Functional Characterization of 8-Oxoguanine DNA Glycosylase of Trypanosoma cruzi 英文参考文献.docVIP

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Functional Characterization of 8-Oxoguanine DNA Glycosylase of Trypanosoma cruzi 英文参考文献.doc

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Functional Characterization of 8-Oxoguanine DNA Glycosylase of Trypanosoma cruzi 英文参考文献

FunctionalCharacterizationof8-OxoguanineDNA GlycosylaseofTrypanosomacruzi CarolinaFurtado1.,MariannaKunrath-Lima1.,MatheusAndradeRaja?o1.,IsabelaCec?′liaMendes1, MichelleBarbideMoura2,PriscilaCarneiroCampos1,AndreaMaraMacedo1,Glo′riaReginaFranco1, Se′rgioDaniloJunhoPena1,SantuzaMariaRibeiroTeixeira1,BennettVanHouten2 ,Carlos RenatoMachado1* 1DepartamentodeBioqu?′micaeImunologia,InstitutodeCie?nciasBiolo′gicas,UniversidadeFederaldeMinasGerais,BeloHorizonte,MinasGerais,Brazil,2Departmentof PharmacologyandChemicalBiology,UniversityofPittsburghSchoolofMedicineandtheUniversityofPittsburghCancerInstitute,HillmanCancerCenter,Pittsburgh, Pennsylvania,UnitedStatesofAmerica Abstract Theoxidativelesion8-oxoguanine(8-oxoG)isremovedduringbaseexcisionrepairbythe8-oxoguanineDNAglycosylase1 (Ogg1).Thislesioncanerroneouslypairwithadenine,andtheexcisionofthisdamagedbasebyOgg1enablestheinsertion ofaguanineandpreventsDNAmutation.Inthisreport,weidentifiedandcharacterizedOgg1fromtheprotozoanparasite Trypanosomacruzi(TcOgg1),thecausativeagentofChagasdisease.Likemostlivingorganisms, T.cruziissusceptibleto oxidativestress,henceDNArepairisessentialforitssurvivalandimprovementofinfection.WeverifiedthattheTcOGG1 gene encodes an 8-oxoG DNA glycosylase by complementing an Ogg1-defective Saccharomyces cerevisiae strain. HeterologousexpressionofTcOGG1reestablished themutationfrequencyoftheyeastmutant ogg12/2 (CD138)towild type levels. We also demonstrate that the overexpression of TcOGG1 increases T. cruzi sensitivity to hydrogen peroxide (H2O2). Analysis of DNA lesions using quantitative PCR suggests that the increased susceptibility to H2O2 of TcOGG1- overexpressor could be a consequence of uncoupled BER in abasic sites and/or strand breaks generated after TcOgg1 removes 8-oxoG, which are not rapidly repaired by the subsequent BER enzymes. This hypothesis is supported by the observation that TcOGG1-overexpressors have reduced levels of 8-oxoG both in the nucleus and in the parasi