Science-2015-Yan-science.aac7629.pdf

Science-2015-Yan-science.aac7629.pdf

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时间:2019-03-10

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1、ResearchArticlecatalyticallycompetentB*com-Structureofayeastspliceosomeatplexthatcatalyzesthefirststepoftrans-esterification.Theend3.6-angstromresolutionproductistheCcomplex,alsoknownasthecatalyticstepIChuangyeYan,1*JingHang,1*RuixueWan,1*MinHuang,2spliceosome,whichcontainsthecleaved5′-exonandanin

2、tronCatherineC.L.Wong,2YigongShi1†lariat-3′-exonintermediate.The1MinistryofEducationKeyLaboratoryofProteinScience,Tsinghua-PekingJointCenterforLifeSciences,Centerforsecondstepoftrans-StructuralBiology,SchoolofLifeSciences,TsinghuaUniversity,Beijing100084,China.esterificationresultsintheliga-2Natio

3、nalCenterforProteinScienceShanghai,InstituteofBiochemistryandCellBiology,ShanghaiInstitutesofBiologicaltionoftwoexons,formingtheSciences,ChineseAcademyofSciences,Shanghai200031,China.post-catalyticPcomplex.Subse-*Theseauthorscontributedequallytothiswork.quently,theligatedexonisre-†Correspondingaut

4、hor.E-mail:shi-lab@tsinghua.edu.cnleased,buttheintronlariatremainsassociatedwiththein-tron-lariatspliceosomal(ILS)Splicingofpre-messengerRNA(pre-mRNA)inyeastisexecutedbythecomplex.Finally,theintronlari-spliceosome,whichconsistoffivesmallnuclearribonucleoproteinatisdissociated,andtheparticles(snRNP

5、s),nineteencomplex(NTC),NTCrelated(NTR),andasnRNPs,NTC,andNTRarerecy-numberofassociatedenzymesandcofactors.Herewereportthethree-cled.TheRNPrearrangementsdimensionalstructureofaSchizosaccharomycespombespliceosomeat3.6aredrivenbyeightevolutionari-angstromresolutionbysingleparticle,cryo-electronmicro

6、scopy.ThislyconservedDExD/H-type,RNA-spliceosomecontainsU2andU5snRNPs,NTC,NTR,U6snRNA,andandependentATPases/helicases(8,onAugust22,2015RNAintronlariat.Theatomicmodelincludes10,574aminoacidsfrom379).proteinsand4RNAmolecules,withacombinedmolecularmassofBiochemicalstudiesduringapproximately1.3mega-Da

7、ltons.Spp42(Prp8inS.cerevisiae),thekeythepastdecadeshaveprovidedproteincomponentofU5snRNP,formsacentralscaffoldandanchorsthevaluableinsightsintothemech-catalyticcenter.Boththeappearanceandtheplacementofproteinani

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