Hsp104 and Prion Propagation

Author(s): Nina V. Romanova, Yury O. Chernoff

Journal Name: Protein & Peptide Letters

Volume 16 , Issue 6 , 2009

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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

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Article Details

Year: 2009
Published on: 01 March, 2012
Page: [598 - 605]
Pages: 8
DOI: 10.2174/092986609788490078
Price: $65

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