Exogenous induction of the Escherichia coli hexose phosphate transport system defined by uhp-lac operon fusions.

The uhp-coded hexose phosphate transport system of Escherichia coli is normally induced by the presence of extracellular glucose-6-phosphate (G6P), whereas internally generated G6P does not provide a regulatory signal. Strains carrying uhp-lac operon fusions in which lac operon expression is under the control of the uhpT promoter were isolated. The direction of transcription of the uhp T gene was found to be counterclockwise on the E. coli chromosome map. The effects of added sugar phosphates on induction of beta-galactosidase and G6P uptake activities were compared in two fusion-carrying strains differing only in the presence of functional Uhp+ activity. Induction of uhp expression by G6P was equally effective in the two strains; accumulation of G6P diminished its ability to serve as an inducer. Mannose-6-phosphate was an effective competitive inhibitor of G6P uptake, but did not inhibit induction by G6P of uhp expression. No sugar phosphates were found that inhibited induction by G6P. Inorganic phosphate competitively inhibited induction by G6P whether G6P transport activity was present or not. Thus, the transport activity is not involved in the regulation of its synthesis, and these results strongly support the view that the uhp regulatory system senses only the external environment.