The regulation of Enzyme IIAGlc expression controls adenylate cyclase activity in Escherichia coli
Krin, Evelyne and Sismeiro, Odile and Danchin, Antoine and Bertin, Philippe N,, 148, 1553-1559 (2002),
doi = https://doi.org/10.1099/00221287-148-5-1553,
publicationName = Microbiology Society,
issn = 1350-0872,
abstract= During the last few years, several genes, such as pap, bgl and flhDC, have been shown to be coregulated by the histone-like nucleoid-structuring (H-NS) protein and the cyclic AMP-catabolite activator protein (cAMP/CAP) complex, suggesting an interaction between both systems in the control of some cellular functions. In this study, the possible effect of H-NS on the cAMP level was investigated. In a CAP-deficient strain, the presence of an hns mutation results in a strong reduction in the amount of cAMP, due to a decrease in adenylate cyclase activity. This is caused by the reduced expression of crr, which encodes the Enzyme IIAGlc of the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS), from its specific P2 promoter. This leads to a twofold reduction in the global amount of Enzyme IIAGlc, the adenylate cyclase activator, responsible for the decrease in adenylate cyclase activity observed in the hns crp strain.,
language=,
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