Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1979 Apr;138(1):40–47. doi: 10.1128/jb.138.1.40-47.1979

Modulation of gene expression by drugs affecting deoxyribonucleic acid gyrase.

B Sanzey
PMCID: PMC218235  PMID: 108253

Abstract

Nalidixic acid (Nal), a drug which affects deoxyribonucleic acid gyrase activity, inhibits the expression of catabolite-sensitive genes: the three maltose operons, the lactose and galactose operons, and the tryptophanase gene. A correlation between the degree of sensitivity to Nal and that to catabolite repression has been observed. The expression of the threonine and tryptophan operons, insensitive to catabolite repression, is insensitive to Nal. The expression of the lacZ gene under the control of the IQ promoter is activated by Nal. Strains carrying a mutation in the nalA locus are resistant to these effects. Novobiocin, which inhibits the negative supercoiling activity of deoxyribonucleic acid gyrase, affects expression of the operons similarly to Nal. The involvement of promoters in Nal and novobiocin action, as well as a possible role of in vivo negative supercoiling in the selectivity of gene expression, are discussed.

Full text

PDF
40

Selected References

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

  1. Abdel-Monem M., Hoffmann-Berling H. Enzymic unwinding of DNA. 1. Purification and characterization of a DNA-dependent ATPase from Escherichia coli. Eur J Biochem. 1976 Jun 1;65(2):431–440. doi: 10.1111/j.1432-1033.1976.tb10358.x. [DOI] [PubMed] [Google Scholar]
  2. BUTTIN G. M'ECANISMES R'EGULATEURS DANS LA BIOSYNTH'ESE DES ENZYMES DU M'ETABOLISME DU GALACTOSE CHEZ ESCHERICHIA COLI K12. I. LA BIOSYNTH'ESE INDUITE DE LA GALACTOKINASE ET L'INDUCTION SIMULTAN'EE DE LA S'EQUENCE ENZYMATIQUE. J Mol Biol. 1963 Aug;7:164–182. doi: 10.1016/s0022-2836(63)80044-3. [DOI] [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. Botchan P., Wang J. C., Echols H. Effect of circularity and superhelicity on transcription from bacteriophagelambda DNA. Proc Natl Acad Sci U S A. 1973 Nov;70(11):3077–3081. doi: 10.1073/pnas.70.11.3077. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Calos M. P. DNA sequence for a low-level promoter of the lac repressor gene and an 'up' promoter mutation. Nature. 1978 Aug 24;274(5673):762–765. doi: 10.1038/274762a0. [DOI] [PubMed] [Google Scholar]
  6. Casadaban M. J. Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J Mol Biol. 1976 Jul 5;104(3):541–555. doi: 10.1016/0022-2836(76)90119-4. [DOI] [PubMed] [Google Scholar]
  7. 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]
  8. Davidson N. Effect of DNA length on the free energy of binding of an unwinding ligand to a supercoiled DNA. J Mol Biol. 1972 May 14;66(2):307–309. doi: 10.1016/0022-2836(72)90482-2. [DOI] [PubMed] [Google Scholar]
  9. Dessein A., Schwartz M., Ullmann A. Catabolite repression in Escherichia coli mutants lacking cyclic AMP. Mol Gen Genet. 1978 Jun 1;162(1):83–87. doi: 10.1007/BF00333853. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. Débarbouillé M., Shuman H. A., Silhavy T. J., Schwartz M. Dominant constitutive mutations in malT, the positive regulator gene of the maltose regulon in Escherichia coli. J Mol Biol. 1978 Sep 15;124(2):359–371. doi: 10.1016/0022-2836(78)90304-2. [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. Falco S. C., Zivin R., Rothman-Denes L. B. Novel template requirements of N4 virion RNA polymerase. Proc Natl Acad Sci U S A. 1978 Jul;75(7):3220–3224. doi: 10.1073/pnas.75.7.3220. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. GOSS W. A., DEITZ W. H., COOK T. M. MECHANISM OF ACTION OF NALIDIXIC ACID ON ESCHERICHIA COLI.II. INHIBITION OF DEOXYRIBONUCLEIC ACID SYNTHESIS. J Bacteriol. 1965 Apr;89:1068–1074. doi: 10.1128/jb.89.4.1068-1074.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Geiger L. E., Morris D. R. Polyamine deficiency reduces the rate of DNA replication fork movement in Escherichia coli. Nature. 1978 Apr 20;272(5655):730–732. doi: 10.1038/272730a0. [DOI] [PubMed] [Google Scholar]
  16. Gellert M., Mizuuchi K., O'Dea M. H., Itoh T., Tomizawa J. I. Nalidixic acid resistance: a second genetic character involved in DNA gyrase activity. Proc Natl Acad Sci U S A. 1977 Nov;74(11):4772–4776. doi: 10.1073/pnas.74.11.4772. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Gellert M., Mizuuchi K., O'Dea M. H., Nash H. A. DNA gyrase: an enzyme that introduces superhelical turns into DNA. Proc Natl Acad Sci U S A. 1976 Nov;73(11):3872–3876. doi: 10.1073/pnas.73.11.3872. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Gellert M., O'Dea M. H., Itoh T., Tomizawa J. Novobiocin and coumermycin inhibit DNA supercoiling catalyzed by DNA gyrase. Proc Natl Acad Sci U S A. 1976 Dec;73(12):4474–4478. doi: 10.1073/pnas.73.12.4474. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Griffith J. D. Visualization of prokaryotic DNA in a regularly condensed chromatin-like fiber. Proc Natl Acad Sci U S A. 1976 Feb;73(2):563–567. doi: 10.1073/pnas.73.2.563. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Hane M. W., Wood T. H. Escherichia coli K-12 mutants resistant to nalidixic acid: genetic mapping and dominance studies. J Bacteriol. 1969 Jul;99(1):238–241. doi: 10.1128/jb.99.1.238-241.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Hofnung M. Divergent operons and the genetic structure of the maltose B region in Escherichia coli K12. Genetics. 1974 Feb;76(2):169–184. doi: 10.1093/genetics/76.2.169. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Kornberg R. D. Structure of chromatin. Annu Rev Biochem. 1977;46:931–954. doi: 10.1146/annurev.bi.46.070177.004435. [DOI] [PubMed] [Google Scholar]
