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dc.contributor.CRUESPUNIVERSIDADE ESTADUAL DE CAMPINASpt_BR
dc.contributor.authorunicampSeraphim, Thiago Vargas-
dc.contributor.authorunicampMcSwane, David Zachary-
dc.contributor.authorunicampRamos, Carlos Henrique Inacio-
dc.typeArtigopt_BR
dc.titleIdentification of regions involved in substrate binding and dimer stabilization within the central domains of yeast Hsp40 Sis1pt_BR
dc.contributor.authorBorges, Júlio C.-
dc.contributor.authorSeraphim, Thiago V.-
dc.contributor.authorMokry, David Z.-
dc.contributor.authorAlmeida, Fabio C. L.-
dc.contributor.authorCyr, Douglas M.-
dc.contributor.authorRamos, Carlos H. I.-
dc.subjectLeveduraspt_BR
dc.subject.otherlanguageYeastpt_BR
dc.description.abstractProtein folding, refolding and degradation are essential for cellular life and are regulated by protein homeostatic processes such those that involve the molecular chaperone DnaK/Hsp70 and its co-chaperone DnaJ. Hsp70 action is initiated when proteins from the DnaJ family bind an unfolded protein for delivery purposes. In eukaryotes, the DnaJ family can be divided into two main groups, Type I and Type II, represented by yeast cytosolic Ydj1 and Sis1, respectively. Although sharing some unique features both members of the DnaJ family, Ydj1 and Sis1 are structurally and functionally distinct as deemed by previous studies, including the observation that their central domains carry the structural and functional information even in switched chimeras. In this study, we combined several biophysical tools for evaluating the stability of Sis1 and mutants that had the central domains (named Gly/Met rich domain and C-terminal Domain I) deleted or switched to those of Ydj1 to gain insight into the role of these regions in the structure and function of Sis1. The mutants retained some functions similar to full length wild-type Sis1, however they were defective in others. We found that: 1) Sis1 unfolds in at least two steps as follows: folded dimer to partially folded monomer and then to an unfolded monomer. 2) The Gly/Met rich domain had intrinsically disordered characteristics and its deletion had no effect on the conformational stability of the protein. 3) The deletion of the C-terminal Domain I perturbed the stability of the dimer. 4) Exchanging the central domains perturbed the conformational stability of the protein. Altogether, our results suggest the existence of two similar subdomains in the C-terminal domain of DnaJ that could be important for stabilizing each other in order to maintain a folded substrate-binding site as well as the dimeric state of the proteinpt_BR
dc.relation.ispartofPLoS onept_BR
dc.publisher.citySan Francisco, CApt_BR
dc.publisher.countryEstados Unidospt_BR
dc.publisherPublic Library of Sciencept_BR
dc.date.issued2012-
dc.date.monthofcirculationDec.pt_BR
dc.language.isoengpt_BR
dc.description.volume7pt_BR
dc.description.issuenumber12pt_BR
dc.rightsAbertopt_BR
dc.sourceWOSpt_BR
dc.identifier.eissn1932-6203pt_BR
dc.identifier.doi10.1371/journal.pone.0050927pt_BR
dc.identifier.urlhttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0050927pt_BR
dc.date.available2020-09-09T14:55:30Z-
dc.date.accessioned2020-09-09T14:55:30Z-
dc.description.provenanceSubmitted by Susilene Barbosa da Silva (susilene@unicamp.br) on 2020-09-09T14:55:30Z No. of bitstreams: 0. Added 1 bitstream(s) on 2021-01-04T15:13:03Z : No. of bitstreams: 1 000312588200082.pdf: 1573451 bytes, checksum: a32339530b535b45ba60f2ebcdc807d0 (MD5)en
dc.description.provenanceMade available in DSpace on 2020-09-09T14:55:30Z (GMT). No. of bitstreams: 0 Previous issue date: 2012en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/348940-
dc.contributor.departmentSem informaçãopt_BR
dc.contributor.departmentSem informaçãopt_BR
dc.contributor.departmentDepartamento de Química Orgânicapt_BR
dc.contributor.unidadeInstituto de Químicapt_BR
dc.contributor.unidadeInstituto de Químicapt_BR
dc.contributor.unidadeInstituto de Químicapt_BR
dc.subject.keywordStabilizationpt_BR
dc.identifier.source000312588200082pt_BR
dc.creator.orcid0000-0002-8682-8962pt_BR
dc.creator.orcidSem informaçãopt_BR
dc.creator.orcid0000-0002-7246-9081pt_BR
dc.type.formArtigo de pesquisapt_BR
dc.identifier.articleide50927pt_BR
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