The Stability of Wild-type and Deletion Mutants of Human C-terminus Hsp70-interacting Protein (CHIP)

dc.creatorMillan, ICR
dc.creatorSquillace, ALA
dc.creatorGava, LM
dc.creatorRamos, CHI
dc.date2013
dc.dateMAY
dc.date2014-07-30T19:00:30Z
dc.date2015-11-26T16:55:03Z
dc.date2014-07-30T19:00:30Z
dc.date2015-11-26T16:55:03Z
dc.date.accessioned2018-03-28T23:42:19Z
dc.date.available2018-03-28T23:42:19Z
dc.identifierProtein And Peptide Letters. Bentham Science Publ Ltd, v. 20, n. 5, n. 524, n. 529, 2013.
dc.identifier0929-8665
dc.identifierWOS:000316862500005
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/72496
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/72496
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1277000
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionCarboxyl terminus of Hsp70 interacting protein (CHIP) is a dimeric co-chaperone involved in providing an appropriate balance between the synthesis and degradation of proteins, which is essential for normal cellular growth and function. Previous work has shown that CHIP, but not its isolated domains, has chaperone activity that is enhanced by heat. In this work, we investigate how heat and urea affect the stability of its domains. We found that the deletion mutant containing the TPR domain, which binds to chaperones Hsp70 or Hsp90, was monomeric and showed similar folding and stability to WT, while the mutant containing the U-box ubiquitin ligase domain was dimeric but had very low stability. The deletion mutants appeared to maintain most of their structure compared to the WT protein, but the regions around the tryptophan residues, which are at the interface of the domains in the WT structure, appeared to be more unfolded, which indicated that the region of contact between domains is likely important for the chaperone function.
dc.description20
dc.description5
dc.description524
dc.description529
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.languageen
dc.publisherBentham Science Publ Ltd
dc.publisherSharjah
dc.publisherEmirados Árabes Unidos
dc.relationProtein And Peptide Letters
dc.relationProtein Pept. Lett.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectCHIP
dc.subjectheat shock protein
dc.subjectprotein folding
dc.subjectprotein-protein interaction
dc.subjectE3 Ubiquitin Ligase
dc.subjectHeat-shock Proteins
dc.subjectChaperone Functions
dc.subjectIdentification
dc.subjectUbiquitylation
dc.titleThe Stability of Wild-type and Deletion Mutants of Human C-terminus Hsp70-interacting Protein (CHIP)
dc.typeArtículos de revistas


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