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Type: Artigo de periódico
Title: Conserved Central Domains Control the Quaternary Structure of Type I and Type II Hsp40 Molecular Chaperones
Author: Ramos, CHI
Oliveira, CLP
Fan, CY
Torriani, IL
Cyr, DM
Abstract: Heat shock protein (Hsp)40s play an essential role in protein metabolism by regulating the polypeptide binding and release cycle of Hsp70. The Hsp4o family is large, and specialized family members direct Hsp70 to perform highly specific tasks. Type I and Type II Hsp40s, such as yeast Ydj1 and Sis1, are homodimers that dictate functions of cytosolic Hsp70, but how they do so is unclear. Type 1 Hsp40s contain a conserved, centrally located cysteine-rich domain that is replaced by a glycine- and methionine-rich region in Type 11 Hsp40s, but the mechanism by which these unique domains influence Hsp40 structure and function is unknown. This is the case because high-resolution structures of full-length forms of these Hsp40s have not been solved. To fill this void, we built low-resolution models of the quaternary structure of Ydj1 and Sis1 with information obtained from biophysical measurements of protein shape, small-angle X-ray scattering, and ab initio protein modeling. Low-resolution models were also calculated for the chimeric Hsp40s YSY and SYS, in which the central domains of Ydj1. and Sis1 were exchanged. Similar to their human homologs, Ydj1 and Sis1 each has a unique shape with major structural differences apparently being the orientation of the J domains relative to the long axis of the dimers. Central domain swapping in YSY and SYS correlates with the switched ability of YSY and SYS to perform unique functions of Sis1 and Ydj1, respectively. Models for the mechanism by which the conserved cysteine-rich domain and glycine- and methionine-rich region confer structural and functional specificity to Type I and Type 11 Hsp40s are discussed. (C) 2008 Elsevier Ltd. All rights reserved.
Subject: Hsp40
molecular chaperone
protein folding
quaternary structure
small-angle scattering
Country: Inglaterra
Editor: Academic Press Ltd Elsevier Science Ltd
Rights: fechado
Identifier DOI: 10.1016/j.jmb.2008.08.019
Date Issue: 2008
Appears in Collections:Unicamp - Artigos e Outros Documentos

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