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The Co-chaperone Cns1 and the Recruiter Protein Hgh1 Link Hsp90 to Translation Elongation via Chaperoning Elongation Factor 2.
Schopf, Florian H; Huber, Eva M; Dodt, Christopher; Lopez, Abraham; Biebl, Maximilian M; Rutz, Daniel A; Mühlhofer, Moritz; Richter, Gesa; Madl, Tobias; Sattler, Michael; Groll, Michael; Buchner, Johannes.
Afiliación
  • Schopf FH; Center for Integrated Protein Science at the Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany.
  • Huber EM; Center for Integrated Protein Science at the Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany.
  • Dodt C; Center for Integrated Protein Science at the Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany.
  • Lopez A; Center for Integrated Protein Science at the Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany; Institute of Structural Biology, Helmholtz Zentrum München, 85764 Neuherberg, Germany.
  • Biebl MM; Center for Integrated Protein Science at the Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany.
  • Rutz DA; Center for Integrated Protein Science at the Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany.
  • Mühlhofer M; Center for Integrated Protein Science at the Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany.
  • Richter G; Center for Integrated Protein Science at the Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany; Gottfried Schatz Research Center, Medical University of Graz, 8036 Graz, Austria.
  • Madl T; Center for Integrated Protein Science at the Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany; Gottfried Schatz Research Center, Medical University of Graz, 8036 Graz, Austria; BioTechMed-Graz, 8010 Graz, Austria.
  • Sattler M; Center for Integrated Protein Science at the Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany; Institute of Structural Biology, Helmholtz Zentrum München, 85764 Neuherberg, Germany.
  • Groll M; Center for Integrated Protein Science at the Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany.
  • Buchner J; Center for Integrated Protein Science at the Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany. Electronic address: johannes.buchner@tum.de.
Mol Cell ; 74(1): 73-87.e8, 2019 04 04.
Article en En | MEDLINE | ID: mdl-30876805
The Hsp90 chaperone machinery in eukaryotes comprises a number of distinct accessory factors. Cns1 is one of the few essential co-chaperones in yeast, but its structure and function remained unknown. Here, we report the X-ray structure of the Cns1 fold and NMR studies on the partly disordered, essential segment of the protein. We demonstrate that Cns1 is important for maintaining translation elongation, specifically chaperoning the elongation factor eEF2. In this context, Cns1 interacts with the novel co-factor Hgh1 and forms a quaternary complex together with eEF2 and Hsp90. The in vivo folding and solubility of eEF2 depend on the presence of these proteins. Chaperoning of eEF2 by Cns1 is essential for yeast viability and requires a defined subset of the Hsp90 machinery as well as the identified eEF2 recruiting factor Hgh1.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Extensión de la Cadena Peptídica de Translación / Saccharomyces cerevisiae / Chaperonas Moleculares / Proteínas HSP90 de Choque Térmico / Factor 2 de Elongación Peptídica / Proteínas de Saccharomyces cerevisiae / Péptidos y Proteínas de Señalización Intracelular Tipo de estudio: Prognostic_studies Idioma: En Revista: Mol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2019 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Extensión de la Cadena Peptídica de Translación / Saccharomyces cerevisiae / Chaperonas Moleculares / Proteínas HSP90 de Choque Térmico / Factor 2 de Elongación Peptídica / Proteínas de Saccharomyces cerevisiae / Péptidos y Proteínas de Señalización Intracelular Tipo de estudio: Prognostic_studies Idioma: En Revista: Mol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2019 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos