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Updated: Jun 30, 2025

Purification of Hsp104, a Protein Disaggregase
Published on: September 30, 2011
Target-locked: A mechanism for disaggregase binding to aggregated proteins
Trevor M Morey1, Walid A Houry2
1Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada.
Abstract:
ClpG is a novel autonomous disaggregase found in Pseudomonas aeruginosa that confers resistance to lethal heat stress. The mechanism by which ClpG specifically targets protein aggregates for disaggregation is unknown. In their recent work published in JBC, Katikaridis et al. (2023) identify an avidity-based mechanism by which four or more ClpG subunits, through specific N-terminal hydrophobic residues located on an exposed β-sheet loop, interact with multiple hydrophobic patches on an aggregated protein substrate. This study establishes a model for substrate binding to a prokaryotic disaggregase that should inform further investigations into other autonomous disaggregases.
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