The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation

Rebecca Mercier; Annemarie Wolmarans; Jonathan Schubert; Hannes Neuweiler; Jill L. Johnson; Paul LaPointe

doi:10.1038/s41467-019-09299-3

Nature Communications (Mar 2019)

The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation

Rebecca Mercier,
Annemarie Wolmarans,
Jonathan Schubert,
Hannes Neuweiler,
Jill L. Johnson,
Paul LaPointe

Affiliations

Rebecca Mercier: Department of Cell Biology, Faculty of Medicine and Dentistry, University of Alberta
Annemarie Wolmarans: Department of Cell Biology, Faculty of Medicine and Dentistry, University of Alberta
Jonathan Schubert: Department of Biotechnology and Biophysics, University of Würzburg
Hannes Neuweiler: Department of Biotechnology and Biophysics, University of Würzburg
Jill L. Johnson: Department of Biological Sciences and the Center for Reproductive Biology, University of Idaho
Paul LaPointe: Department of Cell Biology, Faculty of Medicine and Dentistry, University of Alberta

DOI: https://doi.org/10.1038/s41467-019-09299-3
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 12

Abstract

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Hsp90 is a molecular chaperone that acts together with co-chaperones to ensure folding and activation of many client proteins. Here authors show that a N-terminal motif in Aha-type co-chaperones modulates the apparent affinity of Hsp90 for nucleotide substrates.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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