Movement Protein Pns6 of Rice dwarf phytoreovirus Has Both ATPase and RNA Binding Activities 英文参考文献.docVIP

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Movement Protein Pns6 of Rice dwarf phytoreovirus Has Both ATPase and RNA Binding Activities 英文参考文献.doc

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Movement Protein Pns6 of Rice dwarf phytoreovirus Has Both ATPase and RNA Binding Activities 英文参考文献

MovementProteinPns6ofRicedwarfphytoreovirusHas BothATPaseandRNABindingActivities XuJi1.,DanQian1.,ChunhongWei1,GongyinYe2,ZhongkaiZhang3,ZujianWu4,LianhuiXie4,YiLi1* 1StateKeyLaboratoryofProteinandPlantGeneResearch,Peking-YaleJointCenterforPlantMolecularGeneticsandAgrobiotechnology,CollegeofLifeSciences,Peking University,Beijing,People’sRepublicofChina,2StateKeyLaboratoryofRiceBiology,InstituteofInsectSciences,ZhejiangUniversity,Hangzhou,People’sRepublicof China, 3Biotechnology and Genetic Resources Institute, Yunnan Academy of Agricultural Sciences, Kunming, People’s Republic of China, 4Key Laboratory of Plant VirologyofFujianProvince,InstituteofPlantVirology,FujianAgricultureandForestryUniversity,Fuzhou,People’sRepublicofChina Abstract Cell-to-cell movement is essential for plant viruses to systemically infect host plants. Plant viruses encode movement proteins (MP) to facilitate such movement. Unlike the well-characterized MPs of DNA viruses and single-stranded RNA (ssRNA)viruses,knowledgeofthefunctionalmechanismsofMPsencodedbydouble-strandedRNA(dsRNA)virusesisvery limited.Inparticular,manystudiedMPsofDNAandssRNAvirusesbindnon-specificallyssRNAs,leadingtomodelsinwhich ribonucleoproteincomplexes(RNPs)movefromcelltocell.Thus,itwillbeofspecialinteresttodeterminewhetherMPsof dsRNAvirusesinteractwithgenomicdsRNAsortheirderivativesRNAs.Tothisend,westudiedthebiochemicalfunctionsof MPPns6ofRicedwarfphytoreovirus(RDV),amemberofPhytoreovirusthatcontainsa12-segmenteddsRNAgenome.We reportherethatPns6bindsbothdsRNAsandssRNAs.Intriguingly,Pns6exhibitsnon-sequencespecificityfordsRNAbut showspreferenceforssRNAsequencesderivedfromtheconservedgenomic59-and39-terminalconsensussequencesof RDV. Furthermore, Pns6 exhibits magnesium-dependent ATPase activities. Mutagenesis identified the RNA binding and ATPaseactivitysitesofPns6attheN-andC-termini,respectively.OurresultsuncoveredthenovelpropertyofaviralMPin differentiallyrecognizingdsRNAandssRNAandestablishabiochemicalbasistoenablefu