Bacterial Adaptor Membrane Fusion Proteins and the Structurally Dissimilar Outer Membrane Auxiliary Proteins Have Exchanged Central Domains in -Proteobacteria英文文献资料.docVIP

Bacterial Adaptor Membrane Fusion Proteins and the Structurally Dissimilar Outer Membrane Auxiliary Proteins Have Exchanged Central Domains in -Proteobacteria英文文献资料.doc

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Bacterial Adaptor Membrane Fusion Proteins and the Structurally Dissimilar Outer Membrane Auxiliary Proteins Have Exchanged Central Domains in -Proteobacteria英文文献资料

HindawiPublishingCorporation InternationalJournalofMicrobiology Volume2010,ArticleID589391,5pages doi:10.1155/2010/589391 ResearchArticle BacterialAdaptorMembraneFusionProteinsand theStructurallyDissimilarOuterMembraneAuxiliaryProteins HaveExchangedCentralDomainsinα-Proteobacteria AnthonyY.Xiao,JingWang,andMiltonH.SaierJr. DivisionofBiologicalSciences,UniversityofCaliforniaatSanDiego,LaJolla,CA92093-0116,USA CorrespondenceshouldbeaddressedtoMiltonH.SaierJr.,msaier@ Received10December2009;Accepted31January2010 AcademicEditor:IsabelS′a-Correia Copyright?2010AnthonyY.Xiaoetal. This is an open access article distributed under the Creative Commons Attribution License,whichpermitsunrestricteduse,distribution,andreproductioninanymedium,providedtheoriginalworkisproperly cited. Transportsystemsfrequentlyincludeauxiliaryproteinsthatperformsubfunctionswithinthetransporterproteincomplex.Two suchproteinsfoundinGram-negativebacteriaaretheMembraneFusionProteins(MFPs)andtheOuterMembraneAuxiliary (OMA)proteins.WeheredemonstratethatOMAspresentinα-proteobacteria(butnotinotherbacterialtypes)containalong α-helicalregionthatishomologoustocorrespondingregionsintheMFPs.Theresultssuggestthatduringtheirevolution,OMAs, speci?cally from α-proteobacteria, exchanged their own α-helical domain for one derived from an MFP. The structural and functionalimplicationsofthese?ndingsarediscussed. 1.Introduction milieuwithoutequilibrationofsolutesintheperiplasm,all inasingleenergycoupledstep.Crosslinkingstudiesofthe MFP,AcrAofE.coli(8.A.1.6.1),withitscognatetransporter, AcrB (2.A.6.2.2), and its OMF, TolC (1.B.17.1.1), revealed that AcrA could be crosslinked to both AcrB (via the C- terminalportionofAcrA)andTolC(viathecentralcoiled- coilregionofAcrA)[6]. Most MFPs are about 350–500 residues in length and either span the cytoplasmic membrane once at their N- termini or are anchored to the cytoplasmic membrane via alipoylmoiety.Theseproteinsclusterphylogeneticallyinto subfamilies in accordance with the

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