Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/199540
Type: Artigo de periódico
Title: Stoichiometry And Thermodynamics Of The Interaction Between The C-terminus Of Human 90kda Heat Shock Protein Hsp90 And The Mitochondrial Translocase Of Outer Membrane Tom70.
Author: Gava, Lisandra M
Gonçalves, Danieli C
Borges, Júlio C
Ramos, Carlos H I
Abstract: A large majority of the 1000-1500 proteins in the mitochondria are encoded by the nuclear genome, and therefore, they are translated in the cytosol in the form and contain signals to enable the import of proteins into the organelle. The TOM complex is the major translocase of the outer membrane responsible for preprotein translocation. It consists of a general import pore complex and two membrane import receptors, Tom20 and Tom70. Tom70 contains a characteristic TPR domain, which is a docking site for the Hsp70 and Hsp90 chaperones. These chaperones are involved in protecting cytosolic preproteins from aggregation and then in delivering them to the TOM complex. Although highly significant, many aspects of the interaction between Tom70 and Hsp90 are still uncertain. Thus, we used biophysical tools to study the interaction between the C-terminal domain of Hsp90 (C-Hsp90), which contains the EEVD motif that binds to TPR domains, and the cytosolic fragment of Tom70. The results indicate a stoichiometry of binding of one monomer of Tom70 per dimer of C-Hsp90 with a K(D) of 360±30nM, and the stoichiometry and thermodynamic parameters obtained suggested that Tom70 presents a different mechanism of interaction with Hsp90 when compared with other TPR proteins investigated.
Subject: Amino Acid Sequence
Biophysical Phenomena
Dimerization
Hsp90 Heat-shock Proteins
Humans
In Vitro Techniques
Kinetics
Mitochondrial Membrane Transport Proteins
Models, Molecular
Peptide Fragments
Protein Folding
Protein Interaction Domains And Motifs
Protein Structure, Quaternary
Recombinant Proteins
Thermodynamics
Rights: fechado
Identifier DOI: 10.1016/j.abb.2011.06.015
Address: http://www.ncbi.nlm.nih.gov/pubmed/21781956
Date Issue: 2011
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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