| Literature DB >> 27810894 |
Sophie Bouillet1, Olivier Genest1, Cécile Jourlin-Castelli1, Michel Fons1, Vincent Méjean1, Chantal Iobbi-Nivol2.
Abstract
Here, we show that a partner-switching system of the aquatic Proteobacterium Shewanella oneidensis regulates post-translationally σS (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 σS and possesses kinase and phosphatase activities toward CrsA. In turn, dephosphorylated CrsA binds the anti-sigma domain of CrsR to allow the release of σS 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.Entities:
Keywords: bacteria; bacterial protein kinase; bacterial protein phosphatase; protein-protein interaction; stress response
Mesh:
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Year: 2016 PMID: 27810894 PMCID: PMC5207083 DOI: 10.1074/jbc.M116.751933
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157