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The regulation of Enzyme IIA^Glc expression controls adenylate cyclase activity in Escherichia coli

Unité de Génétique des Génomes Bactériens, Institut Pasteur, 28 rue du Docteur Roux, 75724 Paris Cedex 15, France¹

Author for correspondence: Evelyne Krin. Tel: +33 01 40 61 35 56. Fax: +33 01 45 68 89 48. e-mail: ekrin{at}pasteur.fr

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 IIA^Glc of the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS), from its specific P2 promoter. This leads to a twofold reduction in the global amount of Enzyme IIA^Glc, the adenylate cyclase activator, responsible for the decrease in adenylate cyclase activity observed in the hns crp strain.

Keywords: catabolite repression, cya, regulatory network

Abbreviations: CAP, catabolite activator protein; H-NS, histone-like nucleoid-structuring; PTS, phosphoenolpyruvate:carbohydrate phosphotransferase system

^a Present address: Genopole, Institut Pasteur, 28 rue du Docteur Roux, 75724 Paris Cedex 15, France.

^b Present address: Laboratory of Microbiology, Radioactive Waste & Clean-up Division, SCK/CEN, Boeretang 200, 2400 Mol, Belgium.

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