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
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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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