Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1975 Aug;123(2):391–399. doi: 10.1128/jb.123.2.391-399.1975

Regulation of the lysine biosynthetic pathway in Escherichia coli K-12: isolation of a cis-dominant constitutive mutant for AK III synthesis.

M Cassan, E Boy, F Borne, J C Patte
PMCID: PMC235741  PMID: 238953

Abstract

A method for isolating regulatory mutants for the synthesis of lysine biosynthetic enzymes in Escherichia coli is described. One of them is identified as a cis-dominant constitutive mutant for the synthesis of the lysine-sensitive asportokinase AK III (lysC gene).

Full text

PDF
395

Selected References

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

  1. Boy E., Patte J. C. Multivalent repression of aspartic semialdehyde dehydrogenase in Escherichia coli K-12. J Bacteriol. 1972 Oct;112(1):84–92. doi: 10.1128/jb.112.1.84-92.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. CLARK A. J., MARGULIES A. D. ISOLATION AND CHARACTERIZATION OF RECOMBINATION-DEFICIENT MUTANTS OF ESCHERICHIA COLI K12. Proc Natl Acad Sci U S A. 1965 Feb;53:451–459. doi: 10.1073/pnas.53.2.451. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. COHEN G. N., RICKENBERG H. V. Concentration spécifique réversible des amino acides chez Escherichia coli. Ann Inst Pasteur (Paris) 1956 Nov;91(5):693–720. [PubMed] [Google Scholar]
  4. Celis T. F., Rosenfeld H. J., Maas W. K. Mutant of Escherichia coli K-12 defective in the transport of basic amino acids. J Bacteriol. 1973 Nov;116(2):619–626. doi: 10.1128/jb.116.2.619-626.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Jacoby G. A., Gorini L. A unitary account of the repression mechanism of arginine biosynthesis in Escherichia coli. I. The genetic evidence. J Mol Biol. 1969 Jan 14;39(1):73–87. doi: 10.1016/0022-2836(69)90334-9. [DOI] [PubMed] [Google Scholar]
  6. Jensen R. A. Metabolic interlock. Regulatory interactions exerted between biochemical pathways. J Biol Chem. 1969 Jun 10;244(11):2816–2823. [PubMed] [Google Scholar]
  7. LENNOX E. S. Transduction of linked genetic characters of the host by bacteriophage P1. Virology. 1955 Jul;1(2):190–206. doi: 10.1016/0042-6822(55)90016-7. [DOI] [PubMed] [Google Scholar]
  8. Low B. Formation of merodiploids in matings with a class of Rec- recipient strains of Escherichia coli K12. Proc Natl Acad Sci U S A. 1968 May;60(1):160–167. doi: 10.1073/pnas.60.1.160. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Low K. B. Escherichia coli K-12 F-prime factors, old and new. Bacteriol Rev. 1972 Dec;36(4):587–607. doi: 10.1128/br.36.4.587-607.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Mattern I. E., Pittard J. Regulation of tyrosine biosynthesis in Escherichia coli K-12: isolation and characterization of operator mutants. J Bacteriol. 1971 Jul;107(1):8–15. doi: 10.1128/jb.107.1.8-15.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. PATTE J. C., LOVINY T., COHEN G. N. [Repression of meso-alpha, epsilon-diaminopimelic acid decarboxylase by L-lysine in Escherichia coli]. Biochim Biophys Acta. 1962 Apr 9;58:359–360. doi: 10.1016/0006-3002(62)91024-7. [DOI] [PubMed] [Google Scholar]
  12. Patte J. C., Boy E., Borne F. Role of the lysine-sensitive aspartokinase 3 in the regulation of DAP-decarboxylase synthesis in Escherichia coli K 12. FEBS Lett. 1974 Jul 1;43(1):67–70. doi: 10.1016/0014-5793(74)81107-5. [DOI] [PubMed] [Google Scholar]
  13. Patte J. C., Le Bras G., Cohen G. N. Regulation by methionine of the synthesis of a third aspartokinase and of a second homoserine dehydrogenase in Escherichia coli K 12. Biochim Biophys Acta. 1967 Mar 22;136(2):245–247. doi: 10.1016/0304-4165(67)90069-4. [DOI] [PubMed] [Google Scholar]
  14. Richaud C., Mazat J. P., Gros C., Patte J. C. Subunit structure of aspartokinase 3 of Escherichia coli K12. Eur J Biochem. 1973 Dec 17;40(2):619–629. doi: 10.1111/j.1432-1033.1973.tb03234.x. [DOI] [PubMed] [Google Scholar]
  15. Roth J. R., Antón D. N., Hartman P. E. Histidine regulatory mutants in Salmonella typhimurium. I. Isolation and general properties. J Mol Biol. 1966 Dec 28;22(2):305–323. doi: 10.1016/0022-2836(66)90134-3. [DOI] [PubMed] [Google Scholar]
  16. STACEY K. A., SIMSON E. IMPROVED METHOD FOR THE ISOLATION OF THYMINE-REQUIRING MUTANTS OF ESCHERICHIA COLI. J Bacteriol. 1965 Aug;90:554–555. doi: 10.1128/jb.90.2.554-555.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. 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]
  18. Thèze J., Margarita D., Cohen G. N., Borne F., Patte J. C. Mapping of the structural genes of the three aspartokinases and of the two homoserine dehydrogenases of Escherichia coli K-12. J Bacteriol. 1974 Jan;117(1):133–143. doi: 10.1128/jb.117.1.133-143.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES