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dc.contributor.CRUESPUniversidade Estadual de Campinaspt_BR
dc.typeArtigo de periódicopt_BR
dc.titleLow resolution structural study of two human HSP40 chaperones in solution - DjA1 from subfamily A and DjB4 from subfamily B have different quaternary structurespt_BR
dc.contributor.authorBorges, JCpt_BR
dc.contributor.authorFischer, Hpt_BR
dc.contributor.authorCraievich, AFpt_BR
dc.contributor.authorRamos, CHIpt_BR
unicamp.authorLab Nacl Luz Sincrotron, Ctr Biol Mol Estrutural, BR-13084971 Campinas, SP, Brazil Univ Estadual Campinas, Inst Biol, Dept Bioquim, BR-13084971 Campinas, SP, Brazil Univ Sao Paulo, Inst Fis, Dept Fis Aplicada, BR-05508900 Sao Paulo, Brazilpt_BR
dc.subject.wosDnaj Molecular Chaperonept_BR
dc.subject.wosFinger-like Domainpt_BR
dc.subject.wosTerminal Regionpt_BR
dc.description.abstractProteins that belong to the heat shock protein (Hsp) 40 family assist Hsp70 in many cellular functions and are important for maintaining cell viability. A knowledge of the structural and functional characteristics of the Hsp40 family is therefore essential for understanding the role of the Hsp70 chaperone system in cells. In this work, we used small angle x-ray scattering and analytical ultracentrifugation to study two representatives of human Hsp40, namely, DjA1 (Hdj2/dj2/HSDJ/Rdj1) from subfamily A and DjB4 (Hlj1/DnaJW) from subfamily B, and to determine their quaternary structure. We also constructed low resolution models for the structure of DjA1-(1-332), a C-terminal-deleted mutant of DjA1 in which dimer formation is prevented. Our results, together with the current structural information of the Hsp40 C-terminal and J-domains, were used to generate models of the internal structural organization of DjA1 and DjB4. The characteristics of these models indicated that DjA1 and DjB4 were both dimers, but with substantial differences in their quaternary structures: whereas DjA1 consisted of a compact dimer in which the N and C termini of the two monomers faced each other, DjB4 formed a dimer in which only the C termini of the two monomers were in contact. The two proteins also differed in their ability to bind unfolded luciferase. Overall, our results indicate that these representatives of subfamilies A and B of human Hsp40 have different quaternary structures and chaperone
dc.relation.ispartofJournal Of Biological Chemistrypt_BR
dc.relation.ispartofabbreviationJ. Biol. Chem.pt_BR
dc.publisherAmer Soc Biochemistry Molecular Biology Incpt_BR 8pt_BR
dc.identifier.citationJournal Of Biological Chemistry. Amer Soc Biochemistry Molecular Biology Inc, v. 280, n. 14, n. 13671, n. 13681, 2005.pt_BR
dc.sourceWeb of Sciencept_BR
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