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• W2005039766 abstract "We have investigated the interaction between BgIF and BgIG, two proteins that regulate expression of the E. coli bgI operon. BgIF is both a negative regulator of operon expression and a phosphotransferase involved in uptake of β-glucosides. BgIG is a positive regulator that functions as a transcriptional antiterminator. We show here that BgIF is phosphorylated by the soluble components of the phosphotransferase system: Enzyme I, HPr, and the phosphate donor phosphoenolpyruvate. Phosphorylated BgIF can then transfer phosphate either to β-glucosides or to wild-type BgIG. Mutant BgIG derivatives, which give constitutive expression of the bgI operon, show little or no phosphorylation by BgIF. Hence BgIF exerts its negative effect on operon expression by phosphorylating BgIG, blocking its action as an antiterminator. BgIG is dephosphorylated only in the presence of both BgIF and β-glucosides. Based on these results, we propose the following mechanism: In the absence of β-glucosides, BgIG is phosphorylated by BgIF and is inactive in antitermination. Addition of inducer stimulates BgIF to dephosphorylate BgIG, allowing BgIG to function as a positive regulator of operon expression. β-Glucosides are then phosphorylated and transported into the cell by BgIF." @default.
• W2005039766 created "2016-06-24" @default.
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• W2005039766 date "1989-09-01" @default.
• W2005039766 modified "2023-10-17" @default.
• W2005039766 title "Protein phosphorylation regulates transcription of the β-glucoside utilization operon in E. coli" @default.
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• W2005039766 doi "https://doi.org/10.1016/0092-8674(89)90937-9" @default.
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