Protein & Peptide Letters

Prof. Ben M. Dunn  
Department of Biochemistry and Molecular Biology
University of Florida
College of Medicine
P.O. Box 100245
Gainesville, FL
USA
Email: bdunn@ufl.edu

Back

Hsp104 and Prion Propagation

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

Affiliation: School of Biology and Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta GA, USA.

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”.

Reprint ePrint Rights & PermissionsPrintExport

Article Details

VOLUME: 16
ISSUE: 6
Page: [598 - 605]
Pages: 8
DOI: 10.2174/092986609788490078