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The essential co-chaperone Sgt1 regulates client dwell time in the Hsp90 chaperone cycle.
Mol. Cell 86, 166-179.e6 (2026)
The Hsp90 molecular chaperone system is regulated by numerous co-chaperones that modulate its function. In Saccharomyces cerevisiae, most of these cofactors can be deleted without affecting viability. Of the three essential ones, only the function of Sgt1 has remained enigmatic. Our in vivo and in vitro experiments define key structural elements and determine the essential function of Sgt1 in the chaperoning of client proteins. We demonstrate that yeast Sgt1 adopts a unique binding mode, engaging primarily with the middle domain of Hsp90. Through simultaneous interaction with both Hsp90 and client proteins, Sgt1 enhances client maturation efficiency. Specifically, Sgt1 stabilizes Hsp90-client complexes and prevents their dissociation by the co-chaperone Aha1. Our findings reveal a previously unrecognized layer of Hsp90 regulation, highlighting Sgt1 as a critical modulator of chaperone cycle progression.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Aha1 ; Hsp90 ; Nmr Spectroscopy ; Sgt1 ; Co-chaperones ; Glucocorticoid Receptor ; Molecular Chaperones ; Protein Folding
ISSN (print) / ISBN
1097-2765
e-ISSN
1097-4164
Journal
Molecular Cell
Quellenangaben
Volume: 86,
Issue: 1,
Pages: 166-179.e6
Publisher
Elsevier
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)