Kilburn DG, Miller RC, Jr, Warren RA. Unusual sequence organization in CenB, an inverting endoglucanase from Cellulomonas fimi. J Bacteriol. 1991 Jan;173(1):308–314. [Europe PMC free article] [Abstract] [Google Scholar]
  • Saito T, Suzuki K, Yamamoto J, Fukui T, Miwa K, Tomita K, Nakanishi S, Odani S, Suzuki J, Ishikawa K. Cloning, nucleotide sequence, and expression in Escherichia coli of the gene for poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis. J Bacteriol. 1989 Jan;171(1):184–189. [Europe PMC free article] [Abstract] [Google Scholar]
  • He SY, Collmer A. Molecular cloning, nucleotide sequence, and marker exchange mutagenesis of the exo-poly-alpha-D-galacturonosidase-encoding pehX gene of Erwinia chrysanthemi EC16. J Bacteriol. 1990 Sep;172(9):4988–4995. [Europe PMC free article] [Abstract] [Google Scholar]
  • Melasniemi H, Paloheimo M, Hemiö L. Nucleotide sequence of the alpha-amylase-pullulanase gene from Clostridium thermohydrosulfuricum. J Gen Microbiol. 1990 Mar;136(3):447–454. [Abstract] [Google Scholar]
  • Candussio A, Schmid G, Böck A. Biochemical and genetic analysis of a maltopentaose-producing amylase from an alkaliphilic gram-positive bacterium. Eur J Biochem. 1990 Jul 20;191(1):177–185. [Abstract] [Google Scholar]
  • Pereira ME, Mejia JS, Ortega-Barria E, Matzilevich D, Prioli RP. The Trypanosoma cruzi neuraminidase contains sequences similar to bacterial neuraminidases, YWTD repeats of the low density lipoprotein receptor, and type III modules of fibronectin. J Exp Med. 1991 Jul 1;174(1):179–191. [Europe PMC free article] [Abstract] [Google Scholar]
  • Guiseppi A, Aymeric JL, Cami B, Barras F, Creuzet N. Sequence analysis of the cellulase-encoding celY gene of Erwinia chrysanthemi: a possible case of interspecies gene transfer. Gene. 1991 Sep 30;106(1):109–114. [Abstract] [Google Scholar]
  • Médigue C, Rouxel T, Vigier P, Hénaut A, Danchin A. Evidence for horizontal gene transfer in Escherichia coli speciation. J Mol Biol. 1991 Dec 20;222(4):851–856. [Abstract] [Google Scholar]
  • de Vos AM, Ultsch M, Kossiakoff AA. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science. 1992 Jan 17;255(5042):306–312. [Abstract] [Google Scholar]
  • Baron M, Main AL, Driscoll PC, Mardon HJ, Boyd J, Campbell ID. 1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin. Biochemistry. 1992 Feb 25;31(7):2068–2073. [Abstract] [Google Scholar]
  • Ryu SE, Kwong PD, Truneh A, Porter TG, Arthos J, Rosenberg M, Dai XP, Xuong NH, Axel R, Sweet RW, et al. Crystal structure of an HIV-binding recombinant fragment of human CD4. Nature. 1990 Nov 29;348(6300):419–426. [Europe PMC free article] [Abstract] [Google Scholar]
  • Holmgren A, Bränden CI. Crystal structure of chaperone protein PapD reveals an immunoglobulin fold. Nature. 1989 Nov 16;342(6247):248–251. [Abstract] [Google Scholar]
Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

Full text links 

Read article at publisher's site: https://doi.org/10.1073/pnas.89.19.8990

Read article for free, from open access legal sources, via Unpaywall: https://www.pnas.org/content/pnas/89/19/8990.full.pdfUnpaywall

Citations & impact 

Impact metrics

138
Citations
Jump to Citations
5
Data citations
Jump to Data

Citations of article over time

Alternative metrics

Altmetric item for https://www.altmetric.com/details/3426102
Altmetric
Discover the attention surrounding your research
https://www.altmetric.com/details/3426102

Smart citations by scite.ai
Smart citations by scite.ai include citation statements extracted from the full text of the citing article. The number of the statements may be higher than the number of citations provided by EuropePMC if one paper cites another multiple times or lower if scite has not yet processed some of the citing articles.
Explore citation contexts and check if this article has been supported or disputed.
https://scite.ai/reports/10.1073/pnas.89.19.8990

Supporting
Mentioning
Contrasting
3
195
0

Article citations

Go to all (138) article citations

Other citations

Data 

Similar Articles 

To arrive at the top five similar articles we use a word-weighted algorithm to compare words from the Title and Abstract of each citation.