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Schopf, F.H.* ; Huber, E.M.* ; Dodt, C.* ; Lopez, A. ; Biebl, M.M.* ; Rutz, D.A.* ; Mühlhofer, M.* ; Richter, G.* ; Madl, T.* ; Sattler, M. ; Groll, M.* ; Buchner, J.*

The co-chaperone Cnsl and the recruiter protein Hgh1 Link Hsp90 to translation elongation via chaperoning elongation factor 2.

Mol. Cell 74, 73-87.e8 (2019)
Publ. Version/Full Text Postprint Research data DOI
Open Access Green
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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Publication type Article: Journal article
Document type Scientific Article
Keywords Cns1 ; Co-chaperones ; Cpr7 ; Eef2 ; Hsp90 ; Molecular Chaperones ; S. Cerevisiae ; Ssa1; Saccharomyces-cerevisiae; Interaction Network; Human Interactome; Yeast Genes; Complexes; Systems; Domain; Identification; Architecture; Scattering
ISSN (print) / ISBN 1097-2765
e-ISSN 1097-4164
Journal Molecular Cell
Quellenangaben Volume: 74, Issue: 1, Pages: 73-87.e8 Article Number: , Supplement: ,
Publisher Elsevier
Publishing Place 50 Hampshire St, Floor 5, Cambridge, Ma 02139 Usa
Reviewing status Peer reviewed