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Importance of cycle timing for the function of the molecular chaperone Hsp90.
Nat. Struct. Mol. Biol. 23, 1020-1028 (2016)
Hsp90 couples ATP hydrolysis to large conformational changes essential for activation of client proteins. The structural transitions involve dimerization of the N-terminal domains and formation of 'closed states' involving the N-terminal and middle domains. Here, we used Hsp90 mutants that modulate ATPase activity and biological function as probes to address the importance of conformational cycling for Hsp90 activity. We found no correlation between the speed of ATP turnover and the in vivo activity of Hsp90: some mutants with almost normal ATPase activity were lethal, and some mutants with lower or undetectable ATPase activity were viable. Our analysis showed that it is crucial for Hsp90 to attain and spend time in certain conformational states: a certain dwell time in open states is required for optimal processing of client proteins, whereas a prolonged population of closed states has negative effects. Thus, the timing of conformational transitions is crucial for Hsp90 function and not cycle speed.
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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
Heat-shock-protein; Escherichia-coli Hsp90; Atp Hydrolysis; In-vivo; Steroid-receptor; Client Protein; Mechanism; Nucleotide; Binding; Kinase
ISSN (print) / ISBN
1545-9993
e-ISSN
1545-9985
Zeitschrift
Nature Structural & Molecular Biology
Quellenangaben
Band: 23,
Heft: 11,
Seiten: 1020-1028
Verlag
Nature Publishing Group
Verlagsort
New York, NY
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Structural Biology (STB)