Chaperones ATPase activity

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

Panaretou, B. et al. 2002. Activation of the ATPase activity of hsp90 by the stress-regulated co-chaperone ahal. Mol. Cell 10, 1307-1318. 

Fewell SW, Smith CM, Lyon MA et al (2004) Small molecule modulators of endogenous and co-chaperone-stimulated Hsp70 ATPase activity. J Biol Chem 279 51131-51140... 

Members of the hspVO family of stress proteins bind the GSL 3 sulfogalactosyl ceramide (SGC) (207). The binding site is in the N-terminal ATPase domain (208). Adamantyl SGC, similarly generated via fatty acid replacement, similarly has proven water soluble and is an effective inhibitor of hsp70-SGC binding (200). Adamantyl SGC has been shown to inhibit hsp70 ATPase activity (209) in vitro and therefore may modulate its chaperone function in cells. Such an effect also has therapeutic potential (210). 

The high level of a protein complex with ATPase activity in P. occultum at temperatures near the upper growth limit (11% of the soluble protein at the growth optimum of 100 C 73% at 108 C [53]) led to the suggestion that this protein may be essential for growth at the upper temperature limits of life. Unfortunately, no experimental data are yet available giving information about its physiological role. From its quaternary structure it was concluded that this abundant protein may function as a chaperone. 

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