[A test system based on the lux-regulon from Vibrio fischeri for studying the functional activity of mutant forms of Escherichia coli lon-proteinase].
The possibility of application of the bioluminescence method (Lux-test) for studying in vivo functional activity of Escherichia coli protease Lon and its mutants was demonstrated. This assay is based on the capacity of protease Lon and its mutant forms for specific degradation of the LuxR protein, a positive transcriptional activator of the right operon luxICDABE from the marine bacterium Vibrio fischeri, and thus to affect the level of AB luciferase in the cells. A correlation between in vitro activity of the protease Lon mutants and the intensity of bioluminescence measured by the Lux-test was revealed.
Manukhov
I V
IV
GNIIgenetika State Research Center, Moscow, Russia.
Eroshnikov
G E
GE
Zavil'gel'skiĭ
G B
GB
Ginodman
L M
LM
Mel'nikov
E E
EE
Rotanova
T V
TV
Starkova
N N
NN
Tsirul'nikov
K B
KB
D049069:ATP-Dependent Proteases; D001426:Bacterial Proteins / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D008156:Luciferases / Q000235:genetics; D008163:Luminescent Measurements; D009154:Mutation; D009876:Operon; D049070:Protease La; D018085:Regulon; D012097:Repressor Proteins / Q000235:genetics*; D012697:Serine Endopeptidases / Q000235:genetics / Q000378:metabolism*; D015534:Trans-Activators / Q000235:genetics*; D014733:Vibrio / Q000235:genetics*
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D012097:Repressor Proteins; D015534:Trans-Activators; C064778:LuxR autoinducer binding proteins; D008156:Luciferases; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; C483567:Lon protein, E coli; D049070:Protease La