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

Author

Listed:
  • Rebecca Mercier

    (University of Alberta)

  • Annemarie Wolmarans

    (University of Alberta)

  • Jonathan Schubert

    (University of Würzburg)

  • Hannes Neuweiler

    (University of Würzburg)

  • Jill L. Johnson

    (University of Idaho)

  • Paul LaPointe

    (University of Alberta)

Abstract

Hsp90 is a dimeric molecular chaperone that is essential for the folding and activation of hundreds of client proteins. Co-chaperone proteins regulate the ATP-driven Hsp90 client activation cycle. Aha-type co-chaperones are the most potent stimulators of the Hsp90 ATPase activity but the relationship between ATPase regulation and in vivo activity is poorly understood. We report here that the most strongly conserved region of Aha-type co-chaperones, the N terminal NxNNWHW motif, modulates the apparent affinity of Hsp90 for nucleotide substrates. The ability of yeast Aha-type co-chaperones to act in vivo is ablated when the N terminal NxNNWHW motif is removed. This work suggests that nucleotide exchange during the Hsp90 functional cycle may be more important than rate of catalysis.

Suggested Citation

  • Rebecca Mercier & Annemarie Wolmarans & Jonathan Schubert & Hannes Neuweiler & Jill L. Johnson & Paul LaPointe, 2019. "The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation," Nature Communications, Nature, vol. 10(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-09299-3
    DOI: 10.1038/s41467-019-09299-3
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    Cited by:

    1. Michael Reidy & Kevin Garzillo & Daniel C. Masison, 2023. "Nucleotide exchange is sufficient for Hsp90 functions in vivo," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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