Aggregate reactivation mediated by the Hsp100 chaperones.
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.
Department of Biochemistry, Kansas State University, Manhattan, 66506, USA. michalz@ksu.edu
Michal
M
Zolkiewski
Ting
T
Zhang
Maria
M
Nagy
D001665:Binding Sites; D003198:Computer Simulation; D019281:Dimerization; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D008956:Models, Chemical; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry* / Q000648:ultrastructure*; D046912:Multiprotein Complexes / Q000737:chemistry / Q000648:ultrastructure; D011485:Protein Binding; D011487:Protein Conformation
D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D046912:Multiprotein Complexes