1. Hsp104 and Prion Propagation
- Author
-
Yury O. Chernoff and Nina V. Romanova
- Subjects
Amyloid ,Saccharomyces cerevisiae Proteins ,biology ,Prions ,General Medicine ,Protein aggregation ,Biochemistry ,Article ,Yeast ,Cell biology ,Hsp70 ,Fungal prion ,Structural Biology ,Chaperone (protein) ,Heat shock protein ,biology.protein ,Chaperone complex ,Heat-Shock Proteins - 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".
- Published
- 2009
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