Examining the function and regulation of hsp 70 in cells subjected to metabolic stress

The effects of metabolic stress on the folding pathway of developing proteins and their responses to induced stress were investigated. Cells exposed to amino acid analog or sodium arsenite exhibited inability of newly synthesized proteins to properly fold and remained attached to their respective heat-shock protein (hsp) 70. Maturing proteins became insolouble upon heat shock treatment and showed increased number of hsp 72/73. ATP depletion in cells resulted in the inhibition of hsp 70 release from developing proteins. The results indicated that the effects and responses of proteins to metabolicstress depend on the kind and severity of the induced stress.