Dissimilarity in the Folding of Human Cytosolic Creatine Kinase Isoenzymes 英文参考文献.docVIP

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Dissimilarity in the Folding of Human Cytosolic Creatine Kinase Isoenzymes 英文参考文献.doc

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Dissimilarity in the Folding of Human Cytosolic Creatine Kinase Isoenzymes 英文参考文献

DissimilarityintheFoldingofHumanCytosolicCreatine KinaseIsoenzymes YinWang1,2,ShaWang1,Yan-SongGao1,2,ZheChen1,2,Hai-MengZhou2,3,Yong-BinYan1* 1StateKeyLaboratoryofBiomembraneandMembraneBiotechnology,SchoolofLifeSciences,TsinghuaUniversity,Beijing,China,2ProteinScienceLaboratoryofthe MinistryofEducation,School ofLifeSciences, Tsinghua University,Beijing, China, 3ZhejiangProvincial KeyLaboratory ofAppliedEnzymology, YangtzeDeltaRegion InstituteofTsinghuaUniversity,Zhejiang,China Abstract Creatine kinase (CK, EC ) plays a key role in the energy homeostasis of excitable cells. The cytosolic human CK isoenzymesexistashomodimers(HMCKandHBCK)oraheterodimer(MBCK)formedbythemuscleCKsubunit(M)and/or brainCKsubunit(B)withhighlyconservedthree-dimensionalstructurescomposedofasmallN-terminaldomain(NTD)and a large C-terminal domain (CTD). The isoforms of CK provide a novel system to investigate the sequence/structural determinantsofmultimeric/multidomainproteinfolding.Inthisresearch,theroleofNTDandCTDaswellasthedomain interactionsinCKfoldingwasinvestigatedbycomparingtheequilibriumandkineticfoldingparametersofHMCK,HBCK, MBCKandtwodomain-swappedchimericforms(BnMcandMnBc).Spectroscopicresultsindicatedthatthefiveproteins haddistinctstructuralfeaturesdependingonthedomainorganizations.MBCKBnMchadthesmallestCDsignalsandthe lowest stability against guanidine chloride-induced denaturation. During the biphasic kinetic refolding, three proteins (HMCK,BnMcandMnBc),whichcontainedeithertheNTDorCTDoftheMsubunitandsimilarmicroenvironmentsofthe Trpfluorophores,refoldedabout10-foldfasterthanHBCKforboththefastandslowphase.Thefastfoldingofthesethree proteins led to an accumulation of the aggregation-prone intermediate and slowed down the reactivation rate thereby during the kinetic refolding. Our results suggested that the intra- and inter-subunit domain interactions modified the behaviorofkineticrefolding.Thealternationofdomaininteractionsbasedonisoenzymesalsoprovidesavaluablestrategy toimprov