Genome-based identification and analysis of collagen-related structural motifs in bacterial and viral proteins.
(2003) In Journal of Biological Chemistry 278(34). p.32313-32316- Abstract
- Collagens are extended trimeric proteins composed of the repetitive sequence glycine-X-Y. A (c) under bar ollagen- related (S) under bar tructural (m) under bar otif (CSM) containing glycine-X-Y repeats is also found in numerous proteins often referred to as collagen-like proteins. Little is known about CSMs in bacteria and viruses, but the occurrence of such motifs has recently been demonstrated. Moreover, bacterial CSMs form collagen-like trimers, even though these organisms cannot synthesize hydroxyproline, a critical residue for the stability of the collagen triple helix. Here we present 100 novel proteins of bacteria and viruses (including bacteriophages) containing CSMs identified by in silico analyses of genomic sequences. These... (More)
- Collagens are extended trimeric proteins composed of the repetitive sequence glycine-X-Y. A (c) under bar ollagen- related (S) under bar tructural (m) under bar otif (CSM) containing glycine-X-Y repeats is also found in numerous proteins often referred to as collagen-like proteins. Little is known about CSMs in bacteria and viruses, but the occurrence of such motifs has recently been demonstrated. Moreover, bacterial CSMs form collagen-like trimers, even though these organisms cannot synthesize hydroxyproline, a critical residue for the stability of the collagen triple helix. Here we present 100 novel proteins of bacteria and viruses (including bacteriophages) containing CSMs identified by in silico analyses of genomic sequences. These CSMs differ significantly from human collagens in amino acid content and distribution; bacterial and viral CSMs have a lower proline content and a preference for proline in the X position of GXY triplets. Moreover, the CSMs identified contained more threonine than collagens, and in 17 of 53 bacterial CSMs threonine was the dominating amino acid in the Y position. Molecular modeling suggests that threonines in the Y position make direct hydrogen bonds to neighboring backbone carbonyls and thus substitute for hydroxyproline in the stabilization of the collagen-like triple-helix of bacterial CSMs. The majority of the remaining CSMs were either rich in proline or rich in charged residues. The bacterial proteins containing a CSM that could be functionally annotated were either surface structures or spore components, whereas the viral proteins generally could be annotated as structural components of the viral particle. The limited occurrence of CSMs in eubacteria and lower eukaryotes and the absence of CSMs in archaebacteria suggests that DNA encoding CSMs has been transferred horizontally, possibly from multicellular organisms to bacteria. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/116102
- author
- Rasmussen, Magnus LU ; Jacobsson, Micael and Björck, Lars LU
- organization
- publishing date
- 2003
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 278
- issue
- 34
- pages
- 32313 - 32316
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- wos:000184782100108
- scopus:0042357053
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M304709200
- language
- English
- LU publication?
- yes
- id
- f944839d-43d6-4c4b-a118-ca9d3a285951 (old id 116102)
- alternative location
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12788919&dopt=Abstract
- date added to LUP
- 2016-04-01 11:55:24
- date last changed
- 2022-04-28 22:01:19
@article{f944839d-43d6-4c4b-a118-ca9d3a285951,
abstract = {{Collagens are extended trimeric proteins composed of the repetitive sequence glycine-X-Y. A (c) under bar ollagen- related (S) under bar tructural (m) under bar otif (CSM) containing glycine-X-Y repeats is also found in numerous proteins often referred to as collagen-like proteins. Little is known about CSMs in bacteria and viruses, but the occurrence of such motifs has recently been demonstrated. Moreover, bacterial CSMs form collagen-like trimers, even though these organisms cannot synthesize hydroxyproline, a critical residue for the stability of the collagen triple helix. Here we present 100 novel proteins of bacteria and viruses (including bacteriophages) containing CSMs identified by in silico analyses of genomic sequences. These CSMs differ significantly from human collagens in amino acid content and distribution; bacterial and viral CSMs have a lower proline content and a preference for proline in the X position of GXY triplets. Moreover, the CSMs identified contained more threonine than collagens, and in 17 of 53 bacterial CSMs threonine was the dominating amino acid in the Y position. Molecular modeling suggests that threonines in the Y position make direct hydrogen bonds to neighboring backbone carbonyls and thus substitute for hydroxyproline in the stabilization of the collagen-like triple-helix of bacterial CSMs. The majority of the remaining CSMs were either rich in proline or rich in charged residues. The bacterial proteins containing a CSM that could be functionally annotated were either surface structures or spore components, whereas the viral proteins generally could be annotated as structural components of the viral particle. The limited occurrence of CSMs in eubacteria and lower eukaryotes and the absence of CSMs in archaebacteria suggests that DNA encoding CSMs has been transferred horizontally, possibly from multicellular organisms to bacteria.}},
author = {{Rasmussen, Magnus and Jacobsson, Micael and Björck, Lars}},
issn = {{1083-351X}},
language = {{eng}},
number = {{34}},
pages = {{32313--32316}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{Genome-based identification and analysis of collagen-related structural motifs in bacterial and viral proteins.}},
url = {{http://dx.doi.org/10.1074/jbc.M304709200}},
doi = {{10.1074/jbc.M304709200}},
volume = {{278}},
year = {{2003}},
}