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dc.contributor.CRUESPUNIVERSIDADE ESTADUAL DE CAMPINASpt_BR
dc.typeArtigo de periódicopt_BR
dc.titleIdentification of Regions Involved in Substrate Binding and Dimer Stabilization within the Central Domains of Yeast Hsp40 Sis1pt_BR
dc.contributor.authorBorges, Julio C.pt_BR
dc.contributor.authorSeraphim, Thiago V.pt_BR
dc.contributor.authorMokry, David Z.pt_BR
dc.contributor.authorAlmeida, Fabio C. L.pt_BR
dc.contributor.authorCyr, Douglas M.pt_BR
dc.contributor.authorRamos, Carlos H. I.pt_BR
unicamp.authorSeraphim, Thiago V.pt_BR
unicamp.authorMokry, David Z.pt_BR
unicamp.authorRamos, Carlos H. I.pt_BR
unicamp.author.externalBorges, Julio C.pt
unicamp.author.externalAlmeida, Fabio C. L.pt
unicamp.author.externalCyr, Douglas M.pt
dc.subject.wosMOLECULAR CHAPERONESpt_BR
dc.subject.wosCRYSTAL-STRUCTUREpt_BR
dc.subject.wosDNAK CHAPERONEpt_BR
dc.subject.wosHSP70pt_BR
dc.subject.wosPROTEINpt_BR
dc.subject.wosYDJ1pt_BR
dc.subject.wosULTRACENTRIFUGATIONpt_BR
dc.subject.wosSPECTROSCOPYpt_BR
dc.subject.wosAGGREGATIONpt_BR
dc.subject.wosSPECIFICITYpt_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 protein.pt
dc.relation.ispartofPlos ONEpt_BR
dc.publisher.citySan Franciscopt_BR
dc.publisher.countryUSApt_BR
dc.publisherPublic Library Sciencept_BR
dc.date.issued2012pt_BR
dc.identifier.citationPlos ONE. Public Library Science, v.7, n.12, 2012pt_BR
dc.language.isoengpt_BR
dc.description.volume7pt_BR
dc.description.issuenumber12pt_BR
dc.rightsfechadopt_BR
dc.sourceWOSpt_BR
dc.identifier.issn1932-6203pt_BR
dc.identifier.wosidWOS:000312588200082pt_BR
dc.identifier.doi10.1371/journal.pone.0050927pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipMinisterio da Ciencia e Tecnologia/Conselho Nacional de Pesquisa e Desenvolvimento (MCT/CNPq)pt_BR
dc.description.sponsorship1Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorship1Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.date.available2013-09-19T18:06:42Z
dc.date.available2016-07-01T12:52:01Z-
dc.date.accessioned2013-09-19T18:06:42Z
dc.date.accessioned2016-07-01T12:52:01Z-
dc.description.provenanceMade available in DSpace on 2013-09-19T18:06:42Z (GMT). No. of bitstreams: 0 Previous issue date: 2012en
dc.description.provenanceMade available in DSpace on 2016-07-01T12:52:01Z (GMT). No. of bitstreams: 2 WOS000312588200082.pdf: 1482338 bytes, checksum: cf045d7c166060b1fd8d8618ae8ae4eb (MD5) WOS000312588200082.pdf.txt: 58928 bytes, checksum: 33d25b2b74270c6467a69727eb8fa816 (MD5) Previous issue date: 2012en
dc.identifier.urihttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/2368
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/2368-
dc.contributor.departmentEspectrometria
dc.contributor.unidadeIQpt
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