ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis

Hsp60 and Hsp70, the molecular chaperone proteins, bind themselves to short peptides and unfolded proteins when twisted in the cell functions under stress induced and normal conditions. The disintegration of the substrate polypeptides from the chaperone is caused by the addition of Mg-ATP, and occurs since the ATP analogue is not capable of replacing ATP. The disintegration Hsp 70-substrate proteins require the hydrolysis of the Mg-ATP in addition to the earlier mentioned reactions. Mg-ATP binding is more essential than the Mg-ATP hydrolysis to the disintegration of the molecular chaperone proteins.