Cochaperones convey the energy of ATP hydrolysis for directional action of Hsp90

Leonie Vollmar, Julia Schimpf, Bianca Hermann and Thorsten Hugel ()
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Leonie Vollmar: University of Freiburg
Julia Schimpf: University of Freiburg
Bianca Hermann: University of Freiburg
Thorsten Hugel: University of Freiburg

Nature Communications, 2024, vol. 15, issue 1, 1-11

Abstract: Abstract The molecular chaperone and heat shock protein Hsp90 is part of many protein complexes in eukaryotic cells. Together with its cochaperones, Hsp90 is responsible for the maturation of hundreds of clients. Although having been investigated for decades, it still is largely unknown which components are necessary for a functional complex and how the energy of ATP hydrolysis is used to enable cyclic operation. Here we use single-molecule FRET to show how cochaperones introduce directionality into Hsp90’s conformational changes during its interaction with the client kinase Ste11. Three cochaperones are needed to couple ATP turnover to these conformational changes. All three are therefore essential for a functional cyclic operation, which requires coupling to an energy source. Finally, our findings show how the formation of sub-complexes in equilibrium followed by a directed selection of the functional complex can be the most energy efficient pathway for kinase maturation.

Date: 2024
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DOI: 10.1038/s41467-024-44847-6

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