Journal
BIOLOGICAL CHEMISTRY
Volume 386, Issue 8, Pages 739-744Publisher
WALTER DE GRUYTER GMBH
DOI: 10.1515/BC.2005.086
Keywords
AAA plus protein; chaperone; ClpB; DnaK; Hsp104; Hsp70; protein disaggregation
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Cell survival under severe thermal stress requires the activity of a bi-chaperone system, consisting of the ringforming AAA+ chaperone ClpB (Hsp104) and the DnaK (Hsp70) chaperone system, which acts to solubilize and reactivate aggregated proteins. Recent studies have provided novel insight into the mechanism of protein disaggregation, demonstrating that ClpB/Hsp104 extracts unfolded polypeptides from. an aggregate by threading them through its central pore. This translocation activity is necessary but not sufficient for aggregate solubilization. In addition, the middle (M) domain of ClpB and the DnaK system have essential roles, possibly by providing an unfolding force, which facilitates the extraction of misfolded proteins from aggregates.
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