Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/56524
Type: Artigo de periódico
Title: Conformational and functional studies of a cytosolic 90 kDa heat shock protein Hsp90 from sugarcane
Author: da Silva, VCH
Cagliari, TC
Lima, TB
Gozzo, FC
Ramos, CHI
Abstract: Hsp90s are involved in several cellular processes, such as signaling, proteostasis, epigenetics, differentiation and stress defense. Although Hsp90s from different organisms are highly similar, they usually have small variations in conformation and function. Thus, the characterization of different Hsp90s is important to gain insight into the structure function relationship that makes these chaperones key regulators in protein homeostasis. This work describes the characterization of a cytosolic Hsp90 from sugarcane and its comparison with Hsp90s from other plants. Previous expressed sequence tag (EST) studies in Saccharum spp. (sugarcane) predicted the presence of an mRNA coding for a cytosolic Hsp90. The corresponding cDNA was cloned, and the recombinant protein was purified and its conformation and function characterized. The structural conformation of Hsp90 was assessed by chemical cross-linking and hydrogen/deuterium exchange using mass spectrometry and hydrodynamic assays, which revealed regions accessible to solvent and that Hsp90 is an elongated dimer in solution. The in vivo expression of Hsp90 in sugarcane leaves was confirmed by western blot, and in vitro functional characterization indicated that sugarcane Hsp90 has strong chaperone activity. (C) 2013 Elsevier Masson SAS. All rights reserved.
Subject: Hsp90
Sugarcane
Protein folding
Molecular chaperone
Heat shock protein
Country: França
Editor: Elsevier France-editions Scientifiques Medicales Elsevier
Rights: fechado
Identifier DOI: 10.1016/j.plaphy.2013.03.015
Date Issue: 2013
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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