Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/198710
Type: Artigo de periódico
Title: Heat Causes Oligomeric Disassembly And Increases The Chaperone Activity Of Small Heat Shock Proteins From Sugarcane.
Author: Tiroli-Cepeda, Ana O
Ramos, Carlos H I
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.
Subject: Adaptation, Physiological
Heat-shock Proteins, Small
Heat-shock Response
Hot Temperature
Molecular Chaperones
Plant Proteins
Plant Shoots
Protein Binding
Protein Multimerization
Saccharum
Rights: fechado
Identifier DOI: 10.1016/j.plaphy.2010.01.001
Address: http://www.ncbi.nlm.nih.gov/pubmed/20137963
Date Issue: -1-Uns- -1
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File SizeFormat 
pmed_20137963.pdf875.3 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.