Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/74718
Type: Artigo de periódico
Title: Sugarcane Hsp101 is a hexameric chaperone that binds nucleotides
Author: Cagliari, TC
da Silva, VCH
Borges, JC
Prando, A
Tasic, L
Ramos, CHI
Abstract: The Clp/Hsp100 AAA+ chaperone family is involved in recovering aggregated proteins and little is known about other orthologs of the well studied ClpB from Escherichia coli and Hsp104 from Saccharomyces cerevisiae. Plant Hsp101 is a good model for understanding the relationship between the structure and function of Hsp100 proteins and to investigate the role of these chaperones in disaggregation processes. Here, we present the cloning and purification of a sugarcane ortholog. SHsp101 which is expressed in sugarcane cells and is a folded hexamer that is capable of binding nucleotides. Thus SHsp101 has the structural and functional characteristics of the Clp/Hsp100 AAA+ family. (C) 2011 Elsevier B.V. All rights reserved.
Subject: Hsp101
Sugarcane
Protein folding
Molecular chaperone
Heat shock protein
AAA plus protein
Analytical ultracentrifugation
STD-NMR
Country: Holanda
Editor: Elsevier Science Bv
Rights: fechado
Identifier DOI: 10.1016/j.ijbiomac.2011.08.027
Date Issue: 2011
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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