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The isolated proteolytic domain of Escherichia coli ATP‐dependent protease Lon exhibits the peptidase activity
Author(s) -
Rasulova Fatima S,
Dergousova Natalia I,
Starkova Natalie N,
Melnikov Edward E,
Rumsh Lev D,
Ginodman Lev M,
Rotanova Tatyana V
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00859-x
Subject(s) - protease , proteases , biochemistry , melittin , proteolytic enzymes , escherichia coli , proteolysis , atp hydrolysis , biology , chemistry , atpase , microbiology and biotechnology , peptide , enzyme , gene
Selective protein degradation is an energy‐dependent process performed by high‐molecular‐weight proteases. The activity of proteolytic components of these enzymes is coupled to the ATPase activity of their regulatory subunits or domains. Here, we obtained the proteolytic domain of Escherichia coli protease Lon by cloning the corresponding fragment of the lon gene in pGEX‐KG, expression of the hybrid protein, and isolation of the proteolytic domain after hydrolysis of the hybrid protein with thrombin. The isolated proteolytic domain exhibited almost no activity toward protein substrates (casein) but hydrolyzed peptide substrates (melittin), thereby confirming the importance of the ATPase component for protein hydrolysis. Protease Lon and its proteolytic domain differed in the efficiency and specificity of melittin hydrolysis.