Evolution of Bacterial Phosphoglycerate Mutases Non-Homologous Isofunctional Enzymes Undergoing Gene Losses, Gains and Lateral Transfers 英文参考文献.docVIP

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Evolution of Bacterial Phosphoglycerate Mutases Non-Homologous Isofunctional Enzymes Undergoing Gene Losses, Gains and Lateral Transfers 英文参考文献.doc

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Evolution of Bacterial Phosphoglycerate Mutases Non-Homologous Isofunctional Enzymes Undergoing Gene Losses, Gains and Lateral Transfers 英文参考文献

EvolutionofBacterialPhosphoglycerateMutases: Non-HomologousIsofunctionalEnzymesUndergoing GeneLosses,GainsandLateralTransfers JeremyM.Foster*,PaulJ.Davis,SylvineRaverdy,MarionH.Sibley,ElisabethA.Raleigh,SanjayKumar, ClotildeK.S.Carlow DivisionofParasitology,NewEnglandBiolabs,Inc.,Ipswich,Massachusetts,UnitedStatesofAmerica Abstract Background: The glycolytic phosphoglycerate mutases exist as non-homologous isofunctional enzymes (NISE) having independent evolutionary origins and no similarity in primary sequence, 3D structure, or catalytic mechanism. Cofactor- dependent PGM (dPGM) requires 2,3-bisphosphoglycerate for activity; cofactor-independent PGM (iPGM) does not. The PGMprofileofanygivenbacteriumisunpredictableandsomeorganismssuchasEscherichiacoliencodebothforms. Methods/PrincipalFindings:ToexaminethedistributionofPGMNISEthroughouttheBacteria,andgaininsightintothe evolutionary processes that shape their phyletic profiles, we searched bacterial genome sequences for the presence of dPGM and iPGM. Both forms exhibited patchy distributions throughout the bacterial domain. Species within the same genus,orevenstrainsofthesamespecies,frequentlydifferintheirPGMrepertoire.Thedistributionisfurthercomplicated by the common occurrence of dPGM paralogs, while iPGM paralogs are rare. Larger genomes are more likely to accommodatePGMparalogsorbothNISEforms.LateralgenetransfershaveshapedthePGMprofileswithintradomainand interdomaintransfersapparent.Archaeal-typeiPGMwasidentifiedinmanybacteria,oftenasthesolePGM.Toaddressthe functionofPGMNISEinanorganismencodingbothforms,weanalyzedrecombinantenzymesfromE.coli.BothNISEwere active mutases, but the specific activity of dPGM greatly exceeded that of iPGM, which showed highest activity in the presenceofmanganese.WecreatedPGMnullmutantsinE.colianddiscoveredtheDdPGMmutantgrewslowlyduetoa delayinexitingstationaryphase.OverexpressionofdPGMoriPGMovercamethisdefect. Conclusions/Significance: Our biochemical and genetic analyses in E. coli f