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. 1980 Feb;141(2):770–778. doi: 10.1128/jb.141.2.770-778.1980

Metabolite gene regulation: imidazole and imidazole derivatives which circumvent cyclic adenosine 3',5'-monophosphate in induction of the Escherichia coli L-arabinose operon.

E L Kline, V A Bankaitis, C S Brown, D C Montefiori
PMCID: PMC293687  PMID: 6245056

Abstract

Imidazole, histidine, histamine, histidinol phosphate, urocanic acid, or imidazolepropionic acid were shown to induce the L-arabinose operon in the absence of cyclic adenosine 3',5'-monophosphate. Induction was quantitated by measuring the increased differential rate of synthesis of L-arabinose isomerase in Escherichia coli strains which carried a deletion of the adenyl cyclase gene. The crp gene product (cyclic adenosine 3',5'-monophosphate receptor protein) and the araC gene product (P2) were essential for induction of the L-arabinose operon by imidazole and its derivatives. These compounds were unable to circumvent the cyclic adenosine 3',5'-monophosphate in the induction of the lactose or the maltose operons. The L-arabinose regulon was catabolite repressed upon the addition of glucose to a strain carrying an adenyl cyclase deletion growing in the presence of L-arabinose with imidazole. These results demonstrated that several imidazole derivatives may be involved in metabolite gene regulation (23).

