ATPases chaperone activity

Needham P, Masison D (2008) Prion-impairing mutations in Hsp70 chaperone Ssal effects on ATPase and chaperone activities. Arch Biochem Biophys 478 167-174... 

These proteins show differences in their cycles that have implications for their chaperone activities. We will use the available data to provide for these homologs a comparative description of the mechanistic features of the ATPase cycles, the substrate binding features, the coupling mechanism, and the regulation by co-chaperones. 

III. Chaperone Activity of Clp ATPases and Their Participation in Proteolysis. . 415... 

Several mechanistic aspects regarding the chaperone activity of Clp ATPases and their role in proteolysis have emerged from these structural studies (1) The active sites of the protease are sequestered from the cytoplasm and thus are not in a position to degrade most cellular... 

F. J. Corrales and A. R. Fersht, Toward a mechanism of GroEL-GroES chaperone activity An ATPase-gated and pulsed folding and annealing cage. Proc. Natl. Acad. Sci. USA 93, 4509-... 

Most chaperones show associated ATPase activity, with ATP or ADP being involved in the protein-chaperone interaction... 

The six ATPases belong to the rather large family of AAA ATPases (for ATPases Associated with a variety of cellular Activities) whose eukaryotic members include the motor protein dynein, the membrane fusion factor NSF, and the chaperone... 

Figure 19.22 The gatekeeping or filtering activity of the GroEL ATPase. The turnover number for the ATPase reaction (0.05-0.1 s-"1) is far slower than the refolding rate constant of 2-2.5 s-1 for GroEL-bound bamase. Only slowly folding proteins bind long enough to enter the chaperoning cycles of Figure 19.23.

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