Abstract
FtsH protease is an ATP-dependent protease localized on cytoplasmic membrane. This protease is a member of AAA superfamily. In higher plants, FtsH protease is localization on thylakoid membrane. Function of the FtsH protease was assumed to degrade membrane proteins incorporating as abnormal conformation. This protease also participate in the degradation of photo-damaged subunits of photosystem II.
In many cases, FtsH protease expressed in E.coli is deposited as inclusion bodies. Structure of FtsH protease contains an obvious transmembrane hydrophobic region. The region is responsible for the formation of inclusion bodies. In this study, therefore, it was eliminated from FtsH protease. For the results, though the formation of inclusion bodies was not improved, the expressed proteins were functionally refolded by the treatment of dialysis against the buffers containing the reduced reagents. The refolded FtsH protease has been applied to biochemical characterization.
