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. 1972 Oct;69(10):2922–2926. doi: 10.1073/pnas.69.10.2922

Adenosine 3′:5′-Cyclic Monophosphate Control of the Enzymes of Glutamine Metabolism in Escherichia coli

Stanley Prusiner 1, Richard E Miller 1, Raymond C Valentine 1
PMCID: PMC389675  PMID: 4404145

Abstract

The effect of cAMP on the intracellular levels of five enzymes concerned with the interconversion of glutamate and glutamine in E. coli has been examined. Cyclic AMP added to the culture medium increases the levels of glutamate dehydrogenase (EC 1.4.1.4) and glutamine synthetase (EC 6.3.1.2); it decreases the levels of glutamate synthase (EC 1.4.1.X), and glutaminase A (EC 3.5.1.2). Cyclic AMP did not affect the level of glutaminase B (EC 3.5.1.2). These alterations in enzyme levels by cAMP require cyclic AMP receptor protein, since the levels of these enzymes were unchanged by cAMP in a mutant lacking this receptor. Chloramphenicol also abolished the effects of cAMP, a result that implies protein synthesis is necessary for these changes in enzyme levels to occur. The reciprocal effects of cAMP on the levels of these enzymes may play an important role in the cellular regulation of nitrogen metabolism.

Keywords: glutaminase, glutamate synthase, glutamine synthetase, glutamate dehydrogenase, cyclic AMP

