Abstract
FtsH protease is an ATP dependent protease whose function is to degrade damaged proteins. The major physiological substrate of this protease is D1 protein that is one of the main subunit of photosystem II. Knockout mutants of this protease displays variegated phenotype in Arabidopsis, thus physiological function of this protease is maintenance of chloroplast proteins. Previously, we constructed over-expression system of FtsH protease using E.coli-pET vector system. This system produced recombinant protein as inclusion body, however these were possible to be activated by urea mediated refolding. The refolded proteases showed only ATPase activity. Protease activity has not been detected, though we tried almost all of the conditions which have been reported. In this study, we calculated affinity between FtsH protease and D1 protein by means of molecular dynamics simulation, and analyzed unfoldase activity using bovine serum albumin as a substrate.
