[Proteolysis coupled with ATP. Regulation of activity of proteolytic centers of Escherichia coli lon protease].
Regulation of activity of the proteolytic sites of Lon protease was studied. It was found that ATP-Mg has the properties of a noncompetitive activator of peptidase sites. The processive mechanism of the hydrolysis of protein substrates by Lon protease was experimentally confirmed under the conditions of ATP hydrolysis. It was shown that the oligomeric state of the enzyme is the necessary prerequisite for the processive proteolysis by the native Lon protease. The study of the properties of the mixed mutant Lon-K362Q/S679A confirmed the existence of the intra- and intersubunit pathways of signal transduction from the ATPase to proteolytic sites. The mutual influence of substrates of Lon protease was studied, and the existence of cooperative interactions between the peptidase sites in the oligomeric enzyme was suggested.
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, GSP Moscow, 117997 Russia.
K B
KB
Tsirul'nikov
E E
EE
Mel'nikov
T V
TV
Rotanova
D049069:ATP-Dependent Proteases; D000255:Adenosine Triphosphate / Q000378:metabolism*; D001665:Binding Sites; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006868:Hydrolysis; D009154:Mutation; D049070:Protease La; D012697:Serine Endopeptidases / Q000235:genetics / Q000378:metabolism*
D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D000255:Adenosine Triphosphate; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; C483567:Lon protein, E coli; D049070:Protease La