Replication Protein A (RPA) Hampers the Processive Action of APOBEC3G Cytosine Deaminase on Single-Stranded DNA 英文参考文献.docVIP

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Replication Protein A (RPA) Hampers the Processive Action of APOBEC3G Cytosine Deaminase on Single-Stranded DNA 英文参考文献.doc

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Replication Protein A (RPA) Hampers the Processive Action of APOBEC3G Cytosine Deaminase on Single-Stranded DNA 英文参考文献

ReplicationProteinA(RPA)HamperstheProcessive ActionofAPOBEC3GCytosineDeaminaseon Single-StrandedDNA ArtemG.Lada1,IrinaS.-R.Waisertreiger1.,CorinnE.Grabow1.,AishwaryaPrakash1¤,GloriaE.O. Borgstahl1,IgorB.Rogozin2,3,YouriI.Pavlov1* 1EppleyInstituteforResearchinCancerandAlliedDiseases,UniversityofNebraskaMedicalCenter,Omaha,Nebraska,UnitedStatesofAmerica,2NationalCenterfor BiotechnologyInformation,NationalLibraryofMedicine,NationalInstitutesofHealth,Bethesda,Maryland,UnitedStatesofAmerica,3InstituteofCytologyandGenetics, Novosibirsk,Russia Abstract Background: Editing deaminases have a pivotal role in cellular physiology. A notable member of this superfamily, APOBEC3G(A3G),restrictsretroviruses,andActivationInducedDeaminase(AID)generatesantibodydiversitybylocalized deaminationofcytosinesinDNA.Unconstraineddeaminaseactivitycancausegenome-widemutagenesisandcancer.The mechanisms that protect the genomic DNA from the undesired action of deaminases are unknown. Using the in vitro deaminationassaysandexpressionofA3Ginyeast,weshowthatreplicationproteinA(RPA),theeukaryoticsingle-stranded DNA(ssDNA)bindingprotein,severelyinhibitsthedeaminationactivityandprocessivityofA3G. PrincipalFindings/Methodology:WefoundthatmutationsinducedbyA3Gintheyeastgenomicreporterarechangesofa singlenucleotide.ThisisunexpectedbecauseoftheknownpropertyofA3Gtocatalyzemultipledeaminationsuponone substrate encounter event in vitro. The addition of recombinant RPA to the oligonucleotide deamination assay severely inhibited A3G activity. Additionally, we reveal the inverse correlation between RPA concentration and the number of deaminations induced by A3G invitro on long ssDNA regions. This resembles the‘‘hit andrun’’ single basesubstitution eventsobservedinyeast. Significance:OurdatasuggestthatRPAisaplausibleantimutatorfactorlimitingtheactivityandprocessivityofediting deaminasesinthemodelyeastsystem.BecauseofthesimilarantagonismofyeastRPAandhumanRPAwithA3Ginvitro, weproposethatRPAplaysaroleintheprotecti