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Selected References

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

  1. Ames B. N., Mccann J., Yamasaki E. Methods for detecting carcinogens and mutagens with the Salmonella/mammalian-microsome mutagenicity test. Mutat Res. 1975 Dec;31(6):347–364. doi: 10.1016/0165-1161(75)90046-1. [DOI] [PubMed] [Google Scholar]
  2. BUTCHER R. W., SUTHERLAND E. W. Adenosine 3',5'-phosphate in biological materials. I. Purification and properties of cyclic 3',5'-nucleotide phosphodiesterase and use of this enzyme to characterize adenosine 3',5'-phosphate in human urine. J Biol Chem. 1962 Apr;237:1244–1250. [PubMed] [Google Scholar]
  3. Bachmann B. J., Low K. B., Taylor A. L. Recalibrated linkage map of Escherichia coli K-12. Bacteriol Rev. 1976 Mar;40(1):116–167. doi: 10.1128/br.40.1.116-167.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Boos W. Structurally defective galactose-binding protein isolated from a mutant negative in the -methylgalactoside transport system of Escherichia coli. J Biol Chem. 1972 Sep 10;247(17):5414–5424. [PubMed] [Google Scholar]
  5. Brown C. S., West R., Hilderman R. H., Bayliss F. T., Klines E. L. A new locus (leuK) affecting the regulation of branched-chain amino acid, histidine, and tryptophan biosynthetic enzymes. J Bacteriol. 1978 Aug;135(2):542–550. doi: 10.1128/jb.135.2.542-550.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. 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]
  7. CRIBBS R., ENGLESBERG E. L-ARABINOSE NEGATIVE MUTANTS OF THE L-RIBULOKINASE STRUCTURAL GENE AFFECTING THE LEVELS OF L-ARABINOSE ISOMERASE IN ESCHERICHIA COLI. Genetics. 1964 Jan;49:95–108. doi: 10.1093/genetics/49.1.95. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Coleman W., Jr, Kline E. L., Brown C. S., Williams L. S. Regulation of branched-chain aminoacyl-transfer ribonucleic acid synthetases in an ilvDAC deletion strain of Escherichia coli K-12. J Bacteriol. 1975 Mar;121(3):785–793. doi: 10.1128/jb.121.3.785-793.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. 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]
  10. Dessein A., Tillier F., Ullmann A. Catabolite modulator factor: physiological properties and in vivo effects. Mol Gen Genet. 1978 Jun 1;162(1):89–94. doi: 10.1007/BF00333854. [DOI] [PubMed] [Google Scholar]
  11. Dickson R. C., Abelson J., Barnes W. M., Reznikoff W. S. Genetic regulation: the Lac control region. Science. 1975 Jan 10;187(4171):27–35. doi: 10.1126/science.1088926. [DOI] [PubMed] [Google Scholar]
  12. 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]
  13. Englesberg E., Irr J., Power J., Lee N. Positive control of enzyme synthesis by gene C in the L-arabinose system. J Bacteriol. 1965 Oct;90(4):946–957. doi: 10.1128/jb.90.4.946-957.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. GROSS J., ENGLESBERG E. Determination of the order of mutational sites governing L-arabinose utilization in Escherichia coli B/r bv transduction with phage Plbt. Virology. 1959 Nov;9:314–331. doi: 10.1016/0042-6822(59)90125-4. [DOI] [PubMed] [Google Scholar]
  15. Greenfield L., Boone T., Wilcox G. DNA sequence of the araBAD promoter in Escherichia coli B/r. Proc Natl Acad Sci U S A. 1978 Oct;75(10):4724–4728. doi: 10.1073/pnas.75.10.4724. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Heffernan L., Bass R., Englesberg E. Mutations affecting catabolite repression of the L-arabinose regulon in Escherichia coli B/r. J Bacteriol. 1976 Jun;126(3):1119–1131. doi: 10.1128/jb.126.3.1119-1131.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Hendry L. B., Witham F. H., Chapman O. L. Gene regulation: the involvement of stereochemical recognition in DNA-small molecule interactions. Perspect Biol Med. 1977 Autumn;21(1):120–130. doi: 10.1353/pbm.1977.0018. [DOI] [PubMed] [Google Scholar]
  18. Hendry L. B., Witham F. H. Stereochemical recognition in nucleic acid-amino acid interactions and its implications in biological coding: a model approach. Perspect Biol Med. 1979 Spring;22(3):333–345. doi: 10.1353/pbm.1979.0002. [DOI] [PubMed] [Google Scholar]
  19. Hogg R. W., Englesberg E. L-arabinose binding protein from Escherichia coli B-r. J Bacteriol. 1969 Oct;100(1):423–432. doi: 10.1128/jb.100.1.423-432.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Kline E. L., Bankaitis V., Brown C. S., Montefiori D. Imidazole acetic acid as a substitute for cAMP. Biochem Biophys Res Commun. 1979 Mar 30;87(2):566–574. doi: 10.1016/0006-291x(79)91832-1. [DOI] [PubMed] [Google Scholar]
  21. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  22. MAKMAN R. S., SUTHERLAND E. W. ADENOSINE 3',5'-PHOSPHATE IN ESCHERICHIA COLI. J Biol Chem. 1965 Mar;240:1309–1314. [PubMed] [Google Scholar]
  23. MEHLER A. H., TABOR H., BAUER H. The oxidation of histamine to imidazoleacetic acid in vivo. J Biol Chem. 1952 May;197(1):475–480. [PubMed] [Google Scholar]
  24. Magasanik B., Lund P., Neidhardt F. C., Schwartz D. T. Induction and repression of the histidine-degrading enzymes in Aerobacter aerogenes. J Biol Chem. 1965 Nov;240(11):4320–4324. [PubMed] [Google Scholar]
  25. Nakanishi S., Adhya S., Gottesman M., Pastan I. Activation of transcription at specific promoters by glycerol. J Biol Chem. 1974 Jul 10;249(13):4050–4056. [PubMed] [Google Scholar]
  26. Parsons R. G., Hogg R. W. Crystallization and characterization of the L-arabinose-binding protein of Escherichia coli B-r. J Biol Chem. 1974 Jun 10;249(11):3602–3607. [PubMed] [Google Scholar]
  27. Patrick J. W., Lee N., Barnes N. B., Englesberg E. Coordination of enzyme synthesis in the L-arabinose operon in Escherichia coli. I. The effect of manganous ion on the synthesis of L-arabinose isomerase. J Biol Chem. 1971 Aug 25;246(16):5102–5106. [PubMed] [Google Scholar]
  28. 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]
  29. Riggs A. D., Reiness G., Zubay G. Purification and DNA-binding properties of the catabolite gene activator protein. Proc Natl Acad Sci U S A. 1971 Jun;68(6):1222–1225. doi: 10.1073/pnas.68.6.1222. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. SUTHERLAND E. W., RALL T. W., MENON T. Adenyl cylase. I. Distribution, preparation, and properties. J Biol Chem. 1962 Apr;237:1220–1227. [PubMed] [Google Scholar]
  31. Schlesinger S., Scotto P., Magasanik B. Exogenous and endogenous induction of the histidine-degrading enzymes in Aerobacter aerogenes. J Biol Chem. 1965 Nov;240(11):4331–4337. [PubMed] [Google Scholar]
  32. Ullmann A., Tillier F., Monod J. Catabolite modulator factor: a possible mediator of catabolite repression in bacteria. Proc Natl Acad Sci U S A. 1976 Oct;73(10):3476–3479. doi: 10.1073/pnas.73.10.3476. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Witham F. H., Hendry L. B., Chapman O. L. Chirality and stereochemical recognition in DNA-phytohormone interactions: a model approach. Orig Life. 1978 Sep;9(1):7–15. doi: 10.1007/BF00929709. [DOI] [PubMed] [Google Scholar]
  34. 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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