ATPase Activity and ATP-dependent Conformational Change in the Co-chaperone HSP70/HSP90-organizing Protein (HOP)

Co-chaperones help to maintain cellular homeostasis by modulating the activities of molecular chaperones involved in protein quality control. The HSP70/HSP90-organizing protein (HOP) is a co-chaperone that cooperates with HSP70 and HSP90 in catalysis of protein folding and maturation in the cytosol....

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Autores principales: Yamamoto, Soh, Subedi, Ganesh Prasad, Hanashima, Shinya, Satoh, Tadashi, Otaka, Michiro, Wakui, Hideki, Sawada, Ken-ichi, Yokota, Shin-ichi, Yamaguchi, Yoshiki, Kubota, Hiroshi, Itoh, Hideaki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2014
Materias:
Protein Structure and Folding
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3975032/
https://www.ncbi.nlm.nih.gov/pubmed/24535459
http://dx.doi.org/10.1074/jbc.M114.553255
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author Yamamoto, Soh
Subedi, Ganesh Prasad
Hanashima, Shinya
Satoh, Tadashi
Otaka, Michiro
Wakui, Hideki
Sawada, Ken-ichi
Yokota, Shin-ichi
Yamaguchi, Yoshiki
Kubota, Hiroshi
Itoh, Hideaki
author_facet Yamamoto, Soh
Subedi, Ganesh Prasad
Hanashima, Shinya
Satoh, Tadashi
Otaka, Michiro
Wakui, Hideki
Sawada, Ken-ichi
Yokota, Shin-ichi
Yamaguchi, Yoshiki
Kubota, Hiroshi
Itoh, Hideaki
author_sort Yamamoto, Soh
collection PubMed
description Co-chaperones help to maintain cellular homeostasis by modulating the activities of molecular chaperones involved in protein quality control. The HSP70/HSP90-organizing protein (HOP) is a co-chaperone that cooperates with HSP70 and HSP90 in catalysis of protein folding and maturation in the cytosol. We show here that HOP has ATP-binding activity comparable to that of HSP70/HSP90, and that HOP slowly hydrolyzes ATP. Analysis of deletion mutants revealed that the ATPase domain of HOP is in the N-terminal TPR1-DP1-TPR2A segment. In addition, HOP changes its conformation in the presence of ATP. These results indicate that HOP is a unique co-chaperone that undergoes an ATP-dependent conformational change.
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spelling pubmed-39750322014-04-04 ATPase Activity and ATP-dependent Conformational Change in the Co-chaperone HSP70/HSP90-organizing Protein (HOP) Yamamoto, Soh Subedi, Ganesh Prasad Hanashima, Shinya Satoh, Tadashi Otaka, Michiro Wakui, Hideki Sawada, Ken-ichi Yokota, Shin-ichi Yamaguchi, Yoshiki Kubota, Hiroshi Itoh, Hideaki J Biol Chem Protein Structure and Folding Co-chaperones help to maintain cellular homeostasis by modulating the activities of molecular chaperones involved in protein quality control. The HSP70/HSP90-organizing protein (HOP) is a co-chaperone that cooperates with HSP70 and HSP90 in catalysis of protein folding and maturation in the cytosol. We show here that HOP has ATP-binding activity comparable to that of HSP70/HSP90, and that HOP slowly hydrolyzes ATP. Analysis of deletion mutants revealed that the ATPase domain of HOP is in the N-terminal TPR1-DP1-TPR2A segment. In addition, HOP changes its conformation in the presence of ATP. These results indicate that HOP is a unique co-chaperone that undergoes an ATP-dependent conformational change. American Society for Biochemistry and Molecular Biology 2014-04-04 2014-02-17 /pmc/articles/PMC3975032/ /pubmed/24535459 http://dx.doi.org/10.1074/jbc.M114.553255 Text en © 2014 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version full access. Creative Commons Attribution Unported License (http://creativecommons.org/licenses/by/3.0/) applies to Author Choice Articles
spellingShingle Protein Structure and Folding
Yamamoto, Soh
Subedi, Ganesh Prasad
Hanashima, Shinya
Satoh, Tadashi
Otaka, Michiro
Wakui, Hideki
Sawada, Ken-ichi
Yokota, Shin-ichi
Yamaguchi, Yoshiki
Kubota, Hiroshi
Itoh, Hideaki
ATPase Activity and ATP-dependent Conformational Change in the Co-chaperone HSP70/HSP90-organizing Protein (HOP)
title ATPase Activity and ATP-dependent Conformational Change in the Co-chaperone HSP70/HSP90-organizing Protein (HOP)
title_full ATPase Activity and ATP-dependent Conformational Change in the Co-chaperone HSP70/HSP90-organizing Protein (HOP)
title_fullStr ATPase Activity and ATP-dependent Conformational Change in the Co-chaperone HSP70/HSP90-organizing Protein (HOP)
title_full_unstemmed ATPase Activity and ATP-dependent Conformational Change in the Co-chaperone HSP70/HSP90-organizing Protein (HOP)
title_short ATPase Activity and ATP-dependent Conformational Change in the Co-chaperone HSP70/HSP90-organizing Protein (HOP)
title_sort atpase activity and atp-dependent conformational change in the co-chaperone hsp70/hsp90-organizing protein (hop)
topic Protein Structure and Folding
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3975032/
https://www.ncbi.nlm.nih.gov/pubmed/24535459
http://dx.doi.org/10.1074/jbc.M114.553255
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