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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
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Hsp90 interaction with clients.

G Elif Karagöz1, Stefan G D Rüdiger2

  • 1Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94158, USA.

Trends in Biochemical Sciences
|January 13, 2015
PubMed
Summary

Heat shock protein 90 (Hsp90) acts as a molecular chaperone, guiding protein folding and stability. Its unique binding mechanism ensures proper client protein interaction within the cellular chaperone network.

Keywords:
Alzheimer diseaseheat shock proteinsintrinsically disordered proteinsmolecular chaperonesprotein foldingprotein–protein interactions

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Area of Science:

  • Molecular biology
  • Cellular biology
  • Protein biochemistry

Background:

  • Heat shock protein 90 (Hsp90) is a crucial ATP-dependent molecular chaperone.
  • Hsp90 assists in the folding, stability, and function of a specific subset of proteins, known as clients.
  • Understanding Hsp90's client specificity and its role in the chaperone cascade is vital for cellular proteostasis.

Purpose of the Study:

  • To elucidate the mechanism of Hsp90 client specificity.
  • To describe the role of Hsp90 within the broader cellular chaperone network.
  • To present an emerging model for Hsp90's ATPase activity in client handling.

Main Methods:

  • Analysis of Hsp90's substrate binding interface.
  • Integration of emerging data on chaperone interactions.
  • Discussion of existing models for Hsp90 function.

Main Results:

  • Hsp90 possesses an extended substrate-binding interface recognizing hydrophobic residues across large protein areas.
  • Hsp90 specificity favors downstream folding intermediates, distinct from Hsp70's early-stage client preference.
  • The Hsp90 ATPase cycle appears to regulate client transfer from Hsp70, not direct client binding affinity.

Conclusions:

  • Hsp90's unique binding interface dictates its specificity for partially or fully folded proteins.
  • The chaperone cascade ensures that Hsp70 handles early folding states, while Hsp90 manages later intermediates.
  • Hsp90's ATPase activity is proposed to control the influx of substrates from Hsp70, refining the chaperone-client interaction.