Hsp104 and Prion Propagation

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

Journal Name: Protein & Peptide Letters

Volume 16 , Issue 6 , 2009

Become EABM
Become Reviewer

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

Rights & PermissionsPrintExport Cite as

Article Details

VOLUME: 16
ISSUE: 6
Year: 2009
Page: [598 - 605]
Pages: 8
DOI: 10.2174/092986609788490078
Price: $65

Article Metrics

PDF: 6

Special-new-year-discount