Remodeling of Protein Aggregates by Hsp104

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

Journal Name: Protein & Peptide Letters

Volume 16 , Issue 6 , 2009

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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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Article Details

VOLUME: 16
ISSUE: 6
Year: 2009
Page: [587 - 597]
Pages: 11
DOI: 10.2174/092986609788490087
Price: $65

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