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Selected References

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

  1. Chader G. J. Hormonal effects on the neural retina: induction of glutamine synthetase by cyclic-3',5'-AMP. Biochem Biophys Res Commun. 1971 Jun 4;43(5):1102–1105. doi: 10.1016/0006-291x(71)90575-4. [DOI] [PubMed] [Google Scholar]
  2. De Crombrugghe B., Chen B., Anderson W., Nissley P., Gottesman M., Pastan I., Perlman R. Lac DNA, RNA polymerase and cyclic AMP receptor protein, cyclic AMP, lac repressor and inducer are the essential elements for controlled lac transcription. Nat New Biol. 1971 Jun 2;231(22):139–142. doi: 10.1038/newbio231139a0. [DOI] [PubMed] [Google Scholar]
  3. 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]
  4. Eron L., Block R. Mechanism of initiation and repression of in vitro transcription of the lac operon of Escherichia coli. Proc Natl Acad Sci U S A. 1971 Aug;68(8):1828–1832. doi: 10.1073/pnas.68.8.1828. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Greenblatt J., Schleif R. Arabinose C protein: regulation of the arabinose operon in vitro. Nat New Biol. 1971 Oct 6;233(40):166–170. doi: 10.1038/newbio233166a0. [DOI] [PubMed] [Google Scholar]
  6. JACOB F., MONOD J. Genetic regulatory mechanisms in the synthesis of proteins. J Mol Biol. 1961 Jun;3:318–356. doi: 10.1016/s0022-2836(61)80072-7. [DOI] [PubMed] [Google Scholar]
  7. Levitzki A. Determination of submicro quantities of ammonia. Anal Biochem. 1970 Feb;33(2):335–340. doi: 10.1016/0003-2697(70)90304-0. [DOI] [PubMed] [Google Scholar]
  8. MAKMAN R. S., SUTHERLAND E. W. ADENOSINE 3',5'-PHOSPHATE IN ESCHERICHIA COLI. J Biol Chem. 1965 Mar;240:1309–1314. [PubMed] [Google Scholar]
  9. Miller Z., Varmus H. E., Parks J. S., Perlman R. L., Pastan I. Regulation of gal messenger ribonucleic acid synthesis in Escherichia coli by 3',5'-cyclic adenosine monophosphate. J Biol Chem. 1971 May 10;246(9):2898–2903. [PubMed] [Google Scholar]
  10. Nisseley S. P., Anderson W. B., Gottesman M. E., Perlman R. L., Pastan I. In vitro transcription of the gal operon requires cyclic adenosine monophosphate and cyclic adenosine monophosphate receptor protein. J Biol Chem. 1971 Aug 10;246(15):4671–4678. [PubMed] [Google Scholar]
  11. 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]
  12. Perlman R. L., De Crombrugghe B., Pastan I. Cyclic AMP regulates catabolite and transient repression in E. coli. Nature. 1969 Aug 23;223(5208):810–812. doi: 10.1038/223810a0. [DOI] [PubMed] [Google Scholar]
  13. 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]
  14. Peterkofsky A., Gazdar C. Glucose and the metabolism of adenosine 3':5'-cyclic monophosphate in Escherichia coli. Proc Natl Acad Sci U S A. 1971 Nov;68(11):2794–2798. doi: 10.1073/pnas.68.11.2794. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Prusiner S., Milner L. A rapid radioactive assay for glutamine synthetase, glutaminase, asparagine synthetase, and asparaginase. Anal Biochem. 1970 Oct;37(2):429–438. doi: 10.1016/0003-2697(70)90069-2. [DOI] [PubMed] [Google Scholar]
  16. Prusiner S., Stadtman E. R. On the regulation of glutaminase in E. coli: metabolite control. Biochem Biophys Res Commun. 1971 Dec 17;45(6):1474–1481. doi: 10.1016/0006-291x(71)90186-0. [DOI] [PubMed] [Google Scholar]
  17. Rudack D., Davie B., Holten D. Regulation of rat liver glucose 6- phosphate dehydrogenase levels by adenosine 3', 5' -monophosphate. J Biol Chem. 1971 Dec 25;246(24):7823–7824. [PubMed] [Google Scholar]
  18. Soderling T. R., Hickenbottom J. P., Reimann E. M., Hunkeler F. L., Walsh D. A., Krebs E. G. Inactivation of glycogen synthetase and activation of phosphorylase kinase by muscle adenosine 3',5'-monophosphate-dependent protein kinases. J Biol Chem. 1970 Dec 10;245(23):6317–6328. [PubMed] [Google Scholar]
  19. Stadtman E. R., Ginsburg A., Ciardi J. E., Yeh J., Hennig S. B., Shapiro B. M. Multiple molecular forms of glutamine synthetase produced by enzyme catalyzed adenylation and deadenylylation reactions. Adv Enzyme Regul. 1970;8:99–118. doi: 10.1016/0065-2571(70)90011-7. [DOI] [PubMed] [Google Scholar]
  20. Stadtman E. R., Shapiro B. M., Ginsburg A., Kingdon H. S., Denton M. D. Regulation of glutamine synthetase activity in Escherichia coli. Brookhaven Symp Biol. 1968 Jun;21(2):378–396. [PubMed] [Google Scholar]
  21. Tempest D. W., Meers J. L., Brown C. M. Synthesis of glutamate in Aerobacter aerogenes by a hitherto unknown route. Biochem J. 1970 Apr;117(2):405–407. doi: 10.1042/bj1170405. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Ullmann A., Monod J. Cyclic AMP as an antagonist of catabolite repression in Escherichia coli. FEBS Lett. 1968 Nov;2(1):57–60. doi: 10.1016/0014-5793(68)80100-0. [DOI] [PubMed] [Google Scholar]
  23. Ureta T., Radojković J., Niemeyer H. Inhibition by catecholamines of the induction of rat liver glucokinase. J Biol Chem. 1970 Sep 25;245(18):4819–4824. [PubMed] [Google Scholar]
  24. Varricchio F. Control of glutamate dehydrogenase synthesis in Escherichia coli. Biochim Biophys Acta. 1969 May 6;177(3):560–564. doi: 10.1016/0304-4165(69)90319-5. [DOI] [PubMed] [Google Scholar]
  25. Varricchio F. Control of glutaminase synthesis in Escherichia coli. Arch Mikrobiol. 1972;81(3):234–238. doi: 10.1007/BF00412241. [DOI] [PubMed] [Google Scholar]
  26. Zubay G., Gielow L., Englesberg E. Cell-free studies on the regulation of the arabinose operon. Nat New Biol. 1971 Oct 6;233(40):164–165. doi: 10.1038/newbio233164a0. [DOI] [PubMed] [Google Scholar]

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