A Response Regulator Interfaces between the Frz Chemosensory System and the MglAMglB GTPaseGAP Module to Regulate Polarity in Myxococcus xanthus 英文参考文献.docVIP

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A Response Regulator Interfaces between the Frz Chemosensory System and the MglAMglB GTPaseGAP Module to Regulate Polarity in Myxococcus xanthus 英文参考文献.doc

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A Response Regulator Interfaces between the Frz Chemosensory System and the MglAMglB GTPaseGAP Module to Regulate Polarity in Myxococcus xanthus 英文参考文献

AResponseRegulatorInterfacesbetweentheFrz ChemosensorySystemandtheMglA/MglBGTPase/GAP ModuletoRegulatePolarityinMyxococcusxanthus DanielaKeilberg,KristinWuichet,FlorianDrescher,LotteS?gaard-Andersen* DepartmentofEcophysiology,MaxPlanckInstituteforTerrestrialMicrobiology,Marburg,Germany Abstract Howcellsestablishanddynamicallychangepolarityaregeneralquestionsincellbiology.Cellsoftherod-shapedbacterium Myxococcus xanthus moveon surfaces with defined leadingandlagging cell poles. Occasionally, cells undergo reversals, whichcorrespondtoaninversionoftheleading-laggingpolepolarityaxis.ReversalsareinducedbytheFrzchemosensory system and depend on relocalization of motility proteins between the poles. The Ras-like GTPase MglA localizes to and definestheleadingcellpoleintheGTP-boundform.MglB,thecognateMglAGTPaseactivatingprotein,localizestoand definesthelaggingpole.Duringreversals,MglA-GTPandMglBswitchpolesand,therefore,dynamicallylocalizedmotility proteinsswitchpoles.WeidentifiedtheRomRresponseregulator,whichlocalizesinabipolarasymmetricpatternwitha largeclusteratthelaggingpole,asimportantformotilityandreversals.WeshowthatRomRinteractsdirectlywithMglA and MglB in vitro. Furthermore, RomR, MglA, and MglB affect the localization of each other in all pair-wise directions, suggestingthatRomRstimulatesmotilitybypromotingcorrectlocalizationofMglAandMglBinMglA/RomRandMglB/ RomRcomplexesatoppositepoles.Moreover,localizationanalysessuggestthatthetwoRomRcomplexesmutuallyexclude eachotherfromtheirrespectivepoles.WefurthershowthatRomRinterfaceswithFrzZ,theoutputresponseregulatorof the Frz chemosensory system, to regulate reversals. Thus, RomR serves at the functional interface to connect a classic bacterialsignallingmodule(Frz)toaclassiceukaryoticpolaritymodule(MglA/MglB).Thismodulardesignisparalleledby thephylogeneticdistributionoftheproteins,suggestinganevolutionaryschemeinwhichRomRwasincorporatedintothe MglA/MglBmoduletoregulatecellpolarityfollowedbytheadditionoftheFrzsystemtodynam