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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Detalles Bibliográficos
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
Descripción
Sumario: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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