Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 520, Issue 1, Pages 1-6Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2012.01.012
Keywords
Protein aggregation; Aggregate reactivation; Molecular chaperone; ClpB; Hsp104; AAA plus ATPase
Categories
Funding
- National Institutes of Health [R01GM079277]
- C. Johnson Center for Basic Cancer Research
- Kansas Agricultural Experiment Station [12-233-J]
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Hsp100 family of molecular chaperones shows a unique capability to resolubilize and reactivate aggregated proteins. The Hsp100-mediated protein disaggregation is linked to the activity of other chaperones from the Hsp70 and Hsp40 families. The best-studied members of the Hsp100 family are the bacterial ClpB and Hsp104 from yeast. Hsp100 chaperones are members of a large super-family of energy-driven conformational machines known as AAA+ ATPases. This review describes the current mechanistic model of the chaperone-induced protein disaggregation and explains how the structural architecture of Hsp100 supports disaggregation and how the co-chaperones may participate in the Hsp100-mediated reactions. (C) 2012 Elsevier Inc. All rights reserved.
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