Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Statistics
  • Help & Advice
University of Warwick

The Library

  • Login

The vbs genes that direct synthesis of the siderophore vicibactin in Rhizobium leguminosarum: their expression in other genera requires ECF sigma factor Rpol

Tools
- Tools
+ Tools

UNSPECIFIED (2002) The vbs genes that direct synthesis of the siderophore vicibactin in Rhizobium leguminosarum: their expression in other genera requires ECF sigma factor Rpol. MOLECULAR MICROBIOLOGY, 44 (5). pp. 1153-1166. ISSN 0950-382X

Full text not available from this repository.

Abstract

A cluster of eight genes, vbsGSO , vbsADL , vbsC and vbsP , are involved in the synthesis of vicibactin, a cyclic, trihydroxamate siderophore made by the symbiotic bacterium Rhizobium leguminosarum . None of these vbs genes was required for symbiotic N-2 fixation on peas or Vicia . Transcription of vbsC , vbsGSO and vbsADL (but not vbsP ) was enhanced by growth in low levels of Fe. Transcription of vbsGSO and vbsADL , but not vbsP or vbsC , required the closely linked gene rpoI , which encodes an ECF sigma factor of RNA polymerase. Transfer of the cloned vbs genes, plus rpoI , to Rhodobacter , Paracoccus and Sinorhizobium conferred the ability to make vicibactin on these other genera. We present a biochemical genetic model of vicibactin synthesis, which accommodates the phenotypes of different vbs mutants and the homologies of the vbs gene products. In this model, VbsS, which is similar to many non-ribosomal peptide synthetase multienzymes, has a central role. It is proposed that VbsS activates L-N (5) -hydroxyornithine via covalent attachment as an acyl thioester to a peptidyl carrier protein domain. Subsequent VbsA-catalysed acylation of the hydroxyornithine, followed by VbsL-mediated epimerization and acetylation catalysed by VbsC, yields the vicibactin subunit, which is then trimerized and cyclized by the thioesterase domain of VbsS to give the completed siderophore.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Q Science > QR Microbiology
Journal or Publication Title: MOLECULAR MICROBIOLOGY
Publisher: BLACKWELL PUBLISHING LTD
ISSN: 0950-382X
Date: June 2002
Volume: 44
Number: 5
Number of Pages: 14
Page Range: pp. 1153-1166
Publication Status: Published
URI: http://wrap.warwick.ac.uk/id/eprint/10911

Data sourced from Thomson Reuters' Web of Knowledge

Request changes to a record

Actions (login required)

View Item View Item
twitter

Email us: publications@warwick.ac.uk
Contact Details
About Us