Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/200602
Type: Artigo de periódico
Title: Conformational And Functional Studies Of A Cytosolic 90 kda Heat Shock Protein Hsp90 From Sugarcane.
Author: da Silva, Viviane C H
Cagliari, Thiago C
Lima, Tatiani B
Gozzo, Fábio C
Ramos, Carlos H I
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.
Subject: Amino Acid Sequence
Cloning, Molecular
Cytosol
Hsp90 Heat-shock Proteins
Mass Spectrometry
Models, Molecular
Molecular Chaperones
Molecular Sequence Data
Plant Leaves
Plant Proteins
Protein Conformation
Protein Structure, Tertiary
Saccharum
Sequence Homology, Amino Acid
Rights: fechado
Identifier DOI: 10.1016/j.plaphy.2013.03.015
Address: http://www.ncbi.nlm.nih.gov/pubmed/23619240
Date Issue: 2013
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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