Remodeling of Protein Aggregates by Hsp104

Title: Remodeling of Protein Aggregates by Hsp104

Volume: 16 Issue: 6

Author(s): John R. Glover and Ronnie Lum

Affiliation:

Abstract: Hsp104 is molecular chaperone in the AAA+ family of ATPases that specializes in the resolubilization and refolding of thermally denatured proteins in yeast. In addition to providing high levels of thermotolerance, Hsp104 plays a pivotal role in the propagation of yeast prions, self-replicating, amyloid-like aggregates that are inherited during mitosis and meiosis. In this review, the structure and function of Hsp104 is discussed, its functional interaction with other molecular chaperones, and a model for disaggregation and refolding is proposed.

Cite this article as:

Glover R. John and Lum Ronnie, Remodeling of Protein Aggregates by Hsp104, Protein & Peptide Letters 2009; 16 (6) . https://dx.doi.org/10.2174/092986609788490087