Hsp104 and Prion Propagation

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”.

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