Two different mechanisms for urea action at the LAC and TNA operons in Escherichia coli.
Urea, at concentrations which do not interfere with bacterial growth, specifically inhibits the expression of catabolite sensitive operons. To search for the target and the mechanism of urea action we measured lactose (lac) and tryptophanase (tna) specific mRNA synthesis in vivo and in vitro. We show that urea acts by two different mechanisms at these two catabolite sensitive operons, resembling the manner in which catabolite repression regulates lac and tna. At the lac promoter, urea abolishes transcription initiation or blocks an early step in mRNA elongation without interfering with the binding of RNA polymerase and catabolite gene activator protein (CAP). At the tna promoter, urea does not abolish transcription initiation but could interfere with tnaC translation.
Blazy
B
B
Unité de Biochimie des Régulations Cellulaires, Institut Pasteur, Paris, France.
Ullmann
A
A
D002373:Cyclic AMP Receptor Protein / Q000378:metabolism; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism; D004926:Escherichia coli / Q000187:drug effects / Q000235:genetics*; D007763:Lac Operon; D008190:Lyases / Q000235:genetics*; D009876:Operon; D011401:Promoter Regions, Genetic; D012333:RNA, Messenger / Q000378:metabolism; D014158:Transcription, Genetic / Q000187:drug effects*; D014368:Tryptophanase / Q000235:genetics*; D014508:Urea / Q000494:pharmacology*
D002373:Cyclic AMP Receptor Protein; D012333:RNA, Messenger; D014508:Urea; D012321:DNA-Directed RNA Polymerases; D008190:Lyases; D014368:Tryptophanase