The cyclic 3′,5′-adenosine monophosphate receptor protein and regulation of cyclic 3′,5′-adenosine monophosphate synthesis in Escherichia coli

Botsford, James L.; Drexler, Mark

doi:10.1007/bf00270375

Cited by 68 publications

(52 citation statements)

References 38 publications

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“…Inactivation of crp also affects the cAMP concentration by leading to a drastic increase in the rate of cAMP synthesis (75,170,241,363,679). The increase in the cAMP concentration depends on an intact crr gene.…”

Section: Glcmentioning

confidence: 99%

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

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,187

769

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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.

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Section: Glcmentioning

confidence: 99%

“…In a later study, the presence of other metabolizable sugars was shown to elicit the same effect (758). Interestingly, crp mutants excrete much higher amounts of cAMP than wild-type cells (75,241,679). A putative lowaffinity cAMP exporter (K m of approximately 10 mM) was identified (275).…”

Section: Glcmentioning

confidence: 99%

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

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,187

769

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“…2). Note the presence of 31,000-and 18,000-molecular-weight binding proteins in lane 3 Further protein characterization of mature and immature inclusions revealed that inclusions grown in the absence of cAMP resemble purified EB possessing eucaryotic cellbinding proteins (31), while inclusions grown in the presence of cAMP closely resemble noninfectious RB (Fig. 6).…”

Section: Methodsmentioning

confidence: 96%

Cyclic AMP inhibits developmental regulation of Chlamydia trachomatis

Kaul¹,

Wenman²

1986

J Bacteriol

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The effect of cyclic AMP (cAMP) on the chlamydial growth cycle was studied with Chiamydia trachomatisinfected HeLa cells. At concentrations of 1 mM, cAMP had a profound effect on the chlamydial developmental cycle, resulting in small, immature inclusions. Immunoblot analysis revealed the absence of elementary body (EB)-specific antigens in the cAMP-treated cells. This effect was observed only if cAMP was added within the first 12 h of incubation and continued thereafter. Its withdrawal at any time from the medium led to the reappearance of fully mature, infectious organisms. Analogs or breakdown products of cAMP exerted no inhibitory effect on chlamydial development. Intracellular inclusions from the cAMP-treated cells were unable to infect fresh HeLa monolayers, in contrast to the completely infectious nontreated inclusions. Protein profiles of the cAMP-treated organisms (at any time point) resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresis very closely resembled reticulate bodies (RB) and did not possess characteristic EB-binding proteins. Collectively, these observations suggest an inhibitory role for cAMP at the RB stage of intracellular development. We also identified a cAMP receptor protein which is associated with RB and not with EB, further supporting a role for this system in the developmental regulation of chlamydiae.Chlamydiae are obligate intracellular parasites of eucaryotic cells which have been implicated in a wide spectrum of human diseases (24). The developmental cycle of Chlamydia trachomatis proceeds by attachment to host cells, uptake, and enlargement of the infectious elementary bodies (EB) to form noninfectious, metabolically active reticulate bodies (RB). These RB divide within cytoplasmic inclusions by binary fission and then condense and subsequently rupture to release EB capable of infecting fresh host cells (16,17).The responsiveness of cells to a wide range of stimuli depends upon internal signalling systems such as cyclic AMP (cAMP) or cyclic GMP (cGMP) which regulate cellular activity. cAMP plays an important and multitudinous role in the regulation of both procaryotes and eucaryotes (6,21). In procaryotes, cAMP mainly acts through a cAMP receptor protein (CRP) which is capable of binding two molecules of cAMP (2). Ward and Salari (30) postulated a bidirectional cyclic nucleotide control of chlamydial infections with low levels of cGMP acting as a stimulator and high levels of cAMP acting as an inhibitor. Prostaglandins El and E2 and other compounds known to alter cyclic nucleotide levels in the cell also affect the susceptibility of cells to chlamydial infections. The possible mechanisms of cAMP-mediated inhibition of chlamydial infection include: (i) inhibition of binding and uptake of chlamydiae by HeLa cells, (ii) interference with EB growth subsequent to uptake, or (iii) developmental inhibition at the RB stage.To elucidate this mechanism, we added cAMP to the infectious system at different intervals after inoculation of HeLa cells with purified EB. cAMP was ...

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“…Eflect of carbon source Cellular levels of CAMP are known to fluctuate as a function of the nature of the carbon source on which the strain is grown (Botsford & Drexler, 1978;Epstein et al, 1975). But Joseph et al (1982) showed that when bacteria were grown on a variety of carbon sources, adenylate cyclase activity was inversely related to the intracellular concentration of CAMP.…”

Section: ) As Can Be Seen Inmentioning

confidence: 99%

“…It has also been shown that crp strains overproduce cAMP (Potter et al, 1974;Wayne & Rosen, 1974). This led Botsford & Drexler (1978) to postulate that CAP in its active conformation (i.e. bound to CAMP) might act as a repressor of the adenylate cyclase gene, cya.…”

Section: Introductionmentioning

confidence: 99%

Aspects of the Regulation of Adenylate Cyclase Synthesis in Escherichia coli K12

Roy

Glaser²,

Danchin³

1988

Microbiology

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In Escherichia cofi K 12 expression of the adenylate cyclase gene is subject to multiple controls. In order to gain understanding of the regulation of adenylate cyclase synthesis, operon and protein fusions were constructed by in vitro recombination either into bacteriophage A or low-copynumber plasmids, or directly on the chromosome at the cya locus. The fusions were used in physiological experiments as probes to study transcriptional and translational controls of cya expression. It was found that adenylate cyclase synthesis was insensitive to glucose effects. As already described by other workers, the CAP-CAMP complex had a moderate negative control on cya expression. In addition it was observed that concomitant with a severe slackening of growth rate, specific to the growth of cya strains in rich medium, cya expression was considerably enhanced. This increase of adenylate cyclase synthesis did not appear to be directly dependent on the presence of a functional cAMP receptor (CAP), and seemed to be controlled at the level of transcription. Finally, translation of the cya message was very weak when compared to cya transcription (the mRNA level was the same in protein and operon fusions).

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The cyclic 3′,5′-adenosine monophosphate receptor protein and regulation of cyclic 3′,5′-adenosine monophosphate synthesis in Escherichia coli

Cited by 68 publications

References 38 publications

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

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

Cyclic AMP inhibits developmental regulation of Chlamydia trachomatis

Aspects of the Regulation of Adenylate Cyclase Synthesis in Escherichia coli K12

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