Calpain-Catalyzed Proteolysis of Human dUTPase Specifically Removes the Nuclear Localization Signal Peptide 英文参考文献.docVIP

下载本文档

0
0
约3.17万字
约 7页
2017-05-11 发布于上海
举报
版权申诉

Calpain-Catalyzed Proteolysis of Human dUTPase Specifically Removes the Nuclear Localization Signal Peptide 英文参考文献.doc

1、原创力文档（book118）网站文档一经付费（服务费），不意味着购买了该文档的版权，仅供个人/单位学习、研究之用，不得用于商业用途，未经授权，严禁复制、发行、汇编、翻译或者网络传播等，侵权必究。。
2、本站所有内容均由合作方或网友上传，本站不对文档的完整性、权威性及其观点立场正确性做任何保证或承诺！文档内容仅供研究参考，付费前请自行鉴别。如您付费，意味着您自己接受本站规则且自行承担风险，本站不退款、不进行额外附加服务；查看《如何避免下载的几个坑》。如果您已付费下载过本站文档，您可以点击这里二次下载。
3、如文档侵犯商业秘密、侵犯著作权、侵犯人身权等，请点击“版权申诉”（推荐），也可以打举报电话：400-050-0827(电话支持时间：9:00-18:30)。
4、该文档为VIP文档，如果想要下载，成为VIP会员后，下载免费。
5、成为VIP后，下载本文档将扣除1次下载权益。下载后，不支持退款、换文档。如有疑问请联系我们。
6、成为VIP后，您将拥有八大权益，权益包括：VIP文档下载权益、阅读免打扰、文档格式转换、高级专利检索、专属身份标志、高级客服、多端互通、版权登记。
7、VIP文档为合作方或网友上传，每下载1次，网站将根据用户上传文档的质量评分、类型等，对文档贡献者给予高额补贴、流量扶持。如果你也想贡献VIP文档。上传文档

Calpain-Catalyzed Proteolysis of Human dUTPase Specifically Removes the Nuclear Localization Signal Peptide 英文参考文献

Calpain-CatalyzedProteolysisofHumandUTPase SpecificallyRemovestheNuclearLocalizationSignal Peptide Zolta′nBozo′ky1.,GergelyRo′na1.,Eva′ Klement2,KatalinF.Medzihradszky2,3,Ga′borMere′nyi1,Bea′taG. Ve′rtessy1,4*,PeterFriedrich1* 1InstituteofEnzymology,HungarianAcademyofSciences,Budapest,Hungary,2ProteomicsResearchGroup,BiologicalResearchCentre(BRC),HungarianAcademyof Sciences, Szeged, Hungary, 3Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California, United States of America, 4DepartmentofAppliedBiotechnology,BudapestUniversityofTechnologyandEconomics,Budapest,Hungary Abstract Background: Calpainproteases drive intracellular signaltransduction via specific proteolysis of multiplesubstrates upon Ca -induced activation. Recently, dUTPase, an enzyme essential to maintain genomic integrity, was identified as a 2+ physiological calpain substrate in Drosophila cells. Here we investigate the potential structural/functional significance of calpain-activatedproteolysisofhumandUTPase. Methodology/PrincipalFindings:LimitedproteolysisofhumandUTPasebymammalianm-calpainwasinvestigatedinthe presence and absence of cognate ligands of either calpain or dUTPase. Significant proteolysis was observed only in the presence of Ca(II) ions, inducing calpain action. The presence or absence of the dUTP-analogue a,b-imido-dUTP did not 2+ show any effect on Ca -calpain-induced cleavage of human dUTPase. The catalytic rate constant of dUTPase was unaffectedbycalpaincleavage.GelelectrophoreticanalysisshowedthatCa -calpain-inducedcleavageofhumandUTPase 2+ resulted in several distinctly observable dUTPase fragments. Mass spectrometric identification of the calpain-cleaved fragmentsidentifiedthreecalpaincleavagesites(betweenresidues 4SE5;7TP8;and31LS32).Thecleavagebetweenthe31LS32 peptidebondspecificallyremovestheflexibleN-terminalnuclearlocalizationsignal,indispensableforcognatelocalization. Conclusions/Significance: Results argue for a