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. 1975 Jun;72(6):2300–2304. doi: 10.1073/pnas.72.6.2300

Adenosine 3':5'-cyclic monophosphate as mediator of catabolite repression in Escherichia coli.

W Epstein, L B Rothman-Denes, J Hesse
PMCID: PMC432745  PMID: 166384

Abstract

Measurements of intracellular adenosine 3':5'-cyclic monophosphate (cAMP) concentrations in E. coli under a variety of conditions show that levels of this nucleotide are well correlated with the rate of synthesis of beta-galactosidase (beta-D-galactoside galactohydrolase, EC 3.2.1.23) in both catabolite repression and transient repression. These results, combined with extensive genetic and in vitro studies from a number of laboratories on the role of cAMP in E. coli, provide strong support for the concept that intracellular cAMP levels mediate the effects of catabolite and transient repression on rates on enzyme synthesis. Under all conditions studied, excretion can be described by a single rate constant, 2.1 min-1 at 37 degrees, indicating that intracellular levels cannot be regulated by alterations in the rate of cAMP excretion. Our data are fully consistent with the idea that carbon sources control intracellular cAMP levels by effects on its synthesis.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Brickman E., Soll L., Beckwith J. Genetic characterization of mutations which affect catabolite-sensitive operons in Escherichia coli, including deletions of the gene for adenyl cyclase. J Bacteriol. 1973 Nov;116(2):582–587. doi: 10.1128/jb.116.2.582-587.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Buettner M. J., Spitz E., Rickenberg H. V. Cyclic adenosine 3',5'-monophosphate in Escherichia coli. J Bacteriol. 1973 Jun;114(3):1068–1073. doi: 10.1128/jb.114.3.1068-1073.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Chamberlin M. J. The selectivity of transcription. Annu Rev Biochem. 1974;43(0):721–775. doi: 10.1146/annurev.bi.43.070174.003445. [DOI] [PubMed] [Google Scholar]
  4. Emmer M., deCrombrugghe B., Pastan I., Perlman R. Cyclic AMP receptor protein of E. coli: its role in the synthesis of inducible enzymes. Proc Natl Acad Sci U S A. 1970 Jun;66(2):480–487. doi: 10.1073/pnas.66.2.480. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Epstein W., Jewett S., Fox C. F. Isolation and mapping of phosphotransferase mutants in Escherichia coli. J Bacteriol. 1970 Nov;104(2):793–797. doi: 10.1128/jb.104.2.793-797.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Epstein W., Kim B. S. Potassium transport loci in Escherichia coli K-12. J Bacteriol. 1971 Nov;108(2):639–644. doi: 10.1128/jb.108.2.639-644.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Fairbanks G., Steck T. L., Wallach D. F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971 Jun 22;10(13):2606–2617. doi: 10.1021/bi00789a030. [DOI] [PubMed] [Google Scholar]
  8. Moses V., Prevost C. Catabolite repression of beta-galactosidase synthesis in Escherichia coli. Biochem J. 1966 Aug;100(2):336–353. doi: 10.1042/bj1000336. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Pastan I., Perlman R. Cyclic adenosine monophosphate in bacteria. Science. 1970 Jul 24;169(3943):339–344. doi: 10.1126/science.169.3943.339. [DOI] [PubMed] [Google Scholar]
  10. Perlman R. L., Pastan I. Pleiotropic deficiency of carbohydrate utilization in an adenyl cyclase deficient mutant of Escherichia coli. Biochem Biophys Res Commun. 1969 Sep 24;37(1):151–157. doi: 10.1016/0006-291x(69)90893-6. [DOI] [PubMed] [Google Scholar]
  11. Peterkofsky A., Gazdar C. Glucose inhibition of adenylate cyclase in intact cells of Escherichia coli B. Proc Natl Acad Sci U S A. 1974 Jun;71(6):2324–2328. doi: 10.1073/pnas.71.6.2324. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Rothman-Denes L. B., Hesse J. E., Epstein W. Role of cyclic adenosine 3',5'-monophosphate in the in vivo expression of the galactose operon of Escherichia coli. J Bacteriol. 1973 Jun;114(3):1040–1044. doi: 10.1128/jb.114.3.1040-1044.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Rubin C. S., Erlichman J., Rosen O. M. Cyclic adenosine 3',5'-monophosphate-dependent protein kinase of human erythrocyte membranes. J Biol Chem. 1972 Oct 10;247(19):6135–6139. [PubMed] [Google Scholar]
  14. Taylor A. L., Trotter C. D. Linkage map of Escherichia coli strain K-12. Bacteriol Rev. 1972 Dec;36(4):504–524. doi: 10.1128/br.36.4.504-524.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Ullmann A. Are cyclic AMP effects related to real physiological phenomena? Biochem Biophys Res Commun. 1974 Mar 25;57(2):348–352. doi: 10.1016/0006-291x(74)90936-x. [DOI] [PubMed] [Google Scholar]
  16. Wayne P. K., Rosen O. M. Cyclic 3':5'-adenosine monophosphate in Escherichia coli during transient and catabolite repression. Proc Natl Acad Sci U S A. 1974 Apr;71(4):1436–1440. doi: 10.1073/pnas.71.4.1436. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Zubay G., Schwartz D., Beckwith J. Mechanism of activation of catabolite-sensitive genes: a positive control system. Proc Natl Acad Sci U S A. 1970 May;66(1):104–110. doi: 10.1073/pnas.66.1.104. [DOI] [PMC free article] [PubMed] [Google Scholar]

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