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The Plasticity of the Hsp90 Co-chaperone System.
Sahasrabudhe, Priyanka; Rohrberg, Julia; Biebl, Maximillian M; Rutz, Daniel A; Buchner, Johannes.
Afiliación
  • Sahasrabudhe P; Center for Integrated Protein Science at the Department of Chemistry, Technische Universität München, 85748 Garching, Germany.
  • Rohrberg J; Center for Integrated Protein Science at the Department of Chemistry, Technische Universität München, 85748 Garching, Germany.
  • Biebl MM; Center for Integrated Protein Science at the Department of Chemistry, Technische Universität München, 85748 Garching, Germany.
  • Rutz DA; Center for Integrated Protein Science at the Department of Chemistry, Technische Universität München, 85748 Garching, Germany.
  • Buchner J; Center for Integrated Protein Science at the Department of Chemistry, Technische Universität München, 85748 Garching, Germany. Electronic address: johannes.buchner@tum.de.
Mol Cell ; 67(6): 947-961.e5, 2017 Sep 21.
Article en En | MEDLINE | ID: mdl-28890336
The Hsp90 system in the eukaryotic cytosol is characterized by a cohort of co-chaperones that bind to Hsp90 and affect its function. Although progress has been made regarding the underlying biochemical mechanisms, how co-chaperones influence Hsp90 client proteins in vivo has remained elusive. By investigating the effect of 12 Hsp90 co-chaperones on the activity of different client proteins in yeast, we find that deletion of co-chaperones can have a neutral or negative effect on client activity but can also lead to more active clients. Only a few co-chaperones are active on all clients studied. Closely related clients and even point mutants can depend on different co-chaperones. These effects are direct because differences in client-co-chaperone interactions can be reconstituted in vitro. Interestingly, some co-chaperones affect client conformation in vivo. Thus, co-chaperones adapt the Hsp90 cycle to the requirements of the client proteins, ensuring optimal activation.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Proteínas HSP90 de Choque Térmico / Proteínas de Saccharomyces cerevisiae / Proteínas Adaptadoras Transductoras de Señales / Plasticidad de la Célula Idioma: En Revista: Mol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2017 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Proteínas HSP90 de Choque Térmico / Proteínas de Saccharomyces cerevisiae / Proteínas Adaptadoras Transductoras de Señales / Plasticidad de la Célula Idioma: En Revista: Mol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2017 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos