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- ISSN: 0929-8665
- E-ISSN: 1875-5305
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Remodeling of Protein Aggregates by Hsp104
- Source: Protein and Peptide Letters, Volume 16, Issue 6, Jun 2009, p. 587 - 597
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- 01 Jun 2009
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.
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