Mutational analysis of the enzyme IIIGlc of the phosphoenolpyruvate phosphotransferase system in Escherichia coli

Zeng, Guo-Qing; Reuse, Hilde De; Danchin, Antoine

doi:10.1016/0923-2508(92)90017-i

Cited by 15 publications

(16 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…2) was sufficient to explain the decrease in adenylate cyclase activity, we determined this activity in the double mutant BE1420 containing plasmid pDIA4705 carrying the crr gene. The presence of this plasmid in a ∆crr strain has been shown to restore the wild-type cAMP level and glucose transport (Zeng et al, 1992). The activity measured in the crp hns mutant containing plasmid pDIA4705, 11 400 pmol cAMP (mg protein) −" min −" , was similar to that obtained in the TP2139 crp strain [12 600 pmol cAMP (mg protein) −" min −" ].…”

Section: Figsupporting

confidence: 49%

“…When required, kanamycin and ampicillin were added at 25 and 100 µg ml − ", respectively. Plasmid pDIA3350 was constructed by insertion of the SalI-BamHI fragment of This study pDIA4705 pBR322 derivative carrying crr under anti-Tc r promoter Zeng et al (1992) pDIA3238, corresponding to the full phosphoenolpyruvate : carbohydrate phosphotransferase system (PTS) operon with promoters P0, P1 and P2, into plasmid pDIA3240 (De Reuse et al, 1986). All experiments were performed in accordance with the European regulation requirements concerning the contained use of Genetically Modified Organisms of Group I (agreement no.…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

The regulation of Enzyme IIAGlc expression controls adenylate cyclase activity in Escherichia coli

et al. 2002

View full text Add to dashboard Cite

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.

show abstract

Section: Figsupporting

confidence: 49%

Section: Methodsmentioning

confidence: 99%

The regulation of Enzyme IIAGlc expression controls adenylate cyclase activity in Escherichia coli

et al. 2002

View full text Add to dashboard Cite

show abstract

“…Other observations support this interpretation. When galactosides are present at saturating amounts, 125 I-labeled unphosphorylated EIIA Glc binds in a 1:6 stoichiometry to wild-type LacY (822,987). Some of these residues are also important for the interaction of EIIA Glc with HPr, EIIB Glc , and GlpK (Table 2).…”

Section: Inhibits Transcription Induction Mechanismmentioning

confidence: 99%

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,188

769

View full text Add to dashboard Cite

SUMMARY The phosphoenolpyruvate(PEP):carbohydrate phosphotransferase system (PTS) is found only in bacteria, where it catalyzes the transport and phosphorylation of numerous monosaccharides, disaccharides, amino sugars, polyols, and other sugar derivatives. To carry out its catalytic function in sugar transport and phosphorylation, the PTS uses PEP as an energy source and phosphoryl donor. The phosphoryl group of PEP is usually transferred via four distinct proteins (domains) to the transported sugar bound to the respective membrane component(s) (EIIC and EIID) of the PTS. The organization of the PTS as a four-step phosphoryl transfer system, in which all P derivatives exhibit similar energy (phosphorylation occurs at histidyl or cysteyl residues), is surprising, as a single protein (or domain) coupling energy transfer and sugar phosphorylation would be sufficient for PTS function. A possible explanation for the complexity of the PTS was provided by the discovery that the PTS also carries out numerous regulatory functions. Depending on their phosphorylation state, the four proteins (domains) forming the PTS phosphorylation cascade (EI, HPr, EIIA, and EIIB) can phosphorylate or interact with numerous non-PTS proteins and thereby regulate their activity. In addition, in certain bacteria, one of the PTS components (HPr) is phosphorylated by ATP at a seryl residue, which increases the complexity of PTS-mediated regulation. In this review, we try to summarize the known protein phosphorylation-related regulatory functions of the PTS. As we shall see, the PTS regulation network not only controls carbohydrate uptake and metabolism but also interferes with the utilization of nitrogen and phosphorus and the virulence of certain pathogens.

show abstract

“…Conserved residues are in bold. In addition, residues 47 and 76 are shown in boldface; they are altered by crr mutations that abolish inducer exclusion (Zeng et al 1992;Postma et al 1994 In summary, our results demonstrate that a membrane-bound EII, containing a IIAGl°-like domain, can, like the soluble IIA GI°, interact with both soluble proteins like glycerol kinase, and membrane-bound complexes like the maltose transport system.…”

Section: Discussionmentioning

confidence: 89%

“…A more important clue may come from E. coil and S. typhimurium crr mutations that abolish inducer exclusion. These mutations are localized either in completely conserved positions (G47S, G47C, H75Q, and A76T; Presper et al 1989;Zeng et al 1992;Postma et al 1994) or in residues that are not conserved at all ($78F and E97 K; see Zeng et al 1989;Postma et al 1994). Replacement of Glu-97 by a positively charged lysine residue in IIA GI~ abolished inducer exclusion but not eMG phosphorylation and stimulation of adenylate cyclase (Postma et al 1994).…”

Section: Discussionmentioning

confidence: 99%

Regulation of glycerol and maltose uptake by the IIAGlc-like domain of IINag of the phosphotransferase system inSalmonella typhimurium LT2

Vlag

Postma

1995

Molec. Gen. Genet.

View full text Add to dashboard Cite

Mutational analysis of the enzyme IIIGlc of the phosphoenolpyruvate phosphotransferase system in Escherichia coli

Cited by 15 publications

References 27 publications

The regulation of Enzyme IIAGlc expression controls adenylate cyclase activity in Escherichia coli

The regulation of Enzyme IIAGlc expression controls adenylate cyclase activity in Escherichia coli

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Regulation of glycerol and maltose uptake by the IIAGlc-like domain of IINag of the phosphotransferase system inSalmonella typhimurium LT2

Contact Info

Product

Resources

About