Multidomain ATP-dependent Lon protease of E. coli (Ec-Lon) is
one of the key enzymes of the quality control system of the cellular proteome.
A recombinant form of Ec-Lon with deletion of the inserted characteristic
α-helical HI(CC) domain (Lon-dHI(CC)) has been prepared and investigated
to understand the role of this domain. A comparative study of the ATPase,
proteolytic, and peptidase activities of the intact Lon protease and
Lon-dHI(CC) has been carried out. The ability of the enzymes to undergo
autolysis and their ability to bind DNA have been studied as well. It has been
shown that the HI(CC) domain of Ec-Lon protease is required for the formation
of a functionally active enzyme structure and for the implementation of
protein-protein interactions.
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