FliO Regulation of FliP in the Formation of the Salmonella enterica Flagellum 英文参考文献.docVIP

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FliO Regulation of FliP in the Formation of the Salmonella enterica Flagellum 英文参考文献.doc

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FliO Regulation of FliP in the Formation of the Salmonella enterica Flagellum 英文参考文献

FliORegulationofFliPintheFormationofthe SalmonellaentericaFlagellum CliveS.Barker1,IrinaV.Meshcheryakova1,AllaS.Kostyukova2,FadelA.Samatey1* 1Trans-MembraneTraffickingUnit,OkinawaInstituteofScienceandTechnology,Okinawa,Japan,2DepartmentofNeuroscienceandCellBiology,RobertWoodJohnson MedicalSchool,Piscataway,NewJersey,UnitedStatesofAmerica Abstract ThetypeIIIsecretionsystemoftheSalmonellaflagellumconsistsof6integralmembraneproteins:FlhA,FlhB,FliO,FliP,FliQ, andFliR.However,insomeothertypeIIIsecretionsystems,ahomologueofFliOisapparentlyabsent,suggestingithasa specializedrole.DeletingthefliOgenefromthechromosomeofamotilestrainofSalmonellaresultedinadrasticdecrease of motility. Incubation of the DfliO mutant strain in motility agar, gave rise to pseudorevertants containing extragenic bypass mutations in FliP at positions R143H or F190L. Using membrane topology prediction programs, and alkaline phosphatase or GFPuv chimeric protein fusions into the FliO protein, we demonstrated that FliO is bitopic with its N- terminusintheperiplasmandC-terminusinthecytoplasm.TruncationanalysisofFliOdemonstratedthatoverexpressionof FliO43–125 orFliO1–95wasabletorescuemotilityoftheDfliOmutant.Further,residueleucine91inthecytoplasmicdomain wasidentifiedtobeimportantforfunction.Basedonsecondarystructureprediction,thecytoplasmicdomain,FliO43–125 , should contain beta-structure and alpha-helices. FliO43–125-Ala was purified and studied using circular dichroism spectroscopy; however, this domain was disordered, and its structure was a mixture of beta-sheet and random coil. Coexpressionoffull-lengthFliOwithFliPincreasedexpressionlevelsofFliP,butcoexpressionwiththecytoplasmicdomain ofFliOdidnotenhanceFliPexpressionlevels.OverexpressionofthecytoplasmicdomainofFliOfurtherrescuedmotilityof strains deleted for the fliO gene expressing bypass mutations in FliP. These results suggest FliO maintains FliP stability through transmembrane domain interaction. The results also demonstrate that the cytopla