Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 291, Issue 50, Pages 26151-26163Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M116.751933
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- Centre National de la Recherche Scientifique
- Aix-Marseille Universite
- Ministere de l'enseignement superieur et de la recherche fellowship
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Here, we show that a partner-switching system of the aquatic Proteobacterium Shewanella oneidensis regulates post-translationally sigma(S) (also called RpoS), the general stress response sigma factor. Genes SO2118 and SO2119 encode CrsA and CrsR, respectively. CrsR is a three-domain protein comprising a receiver, a phosphatase, and a kinase/anti-sigma domains, and CrsA is an anti-sigma antagonist. In vitro, CrsR sequesters sigma(S) and possesses kinase and phosphatase activities toward CrsA. In turn, dephosphorylated CrsA binds the anti-sigma domain of CrsR to allow the release of sigma(S). This study reveals a novel pathway that post-translationally regulates the general stress response sigma factor differently than what was described for other proteobacteria like Escherichia coli. We argue that this pathway allows probably a rapid bacterial adaptation.
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