Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/68177
Type: Artigo de periódico
Title: Heat causes oligomeric disassembly and increases the chaperone activity of small heat shock proteins from sugarcane
Author: Tiroli-Cepeda, AO
Ramos, CHI
Abstract: Small heat shock proteins (sHsp) constitute an important chaperone family linked to conformational diseases. In plants, sHsps prevent protein aggregation by acting as thermosensors and to enhance cell stress tolerance. SsHsp17.2 and SsHsp17.9 are the most highly expressed class I sHsps in sugarcane. They exist as dodecamers at 20 degrees C and have distinct substrate specificities. Therefore, they are useful models to study how class I SHsps work. Here we present data on the effects of heat on the oligomerization and chaperone activity of SsHsp17.2 and SsHsp17.9. Using several biophysical and biochemical probes, we show that the effects of heat are completely reversible, an important property for proteins that act at heat shock temperatures. SsHsp17.2 and SsHsp17.9 dodecamers dissociated to dimers at temperatures ranging from 40 to 45 degrees C and this dissociation was followed by enhanced chaperone activity. We conclude that high temperature affects the oligomeric state of these chaperones, resulting in enhanced chaperone activity. (C) 2010 Elsevier Masson SAS. All rights reserved.
Subject: Small heat shock protein
Chaperone activity
Oligomerization
Thermosensor
Sugarcane
Country: França
Editor: Elsevier France-editions Scientifiques Medicales Elsevier
Rights: fechado
Identifier DOI: 10.1016/j.plaphy.2010.01.001
Date Issue: 2010
Appears in Collections:Unicamp - Artigos e Outros Documentos

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