[Lon-protease participates in the regulation of transcription of the Lux-operon of Vibrio fischeri].
Lon protease of Escherichia coli specifically inhibits the activity of the regulatory protein LuxI responsible for synthesis of the autoinducer N-(3-oxo-hexanoyl)homoserine lactone. As a result, transcription of the right lux operon is initiated in lon+ bacteria much later than in lon- mutants. Lon protease does not affect the activity of LuxAB proteins (luciferase) and LuxC, LuxD, and LuxE proteins involved in synthesis of an aldehyde substrate for luciferase.
Zavil'gel'skiĭ
G B
GB
Manukhov
I V
IV
D049069:ATP-Dependent Proteases; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins / Q000235:genetics*; D009876:Operon; D049070:Protease La; D012697:Serine Endopeptidases / Q000235:genetics*; D014157:Transcription Factors / Q000235:genetics* / Q000378:metabolism; D014158:Transcription, Genetic; D014733:Vibrio / Q000235:genetics*
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; C085427:LuxI protein, Bacteria; D014157:Transcription Factors; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; C483567:Lon protein, E coli; D049070:Protease La
Lon-proteaza uchastvuet v reguliatsii transkriptsii Lux-operona Vibrio fischeri.