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PMID:9720920
| Citation |
Rasulova, FS, Dergousova, NI, Starkova, NN, Melnikov, EE, Rumsh, LD, Ginodman, LM and Rotanova, TV (1998) The isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activity. FEBS Lett. 432:179-81 |
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| Abstract |
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. |
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| Keywords |
ATP-Dependent Proteases; Amino Acid Sequence; Catalysis; Endopeptidases/metabolism; Escherichia coli/chemistry; Escherichia coli/enzymology; Escherichia coli Proteins; Heat-Shock Proteins/chemistry; Heat-Shock Proteins/isolation & purification; Heat-Shock Proteins/metabolism; Hydrolysis; Melitten/metabolism; Molecular Sequence Data; Protease La; Protein Structure, Tertiary; Serine Endopeptidases/chemistry; Serine Endopeptidases/isolation & purification; Serine Endopeptidases/metabolism |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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