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. 1967 May;103(2):358–366. doi: 10.1042/bj1030358

Involvement of the lac regulatory genes in catabolite repression in Escherichia coli

J Palmer 1, V Moses 1
PMCID: PMC1270416  PMID: 5340365

Abstract

1. Acute transient catabolite repression of β-galactosidase synthesis, observed when glucose is added to glycerol-grown cells of Escherichia coli (Moses & Prevost, 1966), requires the presence of a functional operator gene (o) in the lactose operon. Total deletion of the operator gene abolished acute transient repression, even in the presence of a functional regulator gene (i). 2. Regulator constitutives (i−) also show transient repression provided that the operator gene is functional. Regulator deletion mutants (idel), with which to test specifically the role of the i gene, have not so far been available. 3. The above mutants, showing various changes in the lactose operon, show no alteration in the effect of glucose on induced tryptophanase synthesis. Glucose metabolism, as measured in terms of the release of 14CO2 from [1-14C]glucose and [6-14C]glucose, also showed no differences between strains exhibiting or not exhibiting transient repression. This suggests no change in the operation of the pentose phosphate cycle, a metabolic activity known to be of paramount importance for glucose repression of β-galactosidase synthesis (Prevost & Moses, 1967). 4. Chronic permanent repression by glucose of β-galactosidase synthesis (less severe in degree than acute transient repression) persists in strains in which transient repression has been genetically abolished. Constitutive alkaline-phosphatase synthesis, which shows no transient repression, also demonstrates chronic permanent repression by glucose. 5. Chloramphenicol repression also persists in mutants with no transient repression, and also affects alkaline phosphatase. It is suggested that chronic permanent repression and chloramphenicol repression are non-specific, and that they do not influence β-galactosidase synthesis via the regulatory system of the lactose operon.

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Selected References

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  1. CLARK D. J., MARR A. G. STUDIES ON THE REPRESSION OF BETA-GALACTOSIDASE IN ESCHERICHIA COLI. Biochim Biophys Acta. 1964 Oct 23;92:85–94. doi: 10.1016/0926-6569(64)90272-x. [DOI] [PubMed] [Google Scholar]
  2. COHN M., HORIBATA K. Physiology of the inhibition by glucose of the induced synthesis of the beta-galactosideenzyme system of Escherichia coli. J Bacteriol. 1959 Nov;78:624–635. doi: 10.1128/jb.78.5.624-635.1959. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. ECHOLS H., GAREN A., GAREN S., TORRIANI A. Genetic control of repression of alkaline phosphatase in E. coli. J Mol Biol. 1961 Aug;3:425–438. doi: 10.1016/s0022-2836(61)80055-7. [DOI] [PubMed] [Google Scholar]
  4. LOOMIS W. F., Jr, MAGASANIK B. THE RELATION OF CATABOLITE REPRESSION TO THE INDUCTION SYSTEM FOR BETA-GALACTOSIDASE IN ESCHERICHIA COLI. J Mol Biol. 1964 Mar;8:417–426. doi: 10.1016/s0022-2836(64)80205-9. [DOI] [PubMed] [Google Scholar]
  5. Loomis W. F., Jr, Magasanik B. Genetic control of catabolite repression of the lac operon in Escherichia coli. Biochem Biophys Res Commun. 1965 Jul 12;20(2):230–234. doi: 10.1016/0006-291x(65)90351-7. [DOI] [PubMed] [Google Scholar]
  6. MAGASANIK B. Catabolite repression. Cold Spring Harb Symp Quant Biol. 1961;26:249–256. doi: 10.1101/sqb.1961.026.01.031. [DOI] [PubMed] [Google Scholar]
  7. MANDELSTAM J. Induction and repression of beta-galactosidase in non-growing Escherichia coli. Biochem J. 1961 Jun;79:489–496. doi: 10.1042/bj0790489. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. MANDELSTAM J. The repression of constitutive beta-galactosidase in Escherichia coli by glucose and other carbon sources. Biochem J. 1962 Mar;82:489–493. doi: 10.1042/bj0820489. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. MCFALL E. Effects of 32P decay on enzyme synthesis. J Mol Biol. 1961 Apr;3:219–224. doi: 10.1016/s0022-2836(61)80048-x. [DOI] [PubMed] [Google Scholar]
  10. MCFALL E., MAGASANIK B. Thymine starvation and enzyme synthesis. Biochim Biophys Acta. 1960 Dec 18;45:610–612. doi: 10.1016/0006-3002(60)91505-5. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. NAKADA D., MAGASANIK B. THE ROLES OF INDUCER AND CATABOLITE REPRESSOR IN THE SYNTHESIS OF BETA-GALACTOSIDASE BY ESCHERICHIA COLI. J Mol Biol. 1964 Jan;8:105–127. doi: 10.1016/s0022-2836(64)80153-4. [DOI] [PubMed] [Google Scholar]
  13. NEIDHARDT F. C. Mutant of Aerobacter aerogenes lacking glucose repression. J Bacteriol. 1960 Oct;80:536–543. doi: 10.1128/jb.80.4.536-543.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. PAIGEN K. CHANGES IN THE INDUCIBILITY OF GALACTOKINASE AND BETA-GALACTOSIDASE DURING INHIBITION OF GROWTH IN ESCHERICHIA COLI. Biochim Biophys Acta. 1963 Oct 1;77:318–328. doi: 10.1016/0006-3002(63)90502-x. [DOI] [PubMed] [Google Scholar]
  15. Prevost C., Moses V. Pool sizes of metabolic intermediates and their relation to glucose repression of beta-galactosidase synthesis in Escherichia coli. Biochem J. 1967 May;103(2):349–357. doi: 10.1042/bj1030349. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. SYPHERD P. S., STRAUSS N. THE ROLE OF RNA IN REPRESSION OF ENZYME SYNTHESIS. Proc Natl Acad Sci U S A. 1963 Dec;50:1059–1066. doi: 10.1073/pnas.50.6.1059. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Steers E., Jr, Craven G. R., Anfinsen C. B. Comparison of beta-galactosidases from normal (i-o+z+) and operator constitutive (i-ocz+) strains of E. coli. Proc Natl Acad Sci U S A. 1965 Oct;54(4):1174–1181. doi: 10.1073/pnas.54.4.1174. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. TAYLOR A. L., THOMAN M. S. THE GENETIC MAP OF ESCHERICHIA COLI K-12. Genetics. 1964 Oct;50:659–677. doi: 10.1093/genetics/50.4.659. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. TORRIANI A., ROTHMAN F. Mutants of Escherichia coli constitutive for alkaline phosphatase. J Bacteriol. 1961 May;81:835–836. doi: 10.1128/jb.81.5.835-836.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]

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