[Isolation and characterization of fragments of ATP-dependent protease Lon from Escherichia coli obtained by limited proteolysis].
Conditions of limited proteolysis of the protease Lon from Escherichia coli that provided the formation of fragments approximately corresponding to the enzyme domains were found for studying the domain functioning. A method of isolation of the domains was developed, and their functional characteristics were compared. The isolated proteolytic domain (LonP fragment) of the enzyme was shown to exhibit both peptidase and proteolytic activities; however, it cleaved large protein substrates at a significantly lower rate than the full-size protease Lon. On the other hand, the LonAP fragment, containing both the ATPase and the proteolytic domains, retained almost all of the enzymatic properties of the full-size protein. Both LonP and LonAP predominantly form dimers unlike the native protease Lon functioning as a tetramer. These results suggest that the N-terminal domain of protease Lon plays a considerable role in the process of the enzyme oligomerization.
Vasil'eva
O V
OV
Martynova
N Iu
NIu
Potapenko
N A
NA
Ovchinnikova
T V
TV
D000255:Adenosine Triphosphate / Q000737:chemistry*; D002364:Caseins / Q000737:chemistry; D019281:Dimerization; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics; D006868:Hydrolysis; D009154:Mutation; D010446:Peptide Fragments / Q000737:chemistry* / Q000302:isolation & purification; D049070:Protease La / Q000737:chemistry* / Q000235:genetics; D017434:Protein Structure, Tertiary
D002364:Caseins; D029968:Escherichia coli Proteins; D010446:Peptide Fragments; D000255:Adenosine Triphosphate; C483567:Lon protein, E coli; D049070:Protease La