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

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.     

Regulation of membrane functions and fatty acid composition in Escherichia coli by cyclic AMP receptor protein.

Adenosine 3′,5′-cyclic monophosphate (cAMP) has been shown to be involved in regulating a number of membrane functions in Escherichia coli cells, including various respiratory and transport activities. In this report we show that this regulation is mediated by the cAMP receptor protein (CRP). In addition, data are presented which show that the cAMP-CRP system is involved in regulating the E. coli fatty acid composition.     

Control by cAMP-CRP complex of the expression of the PTS-dependent Erwinia chrysanthemi clb genes in Escherichia coli

Abstract Influence of the crp, cya and ptsIH gene products on the functioning and/or regulation of the Erwinia chrysanthemi clb genes was studied in Escherichia coli . Transport of cellobiose was found to be mediated by the phosphotransferase system and the expression of the clb genes to be positively controlled by the cAMP-CRP complex. We postulate that the same situation may occur in E. chrysanthemi .     

Regulation of a macrolide resistance-beta-galactosidase (ermC-lacZ) gene fusion in Escherichia coli.

A fusion constructed between the putative attenuator plus the first 219 nucleotides of the ermC (erythromycin resistance) structural gene and a 5' terminally deleted lacZ gene produced a moderate, basal level of beta-galactosidase which was increased by erythromycin addition. Another construction containing an intact ermC gene in addition to the fusion produced lower levels of beta-galactosidase, suggesting that the ermC gene product exerts negative feedback control on expression.