Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/199627
Type: Artigo de periódico
Title: Sugarcane Hsp101 Is A Hexameric Chaperone That Binds Nucleotides.
Author: Cagliari, Thiago C
da Silva, Viviane C H
Borges, Júlio C
Prando, Alessandra
Tasic, Ljubica
Ramos, Carlos H I
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.
Subject: Amino Acid Sequence
Chimera
Cloning, Molecular
Escherichia Coli
Escherichia Coli Proteins
Heat-shock Proteins
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Chaperones
Molecular Sequence Data
Nucleotides
Plant Proteins
Plasmids
Polymerization
Protein Binding
Protein Folding
Protein Structure, Tertiary
Recombinant Proteins
Saccharomyces Cerevisiae
Saccharomyces Cerevisiae Proteins
Saccharum
Structure-activity Relationship
Transcription Factors
Ultracentrifugation
Rights: fechado
Identifier DOI: 10.1016/j.ijbiomac.2011.08.027
Address: http://www.ncbi.nlm.nih.gov/pubmed/21903129
Date Issue: 2011
Appears in Collections:Unicamp - Artigos e Outros Documentos

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