Disulfide Bond Formation and ToxR Activity in Vibrio cholerae 英文参考文献.docVIP

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Disulfide Bond Formation and ToxR Activity in Vibrio cholerae 英文参考文献.doc

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Disulfide Bond Formation and ToxR Activity in Vibrio cholerae 英文参考文献

DisulfideBondFormationandToxRActivityinVibrio cholerae VeraH.I.Fengler,EvaC.Boritsch,SarahTutz,AndreaSeper,HannaEbner,SandroRoier,StefanSchild, JoachimReidl* InstituteofMolecularBiosciences,UniversityofGraz,Humboldtstrasse,Graz,Austria Abstract VirulencefactorproductioninVibriocholeraeiscomplex,withToxRSbeinganimportantpartoftheregulatorycascade. Additionally, ToxR is the transcriptional regulator for the genes encoding the major outer membrane porins OmpU and OmpT.ToxRisatransmembraneproteinandcontainstwocysteineresiduesintheperiplasmicdomain.Thisstudyaddresses theinfluenceofthethiol-disulfideoxidoreductasesystemDsbAB,ToxRcysteineresiduesandToxR/ToxSinteractiononToxR activity.TheresultsshowthatporinproductioncorrelateswithToxRintrachaindisulfidebondformation,whichdependson DsbAB.Incontrast,formationofToxRintrachainorinterchaindisulfidebondsisdispensableforvirulencefactorproduction andinvivocolonization.ThisstudyfurtherrevealsthatintheabsenceofToxS,ToxRinterchaindisulfidebondformationis facilitated, whereat cysteinyl dependent homo- and oligomerization of ToxR is suppressed if ToxS is coexpressed. In summary,newinsightsintogeneregulationbyToxRarepresented,demonstratingamechanismbywhichToxRactivityis linkedtoaDsbABdependentintrachaindisulfidebondformation. Citation:FenglerVHI,BoritschEC,TutzS,SeperA,EbnerH,etal.(2012)DisulfideBondFormationandToxRActivityinVibriocholerae.PLoSONE7(10):e47756. doi:10.1371/journal.pone.0047756 Editor:MichaelHensel,UniversityofOsnabrueck,Germany ReceivedAugust2,2012;AcceptedSeptember20,2012;PublishedOctober29,2012 Copyright: ? 2012 Fengler et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricteduse,distribution,andreproductioninanymedium,providedtheoriginalauthorandsourcearecredited. Funding:ThisworkwassupportedbytheAustrianScienceFund(FWF)W901(DKMolecularEnzymology)toVHIF,AS,SR,SSandJRandbytheGermanResearch Foundation(DFG)Re1561/4-1.Thefundershadnoroleinst