Abstract
High-ordered aggregates (amyloids) may disrupt cell functions, cause toxicity at certain conditions and provide a basis for self-perpetuated, protein-based infectious heritable agents (prions). Heat shock proteins acting as molecular chaperones counteract protein aggregation and influence amyloid propagation. The yeast Hsp104/Hsp70/Hsp40 chaperone complex plays a crucial role in interactions with both ordered and unordered aggregates. The main focus of this review will be on the Hsp104 chaperone, a molecular “disaggregase”.
Keywords: Hsp104, yeast prion, Saccharomyces cerevisiae, chaperone, amyloid
Protein & Peptide Letters
Title: Hsp104 and Prion Propagation
Volume: 16 Issue: 6
Author(s): Nina V. Romanova and Yury O. Chernoff
Affiliation:
Keywords: Hsp104, yeast prion, Saccharomyces cerevisiae, chaperone, amyloid
Abstract: High-ordered aggregates (amyloids) may disrupt cell functions, cause toxicity at certain conditions and provide a basis for self-perpetuated, protein-based infectious heritable agents (prions). Heat shock proteins acting as molecular chaperones counteract protein aggregation and influence amyloid propagation. The yeast Hsp104/Hsp70/Hsp40 chaperone complex plays a crucial role in interactions with both ordered and unordered aggregates. The main focus of this review will be on the Hsp104 chaperone, a molecular “disaggregase”.
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Cite this article as:
Romanova V. Nina and Chernoff O. Yury, Hsp104 and Prion Propagation, Protein & Peptide Letters 2009; 16 (6) . https://dx.doi.org/10.2174/092986609788490078
DOI https://dx.doi.org/10.2174/092986609788490078 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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