Prof. Eli Chapman, Scripps Research Institute

ATP binding requirements and in vivo function of GroEL

The GroEL-GroES chaperonin system provides kinetic assistance to proteins as they fold amidst the challenges of the bacterial cytosol, providing a critical final step in the path from genetic information to effector protein. This incredible, near megadalton machinery harnesses the power of ATP-binding to drive large, rigid-body movements that lead to an enclosed, hydrophilic chamber, allowing a newly translated or stress-denatured polypeptide to fold in seclusion. Chaperonin function is essential in all organisms and comprises the only essential chaperone system in bacteria. This central role in organismal function and implications in diseases caused by protein malfunction necessitate a continued effort to understand chaperonin function. For these reasons, we have worked to understand the requirements of ATP in the GroEL-GroES refolding cycle, the physiologic function of GroEL, and how cellular insult affects GroEL sub-cellular
location.

For more information contact Prof. Loren Williams (404-894-9752).