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. 1993 Jan;175(1):74–79. doi: 10.1128/jb.175.1.74-79.1993

Effect of glpT and glpD mutations on expression of the phoA gene in Escherichia coli.

N N Rao 1, M F Roberts 1, A Torriani 1, J Yashphe 1
PMCID: PMC196098  PMID: 8416912

Abstract

In vivo 31P nuclear magnetic resonance analysis of Escherichia coli cells showed that the intracellular concentration of P(i) remained constant in wild-type and in a glpT mutant strain whether the cells were grown on excess (2 mM) P(i) or sn-glycerol-3-phosphate as a phosphate source. The function of the phoA promoter (measured by beta-galactosidase activity in a phoA-lacZ fusion strain) was repressed when glpT+ cells were utilizing sn-glycerol-3-phosphate as the sole source of phosphate. These cells were devoid of alkaline phosphatase activity. However, the phoA promoter was fully active in a glpT mutant. These results indicated that the repression of the enzyme synthesis was not due to a variation in the level of cytoplasmic P(i) but was due to the P(i) excreted into the periplasm and/or to the medium.

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Selected References

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