Reactivation of Aggregated Proteins by the ClpB/DnaK Bi-Chaperone System

Abstract

Protein aggregation is a common problem in protein biochemistry and is linked to many cellular pathologies and human diseases. The molecular chaperone ClpB can resolubilize and reactivate aggregated proteins. This unit describes the procedure for following reactivation of an aggregated enzyme glucose-6-phosphate dehydrogenase mediated by ClpB from Escherichia coli in cooperation with another molecular chaperone, DnaK. The procedures for purification of these chaperones are also described.

Keywords: ClpB; DnaK; molecular chaperone; protein aggregation; protein misfolding.