Induction of protease La under stress and its effect on intracellular proteolysis in Escherichia coli.
Induction of protease La was found to increase to higher extent in E. coli that had been treated with canavanine for longer period. However, hydrolysis of canavanine-containing proteins occurred rapidly but at nearly an identical rate regardless of the period of canavanine-treatment. Exposure of E. coli to heat also raised the level of protease La but showed little effect on overall rate of proteolysis. These results suggest that induction of protease La under stress occurs as a part of heat shock response but not necessarily for elimination of denatured or abnormal proteins.
Lee
C S
CS
Department of Molecular Biology and SRC for Cell Differentiation, College of Natural Sciences, Seoul National University, Korea.
Park
W J
WJ
Jung
E M
EM
Choi
K H
KH
Ha
D B
DB
Chung
C H
CH
D049069:ATP-Dependent Proteases; D001426:Bacterial Proteins / Q000378:metabolism*; D002172:Canavanine / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004790:Enzyme Induction; D004926:Escherichia coli / Q000201:enzymology*; D006360:Heat-Shock Proteins; D006868:Hydrolysis; D007700:Kinetics; D012697:Serine Endopeptidases / Q000378:metabolism*; D013696:Temperature
D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; D002172:Canavanine; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases