THE ROLE OF ATP HYDROLYSIS IN THE FUNCTION OF THE CHAPERONIN GROEL - DYNAMIC COMPLEX-FORMATION WITH GROES

In order to understand the role of ATP hydrolysis of the chaperonin Gr oEL during protein folding, we have studied GroEL-GroES complex format ion in the presence of ATP or ADP by using capillary electrophoresis a nd surface plasmon resonance. Capillary electrophoresis analysis showe d that the GroEL 14-mer and GroES 7-mer formed a 1:1 complex in the pr esence of ATP. In the presence of ADP, both the association and dissoc iation rates of the complex were slower by about one order of magnitud e than the rates in the presence of ATP at 25 degrees C. The implicati ons of such a stable complex on the overall mechanism of chaperonin fu nction are discussed.