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Protein & Peptide Letters
ISSN (Print): 0929-8665
ISSN (Online): 1875-5305
VOLUME: 16
ISSUE: 6
DOI: 10.2174/092986609788490078      Price:  $58









Hsp104 and Prion Propagation

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Author(s): Nina V. Romanova and Yury O. Chernoff
Pages 598-605 (8)
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
Affiliation:
School of Biology and Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta GA, USA.