  23. Müller-Hill B., Kania J. Lac repressor can be fused to beta-galactosidase. Nature. 1974 Jun 7;249(457):561–563. doi: 10.1038/249561a0. [DOI] [PubMed] [Google Scholar]
  24. Rouvière-Yaniv J., Gros F. Characterization of a novel, low-molecular-weight DNA-binding protein from Escherichia coli. Proc Natl Acad Sci U S A. 1975 Sep;72(9):3428–3432. doi: 10.1073/pnas.72.9.3428. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Ryan M. J. Coumermycin A1: A preferential inhibitor of replicative DNA synthesis in Escherichia coli. I. In vivo characterization. Biochemistry. 1976 Aug 24;15(17):3769–3777. doi: 10.1021/bi00662a020. [DOI] [PubMed] [Google Scholar]
  26. Saint-Girons I. New regulatory mutations affecting the expression of the threonine operon in Escherichia coli K-12. Mol Gen Genet. 1978 Jun 1;162(1):95–100. doi: 10.1007/BF00333855. [DOI] [PubMed] [Google Scholar]
  27. Saucier J. M., Wang J. C. Angular alteration of the DNA helix by E. coli RNA polymerase. Nat New Biol. 1972 Oct 11;239(93):167–170. doi: 10.1038/newbio239167a0. [DOI] [PubMed] [Google Scholar]
  28. Schrenk W. J., Miller J. H. Specialized transducing phages carrying fusions of the trp and lac regions of the E. coli chromosome. Mol Gen Genet. 1974;131(1):9–19. doi: 10.1007/BF00269382. [DOI] [PubMed] [Google Scholar]
  29. Schwartz M. Expression phénotypique et localisation génétique de mutations affectant le métabolisme du maltose chez Escherichia coli K 12. Ann Inst Pasteur (Paris) 1967 Jun;112(6):673–698. [PubMed] [Google Scholar]
  30. Shuman H., Schwartz M. The effect of nalidixic acid on the expression of some genes in Escherichia coli K-12. Biochem Biophys Res Commun. 1975 May 5;64(1):204–209. doi: 10.1016/0006-291x(75)90239-9. [DOI] [PubMed] [Google Scholar]
  31. Silhavy T. J., Casadaban M. J., Shuman H. A., Beckwith J. R. Conversion of beta-galactosidase to a membrane-bound state by gene fusion. Proc Natl Acad Sci U S A. 1976 Oct;73(10):3423–3427. doi: 10.1073/pnas.73.10.3423. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Silverstone A. E., Arditti R. R., Magasanik B. Catabolite-insensitive revertants of lac promoter mutants. Proc Natl Acad Sci U S A. 1970 Jul;66(3):773–779. doi: 10.1073/pnas.66.3.773. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Smith C. L., Kubo M., Imamoto F. Promoter-specific inhibition of transcription by antibiotics which act on DNA gyrase. Nature. 1978 Oct 5;275(5679):420–423. doi: 10.1038/275420a0. [DOI] [PubMed] [Google Scholar]
  34. Suelter C. H., Wang J., Snell E. E. Direct spectrophotometric assay of tryptophanase. FEBS Lett. 1976 Jul 15;66(2):230–232. doi: 10.1016/0014-5793(76)80510-8. [DOI] [PubMed] [Google Scholar]
  35. Sugino A., Peebles C. L., Kreuzer K. N., Cozzarelli N. R. Mechanism of action of nalidixic acid: purification of Escherichia coli nalA gene product and its relationship to DNA gyrase and a novel nicking-closing enzyme. Proc Natl Acad Sci U S A. 1977 Nov;74(11):4767–4771. doi: 10.1073/pnas.74.11.4767. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. 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]
  37. 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]
  38. Wang J. C. Interaction between DNA and an Escherichia coli protein omega. J Mol Biol. 1971 Feb 14;55(3):523–533. doi: 10.1016/0022-2836(71)90334-2. [DOI] [PubMed] [Google Scholar]
  39. Wang J. C. Interactions between twisted DNAs and enzymes: the effects of superhelical turns. J Mol Biol. 1974 Aug 25;87(4):797–816. doi: 10.1016/0022-2836(74)90085-0. [DOI] [PubMed] [Google Scholar]
  40. Weiner J. H., Bertsch L. L., Kornberg A. The deoxyribonucleic acid unwinding protein of Escherichia coli. Properties and functions in replication. J Biol Chem. 1975 Mar 25;250(6):1972–1980. [PubMed] [Google Scholar]
  41. Winshell E. B., Rosenkranz H. S. Nalidixic Acid and the Metabolism of Escherichia coli. J Bacteriol. 1970 Dec;104(3):1168–1175. doi: 10.1128/jb.104.3.1168-1175.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Worcel A., Burgi E. On the structure of the folded chromosome of Escherichia coli. J Mol Biol. 1972 Nov 14;71(2):127–147. doi: 10.1016/0022-2836(72)90342-7. [DOI] [PubMed] [Google Scholar]
  43. 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]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES