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          Document History for Document ID 439728

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Document Version Version Comment Date Status
439728.0 [No comment] 14.08.2012 15:28 Released

ID: 439728.0, MPI für Infektionsbiologie / RNA Biology
Acid stress activation of the sigma(E) stress response in Salmonella enterica serovar Typhimurium
Authors:Muller, Cécile; Bang, Iel-Soo; Velayudhan, Jyoti; Karlinsey, Joyce; Papenfort, Kai; Vogel, Jörg; Fang, Ferric C.
Language:English
Date of Publication (YYYY-MM-DD):2009-03
Title of Journal:Molecular Microbiology
Volume:71
Issue / Number:5
Start Page:1228
End Page:1238
Review Status:Peer-review
Audience:Experts Only
Abstract / Description:The alternative sigma factor sigma(E) is activated by unfolded outer membrane proteins (OMPs) and plays an essential role in Salmonella pathogenesis. The canonical pathway of sigma(E) activation in response to envelope stress involves sequential proteolysis of the anti-sigma factor RseA by the PDZ proteases DegS and RseP. Here we show that sigma(E) in Salmonella enterica sv. Typhimurium can also be activated by acid stress. A sigma(E)-deficient mutant exhibits increased susceptibility to acid pH and reduced survival in an acidified phagosomal vacuole. Acid activation of sigma(E)-dependent gene expression is independent of the unfolded OMP signal or the DegS protease but requires processing of RseA by RseP. The RseP PDZ domain is indispensable for acid induction, suggesting that acid stress may disrupt an inhibitory interaction between RseA and the RseP PDZ domain to allow RseA proteolysis in the absence of antecedent action of DegS. These observations demonstrate a novel environmental stimulus and activation pathway for the sigma(E) regulon that appear to be critically important during Salmonella-host cell interactions.
Free Keywords:ESCHERICHIA-COLI; PDZ DOMAIN; ANTIOXIDANT DEFENSES; RSEA; PROTEASE;; YAEL; DEGS; PROTEOLYSIS; RPOE; ACIDIFICATION
Comment of the Author/Creator:This work was supported by a grant from the National Institutes of Health (AI44486) and a grant from the Korea Research Foundation (KRF-2008-314-C00328).
External Publication Status:published
Document Type:Article
Communicated by:Hilmar Fünning
Affiliations:MPI für Infektionsbiologie/RNA Biology
External Affiliations:Departments of Laboratory Medicine and Microbiology, University of Washington School of Medicine, Seattle, WA 98195-7242, USA.
Identifiers:ISSN:0950-382X %R 10.1111/j.1365-2958.2009.06597.x [ID No:1]
ISI:000263522000013 [ID No:2]
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