Disulfide bond formation and ToxR activity in Vibrio cholerae.
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ABSTRACT:
SUBMITTER: Fengler VH
PROVIDER: S-EPMC3483227 | biostudies-literature | 2012
REPOSITORIES: biostudies-literature
Publications
Disulfide bond formation and ToxR activity in Vibrio cholerae.
Fengler Vera H I VH Boritsch Eva C EC Tutz Sarah S Seper Andrea A Ebner Hanna H Roier Sandro S Schild Stefan S Reidl Joachim J
PloS one 20121029 10
Virulence factor production in Vibrio cholerae is complex, with ToxRS being an important part of the regulatory cascade. Additionally, ToxR is the transcriptional regulator for the genes encoding the major outer membrane porins OmpU and OmpT. ToxR is a transmembrane protein and contains two cysteine residues in the periplasmic domain. This study addresses the influence of the thiol-disulfide oxidoreductase system DsbAB, ToxR cysteine residues and ToxR/ToxS interaction on ToxR activity. The resul ...[more]
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