Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/337007
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dc.contributor.CRUESPUNIVERSIDADE ESTADUAL DE CAMPINASpt_BR
dc.contributor.authorunicampPinheiro, Glaucia Melina Squizato-
dc.contributor.authorunicampRamos, Carlos Henrique Inacio-
dc.typeArtigopt_BR
dc.titleSolution NMR investigation on the structure and function of the isolated J-domain from Sis1: Evidence of transient inter-domain interactions in the full-length proteinpt_BR
dc.contributor.authorPinheiro, Glaucia M. S.-
dc.contributor.authorAmorim, Gisele C.-
dc.contributor.authorIqbal, Anwar-
dc.contributor.authorAlmeida, Fabio C. L.-
dc.contributor.authorRamosa, C. H. I.-
dc.subjectProteínas de choque térmicopt_BR
dc.subject.otherlanguageHeat shock proteinpt_BR
dc.description.abstractJ-domain/Hsp40 proteins cooperate in aiding with folding in the cell by binding partially folded client proteins and delivering them to be folded by Hsp70. The delivery occurs concomitantly to the stimulation of the ATPase activity of Hsp70 via the N-terminally located J-domain. Although several lines of investigation have been used to study J-domain proteins, the presence of highly flexible domains (G/F- and G/M-rich) hold up obtaining a detailed full-length structure. In this work, we present the high-resolution structure of the J-domain and the N-terminal part of the G/F domain of Sis1, solved by NMR, and used chemical-shift perturbation approaches to further study the structure/function relationship of the Sis1/Hsp70 interaction. When the J-domain was compared to the full-length protein and to a G/M domain deletion mutant, an internal interaction patch formed by hydrophobic and positively charged residues (V2, D9, R27, T39, F52 and R73) was identified. Curiously, the same patch is protected by internal contacts in the full-length protein and, in combination with the loop containing the conserved HPD motif, participates in the interaction with Hsp70. Combined, these results suggest that the J-domain in the full-length Sis1 is in a transient intermediate conformation, in which its interacting patch is protected and, at the same time, also in a favorable condition to bind Hsp70, facilitating the interaction between the two proteins. Finally, 1D NMR experiments showed that the addition of ATP is followed by the disruption of the J-domain/Hsp70 complex, a necessary step for aiding the folding of the client proteinpt_BR
dc.relation.ispartofArchives of biochemistry and biophysicspt_BR
dc.publisher.cityMaryland Heights, MOpt_BR
dc.publisher.countryEstados Unidospt_BR
dc.publisherElsevierpt_BR
dc.date.issued2019-
dc.date.monthofcirculationJulypt_BR
dc.language.isoengpt_BR
dc.description.volume669pt_BR
dc.description.firstpage71pt_BR
dc.description.lastpage79pt_BR
dc.rightsFechadopt_BR
dc.sourceWOSpt_BR
dc.identifier.issn0003-9861pt_BR
dc.identifier.eissn1096-0384pt_BR
dc.identifier.doi10.1016/j.abb.2019.05.020pt_BR
dc.identifier.urlhttps://www.sciencedirect.com/science/article/pii/S0003986119301195pt_BR
dc.description.sponsorshipCOORDENAÇÃO DE APERFEIÇOAMENTO DE PESSOAL DE NÍVEL SUPERIOR - CAPESpt_BR
dc.description.sponsorshipCONSELHO NACIONAL DE DESENVOLVIMENTO CIENTÍFICO E TECNOLÓGICO - CNPQpt_BR
dc.description.sponsorshipFUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULO - FAPESPpt_BR
dc.description.sponsordocumentnumbersem informaçãopt_BR
dc.description.sponsordocumentnumbersem informaçãopt_BR
dc.description.sponsordocumentnumber2012/50161-8; 2017/26131-5; 2017/01074-9; 2018/11948-9pt_BR
dc.date.available2020-03-20T14:12:47Z-
dc.date.accessioned2020-03-20T14:12:47Z-
dc.description.provenanceSubmitted by Sanches Olivia (olivias@unicamp.br) on 2020-03-20T14:12:47Z No. of bitstreams: 0. Added 1 bitstream(s) on 2020-07-20T14:18:15Z : No. of bitstreams: 1 000472985500009.pdf: 2433262 bytes, checksum: b06dea801434332aa30a1a96c172ebb8 (MD5)en
dc.description.provenanceMade available in DSpace on 2020-03-20T14:12:47Z (GMT). No. of bitstreams: 0 Previous issue date: 2019en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/337007-
dc.contributor.departmentsem informaçãopt_BR
dc.contributor.departmentDepartamento de Química Orgânicapt_BR
dc.contributor.unidadeInstituto de Químicapt_BR
dc.subject.keywordJ-domainpt_BR
dc.subject.keywordProtein-protein interactionpt_BR
dc.subject.keywordHsp70pt_BR
dc.subject.keywordChaperonept_BR
dc.subject.keywordNMRpt_BR
dc.identifier.source000472985500009pt_BR
dc.creator.orcid0000-0002-9001-5729pt_BR
dc.creator.orcid0000-0002-7246-9081pt_BR
dc.type.formArtigo de Periódicopt_BR
dc.description.sponsorNoteResearch in the laboratory of CHIR is supported by grants from Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP 2012/50161-8, 2017/26131-5, 2017/01074-9 and 2018/11948-9), Conselho Nacional de Pesquisa e Desenvolvimento (CNPq), CAPES and INBEBpt_BR
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