Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/355973
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dc.contributor.CRUESPUNIVERSIDADE ESTADUAL DE CAMPINASpt_BR
dc.contributor.authorunicampMurakami, Letícia Maria Zanphorlin-
dc.contributor.authorunicampLima, Tatiani Brenelli de-
dc.contributor.authorunicampGozzo, Fábio Cesar-
dc.contributor.authorunicampRamos, Carlos Henrique Inacio-
dc.typeArtigopt_BR
dc.titleHeat shock protein 90 kDa (Hsp90) has a second functional interaction site with the mitochondrial import receptor tom70pt_BR
dc.contributor.authorZanphorlin, Leticia M.-
dc.contributor.authorLima, Tatiani B.-
dc.contributor.authorWong, Michael J.-
dc.contributor.authorBalbuena, Tiago S.-
dc.contributor.authorMinetti, Conceição A. S. A.-
dc.contributor.authorRemeta, David P.-
dc.contributor.authorYoung, Jason C.-
dc.contributor.authorBarbosa, Leandro R. S.-
dc.contributor.authorGozzo, Fabio C.-
dc.contributor.authorRamos, Carlos H. I.-
dc.subjectChaperonas molecularespt_BR
dc.subject.otherlanguageMolecular chaperonespt_BR
dc.description.abstractTo accomplish its crucial role, mitochondria require proteins that are produced in the cytosol, delivered by cytosolic Hsp90, and translocated to its interior by the translocase outer membrane (TOM) complex. Hsp90 is a dimeric molecular chaperone and its function is modulated by its interaction with a large variety of co-chaperones expressed within the cell. An important family of co-chaperones is characterized by the presence of one TPR (tetratricopeptide repeat) domain, which binds to the C-terminal MEEVD motif of Hsp90. These include Tom70, an important component of the TOM complex. Despite a wealth of studies conducted on the relevance of Tom70·Hsp90 complex formation, there is a dearth of information regarding the exact molecular mode of interaction. To help fill this void, we have employed a combined experimental strategy consisting of cross-linking/mass spectrometry to investigate binding of the C-terminal Hsp90 domain to the cytosolic domain of Tom70. This approach has identified a novel region of contact between C-Hsp90 and Tom70, a finding that is confirmed by probing the corresponding peptides derived from cross-linking experiments via isothermal titration calorimetry and mitochondrial import assays. The data generated in this study are combined to input constraints for a molecular model of the Hsp90/Tom70 interaction, which has been validated by small angle x-ray scattering, hydrogen/deuterium exchange, and mass spectrometry. The resultant model suggests that only one of the MEEVD motifs within dimeric Hsp90 contacts Tom70. Collectively, our findings provide significant insight on the mechanisms by which preproteins interact with Hsp90 and are translocated via Tom70 to the mitochondriapt_BR
dc.relation.ispartofJournal of biological chemistrypt_BR
dc.relation.ispartofabbreviationJ. biol. chem.pt_BR
dc.publisher.cityBethesda, MDpt_BR
dc.publisher.countryEstados Unidospt_BR
dc.publisherAmerican Society for Biochemistry and Molecular Biologypt_BR
dc.date.issued2016-
dc.date.monthofcirculationSept.pt_BR
dc.language.isoengpt_BR
dc.description.volume291pt_BR
dc.description.issuenumber36pt_BR
dc.description.firstpage18620pt_BR
dc.description.lastpage18631pt_BR
dc.rightsFechadopt_BR
dc.sourceWOSpt_BR
dc.identifier.issn0021-9258pt_BR
dc.identifier.eissn1083-351Xpt_BR
dc.identifier.doi10.1074/jbc.M115.710137pt_BR
dc.identifier.urlhttps://www.sciencedirect.com/science/article/pii/S0021925820307638pt_BR
dc.description.sponsorshipFUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULO - FAPESPpt_BR
dc.description.sponsorshipCONSELHO NACIONAL DE DESENVOLVIMENTO CIENTÍFICO E TECNOLÓGICO - CNPQpt_BR
dc.description.sponsordocumentnumberSem informaçãopt_BR
dc.description.sponsordocumentnumber2012/50161-8pt_BR
dc.date.available2021-02-17T14:37:41Z-
dc.date.accessioned2021-02-17T14:37:41Z-
dc.description.provenanceSubmitted by Thais de Brito Barroso (tbrito@unicamp.br) on 2021-02-17T14:37:41Z No. of bitstreams: 0. Added 1 bitstream(s) on 2021-05-24T16:47:27Z : No. of bitstreams: 1 000383242300003.pdf: 3144157 bytes, checksum: 87721265ad72c497fb472b044d11398f (MD5)en
dc.description.provenanceMade available in DSpace on 2021-02-17T14:37:41Z (GMT). No. of bitstreams: 0 Previous issue date: 2016en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/355973-
dc.contributor.departmentSem informaçãopt_BR
dc.contributor.departmentSem informaçãopt_BR
dc.contributor.departmentDepartamento de Química Orgânicapt_BR
dc.contributor.departmentDepartamento de Química Orgânicapt_BR
dc.contributor.unidadeInstituto de Químicapt_BR
dc.subject.keywordHeat shock protein 90 (Hsp90)pt_BR
dc.subject.keywordMitochondrial transportpt_BR
dc.subject.keywordProtein assemblypt_BR
dc.subject.keywordProtein foldingpt_BR
dc.identifier.source000383242300003pt_BR
dc.creator.orcidSem informaçãopt_BR
dc.creator.orcid0000-0003-4869-0592pt_BR
dc.creator.orcid0000-0002-5270-4427pt_BR
dc.creator.orcid0000-0002-7246-9081pt_BR
dc.type.formArtigopt_BR
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