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Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology
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Functional and physical interaction between yeast Hsp90 and Hsp70.

Andrea N Kravats1, Joel R Hoskins1, Michael Reidy2

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Proceedings of the National Academy of Sciences of the United States of America
|February 22, 2018
PubMed
Summary

Yeast heat shock protein 90 (Hsp90) directly interacts with heat shock protein 70 (Hsp70) via its middle domain. This interaction is crucial for protein remodeling and cellular function, especially under heat stress.

Keywords:
Hsp82Ssa1Sti1Ydj1molecular chaperones

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Area of Science:

  • Molecular biology
  • Cellular biology
  • Biochemistry

Background:

  • Heat shock protein 90 (Hsp90) is a vital ATP-dependent molecular chaperone in eukaryotes.
  • Hsp90 stabilizes over 200 client proteins, including kinases and receptors, regulating cell signaling.
  • Hsp90 function relies on cochaperones, notably Hsp70, with Hop mediating their indirect interaction in higher eukaryotes.

Purpose of the Study:

  • To investigate the direct interaction between yeast Hsp90 (Hsp82) and yeast Hsp70 (Ssa1) in vitro.
  • To identify the specific region in yeast Hsp90 responsible for this interaction.
  • To understand the in vivo and in vitro consequences of mutations in this interaction region.

Main Methods:

  • In vitro binding assays using purified yeast Hsp90 and Hsp70.
  • Site-directed mutagenesis of yeast Hsp90 to create substitution mutants.
  • Analysis of yeast growth at high temperatures.
  • Co-immunoprecipitation assays using cell lysates to assess protein interactions.
  • In vitro protein remodeling assays.

Main Results:

  • Yeast Hsp90 and Hsp70 directly interact in vitro, independent of the Hop homolog (Sti1).
  • A specific region in the middle domain of yeast Hsp90 is essential for this direct interaction.
  • Mutations in this region impair yeast growth at high temperatures and reduce Hsp70 interaction in vivo.
  • Purified Hsp90 mutants exhibit defective physical interaction with Hsp70 and impaired protein remodeling activity in vitro.
  • This Hsp90 region is also critical for interactions with other cochaperones and client proteins.

Conclusions:

  • Yeast Hsp90 and Hsp70 can interact directly, challenging the model of exclusively indirect interaction mediated by Hop in higher eukaryotes.
  • A conserved middle domain region of Hsp90 is a key interface for direct Hsp70 interaction and protein remodeling.
  • Competition between Hsp70 and other Hsp90 cochaperones for this interaction surface may regulate Hsp90 chaperone activity.