Abstract
Hsp104 is molecular chaperone in the AAA+ family of ATPases that specializes in the resolubilization and refolding of thermally denatured proteins in yeast. In addition to providing high levels of thermotolerance, Hsp104 plays a pivotal role in the propagation of yeast prions, self-replicating, amyloid-like aggregates that are inherited during mitosis and meiosis. In this review, the structure and function of Hsp104 is discussed, its functional interaction with other molecular chaperones, and a model for disaggregation and refolding is proposed.
Protein & Peptide Letters
Title: Remodeling of Protein Aggregates by Hsp104
Volume: 16 Issue: 6
Author(s): John R. Glover and Ronnie Lum
Affiliation:
Abstract: Hsp104 is molecular chaperone in the AAA+ family of ATPases that specializes in the resolubilization and refolding of thermally denatured proteins in yeast. In addition to providing high levels of thermotolerance, Hsp104 plays a pivotal role in the propagation of yeast prions, self-replicating, amyloid-like aggregates that are inherited during mitosis and meiosis. In this review, the structure and function of Hsp104 is discussed, its functional interaction with other molecular chaperones, and a model for disaggregation and refolding is proposed.
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Cite this article as:
Glover R. John and Lum Ronnie, Remodeling of Protein Aggregates by Hsp104, Protein & Peptide Letters 2009; 16 (6) . https://dx.doi.org/10.2174/092986609788490087
DOI https://dx.doi.org/10.2174/092986609788490087 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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