VrrA mediates Hfq-dependent regulation of OmpT synthesis in Vibrio cholerae

J Mol Biol. 2010 Jul 23;400(4):682-8. doi: 10.1016/j.jmb.2010.05.061. Epub 2010 Jun 2.

Abstract

OmpT, an outer membrane porin of Vibrio cholerae, is tightly regulated by the organism in response to different environments. Two transcriptional regulators, cAMP receptor protein (CRP) and ToxR, compete at the ompT promoter region. CRP activates ompT transcription by a loop-forming mechanism, while ToxR functions as an antiactivator and repressor, depending on its interplay with CRP. VrrA, a 140-nt small noncoding RNA in V. cholerae, is controlled by the alternative sigma factor sigma(E). We have demonstrated previously that VrrA represses ompA translation by base-pairing with the 5' region of the mRNA, thereby affecting the release of outer membrane vesicles and modulating the colonization ability of V. cholerae. In this study, we demonstrate that VrrA RNA represses ompT translation by base-pairing with the 5' region of the mRNA and that regulation requires the RNA chaperone protein Hfq. These results add new insight into the regulation of OmpT. In addition to pH/temperature signals via the ToxR regulon and carbon source signals via the cAMP-CRP complex, OmpT is further regulated by signals received via the sigma(E) regulon through VrrA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 5' Untranslated Regions / genetics
  • Bacterial Proteins / biosynthesis*
  • Base Pairing
  • Gene Expression Regulation, Bacterial*
  • Host Factor 1 Protein / metabolism*
  • Porins / biosynthesis*
  • RNA, Bacterial / metabolism*
  • RNA, Untranslated / metabolism*
  • Vibrio cholerae / physiology*

Substances

  • 5' Untranslated Regions
  • Bacterial Proteins
  • Host Factor 1 Protein
  • Porins
  • RNA, Bacterial
  • RNA, Untranslated
  • ompT protein, bacteria