A switch point in the molecular chaperone Hsp90 responding to client interaction

Daniel Andreas Rutz, Qi Luo, Lee Freiburger, Tobias Madl, Ville R. I. Kaila, Michael Sattler and Johannes Buchner ()
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Daniel Andreas Rutz: Center for integrated protein science at the Department Chemie of the Technische Universität München
Qi Luo: Center for integrated protein science at the Department Chemie of the Technische Universität München
Lee Freiburger: Center for integrated protein science at the Department Chemie of the Technische Universität München
Tobias Madl: Helmholtz Zentrum München
Ville R. I. Kaila: Center for integrated protein science at the Department Chemie of the Technische Universität München
Michael Sattler: Center for integrated protein science at the Department Chemie of the Technische Universität München
Johannes Buchner: Center for integrated protein science at the Department Chemie of the Technische Universität München

Nature Communications, 2018, vol. 9, issue 1, 1-14

Abstract: Abstract Heat shock protein 90 (Hsp90) is a dimeric molecular chaperone that undergoes large conformational changes during its functional cycle. It has been established that conformational switch points exist in the N-terminal (Hsp90-N) and C-terminal (Hsp90-C) domains of Hsp90, however information for switch points in the large middle-domain (Hsp90-M) is scarce. Here we report on a tryptophan residue in Hsp90-M as a new type of switch point. Our study shows that this conserved tryptophan senses the interaction of Hsp90 with a stringent client protein and transfers this information via a cation–π interaction with a neighboring lysine. Mutations at this position hamper the communication between domains and the ability of a client protein to affect the Hsp90 cycle. The residue thus allows Hsp90 to transmit information on the binding of a client from Hsp90-M to Hsp90-N which is important for progression of the conformational cycle and the efficient processing of client proteins.

Date: 2018
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DOI: 10.1038/s41467-018-03946-x

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