Hsp104 and Prion Propagation
Nina V. Romanova and Yury O. Chernoff
Affiliation: School of Biology and Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta GA, USA.
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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