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Related Experiment Video

Updated: Jun 22, 2026

Purification of Hsp104, a Protein Disaggregase

Purification of Hsp104, a Protein Disaggregase

Published on: September 30, 2011

Hsp70 structure, function, regulation and influence on yeast prions.

Deepak Sharma¹, Daniel C Masison

¹Laboratory of Biochemistry and Genetics, National Institute of Diabetes, Digestive and Kidney Diseases, National institutes of Health, Bethesda, MD 20892-0851, USA.

Protein and Peptide Letters

|June 13, 2009

Summary

Heat shock proteins (Hsps), especially Hsp70, protect cells from stress by aiding protein folding. Co-chaperones fine-tune Hsp70

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Last Updated: Jun 22, 2026

Purification of Hsp104, a Protein Disaggregase

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Area of Science:

Molecular Biology
Cellular Stress Response
Protein Homeostasis

Background:

Heat shock proteins (Hsps) are crucial for cellular protection against various stressors.
Hsp70, a highly conserved Hsp, plays a vital role in maintaining protein conformation and function.
Co-chaperones modulate Hsp70 activity and substrate specificity.

Purpose of the Study:

To elucidate the structure and function of Hsp70.
To explore the regulatory mechanisms of Hsp70 by co-factors.
To investigate the role of Hsp70 in the propagation of yeast prions.

Main Methods:

Review of existing literature on Hsp70 structure and function.
Analysis of regulatory interactions between Hsp70 and co-chaperones.
Examination of Hsp70's involvement in prion biology.

Main Results:

Hsp70 assists proteins in achieving their native state or recovering function post-misfolding.
Co-chaperones significantly influence Hsp70's substrate range and functional outcomes.
Hsp70 impacts the propagation dynamics of yeast prions.

Conclusions:

Hsp70 is a central component of the cellular chaperone machinery.
Co-factor regulation is essential for Hsp70's diverse cellular roles.
Hsp70 influences the conformational templating characteristic of prion propagation.