CHAPERONIN GROE AND ADP FACILITATE THE FOLDING OF VARIOUS PROTEINS AND PROTECT AGAINST HEAT INACTIVATION

In the presence of ADP, the molecular chaperones GroEL and GroES from Escherichia coli not only facilitated the refolding of various proteins, but also prevented their irreversible heat inactivation in vitro. Without nucleotides the refolding reactions were arrested by GroEL. Addition of GroES and ADP to the reaction mixture initiated the refolding reactions and the enzyme activities were regained efficiently. The presence of GroE (GroEL and GroES) and ADP also protected against heat inactivation of native enzymes at various temperatures. These findings suggest that in the presence of GroES, nucleotide binding is an important event in the mechanism of GroEL-facilitated protein folding.