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. 1972 Jun;110(3):1127–1134. doi: 10.1128/jb.110.3.1127-1134.1972

New Amino Acid Regulatory Locus Having Unusual Properties in Heterozygous Merodiploids

Ellis L Kline 1
PMCID: PMC247536  PMID: 4555405

Abstract

Spontaneous mutants of Escherichia coli B/r resistant to 5′,5′,5′,-trifluoro-dl-leucine contain defects in a gene which maps to the left of the threonine region. Low-level constitutive expression of the isoleucine-valine and leucine operons is caused by this mutation in haploid strains. This is in contrast to extremely high levels of gene expression in the heterozygous merodiploids (F' wild type/mutant allele). The properties of these mutants define a new locus and suggest that it encodes a subunit protein which is involved in the repression of the structural genes for the branched-chain amino acid pathways.

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Selected References

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  1. ARMSTRONG F. B., WAGNER R. P. ISOLEUCINE-VALINE REQUIRING MUTANTS OF SALMONELLA TYPHIMURIUM. Genetics. 1964 Nov;50:957–965. doi: 10.1093/genetics/50.5.957. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Alexander R. R., Calvo J. M., Freundlich M. Mutants of Salmonella typhimurium with an altered leucyl-transfer ribonucleic acid synthetase. J Bacteriol. 1971 Apr;106(1):213–220. doi: 10.1128/jb.106.1.213-220.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Boyer H. W., Roulland-Dussoix D. A complementation analysis of the restriction and modification of DNA in Escherichia coli. J Mol Biol. 1969 May 14;41(3):459–472. doi: 10.1016/0022-2836(69)90288-5. [DOI] [PubMed] [Google Scholar]
  4. Burns R. O., Calvo J., Margolin P., Umbarger H. E. Expression of the leucine operon. J Bacteriol. 1966 Apr;91(4):1570–1576. doi: 10.1128/jb.91.4.1570-1576.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Calvo J. M., Freundlich M., Umbarger H. E. Regulation of branched-chain amino acid biosynthesis in Salmonella typhimurium: isolation of regulatory mutants. J Bacteriol. 1969 Mar;97(3):1272–1282. doi: 10.1128/jb.97.3.1272-1282.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Calvo J. M., Morgolin P., Umbarger H. E. Operator constitutive mutations in the leucine operon of Salmonella typhimurium. Genetics. 1969 Apr;61(4):777–787. doi: 10.1093/genetics/61.4.777. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Davies J., Jacob F. Genetic mapping of the regulator and operator genes of the lac operon. J Mol Biol. 1968 Sep 28;36(3):413–417. doi: 10.1016/0022-2836(68)90165-4. [DOI] [PubMed] [Google Scholar]
  8. Doolittle W. F., Yanofsky C. Mutants of Escherichia coli with an altered tryptophanyl-transfer ribonucleic acid synthetase. J Bacteriol. 1968 Apr;95(4):1283–1294. doi: 10.1128/jb.95.4.1283-1294.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. EIDLIC L., NEIDHARDT F. C. ROLE OF VALYL-SRNA SYNTHETASE IN ENZYME REPRESSION. Proc Natl Acad Sci U S A. 1965 Mar;53:539–543. doi: 10.1073/pnas.53.3.539. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. FREUNDLICH M., BURNS R. O., UMBARGER H. E. Control of isoleucine, valine, and leucine biosynthesis. I. Multivalent repression. Proc Natl Acad Sci U S A. 1962 Oct 15;48:1804–1808. doi: 10.1073/pnas.48.10.1804. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. GAREN A., ECHOLS H. Genetic control of induction of alkaline phosphatase synthesis in E. coli. Proc Natl Acad Sci U S A. 1962 Aug;48:1398–1402. doi: 10.1073/pnas.48.8.1398. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. 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]
  13. Hatfield G. W., Burns R. O. Specific binding of leucyl transfer RNA to an immature form of L-threonine deaminase: its implications in repression. Proc Natl Acad Sci U S A. 1970 Aug;66(4):1027–1035. doi: 10.1073/pnas.66.4.1027. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Iaccarino M., Berg P. Isoleucine auxotrophy as a consequence of a mutationally altered isoleucyl-transfer ribonucleic acid synthetase. J Bacteriol. 1971 Feb;105(2):527–537. doi: 10.1128/jb.105.2.527-537.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Ito J., Crawford I. P. Regulation of the enzymes of the tryptophan pathway in Escherichia coli. Genetics. 1965 Dec;52(6):1303–1316. doi: 10.1093/genetics/52.6.1303. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Ito K., Hiraga S., Yura T. Tryptophanyl transfer RNA synthetase and expression of the tryptophan operon in the trpS mutants of Escherichia coli. Genetics. 1969 Mar;61(3):521–538. doi: 10.1093/genetics/61.3.521. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Jensen R. A. Metabolic interlock. Regulatory interactions exerted between biochemical pathways. J Biol Chem. 1969 Jun 10;244(11):2816–2823. [PubMed] [Google Scholar]
  18. Kadner R. J., Maas W. K. Regulatory gene mutations affecting arginine biosynthesis in Escherichia coli. Mol Gen Genet. 1971;111(1):1–14. doi: 10.1007/BF00286549. [DOI] [PubMed] [Google Scholar]
  19. Kane J. F., Jensen R. A. Metabolic interlock. The influence of histidine on tryptophan biosynthesis in Bacillus subtilis. J Biol Chem. 1970 May 10;245(9):2384–2390. [PubMed] [Google Scholar]
  20. Kessler D. P., Englesberg E. Arabinose-leucine deletion mutants of Escherichia coli B-r. J Bacteriol. 1969 Jun;98(3):1159–1169. doi: 10.1128/jb.98.3.1159-1169.1969. [DOI] [PMC free article] [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. 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]
  23. Low B., Gates F., Goldstein T., Söll D. Isolation and partial characterization of temperature-sensitive Escherichia coli mutants with altered leucyl- and seryl-transfer ribonucleic acid synthetases. J Bacteriol. 1971 Nov;108(2):742–750. doi: 10.1128/jb.108.2.742-750.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. MARGOLIN P. Genetic fine structure of the leucine operon in Salmonella. Genetics. 1963 Mar;48:441–457. doi: 10.1093/genetics/48.3.441. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Markovitz A., Rosenbaum N. A regulator gene that is dominant on an episome and recessive on a chromosome. Proc Natl Acad Sci U S A. 1965 Oct;54(4):1084–1091. doi: 10.1073/pnas.54.4.1084. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Morse D. E., Yanofsky C. Amber mutants of the trpR regulatory gene. J Mol Biol. 1969 Aug 28;44(1):185–193. doi: 10.1016/0022-2836(69)90413-6. [DOI] [PubMed] [Google Scholar]
  27. Mosteller R. D., Yanofsky C. Evidence that tryptophanyl transfer ribonucleic acid is not the corepressor of the tryptophan operon of Escherichia coli. J Bacteriol. 1971 Jan;105(1):268–275. doi: 10.1128/jb.105.1.268-275.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Neidhardt F. C. Roles of amino acid activating enzymes in cellular physiology. Bacteriol Rev. 1966 Dec;30(4):701–719. doi: 10.1128/br.30.4.701-719.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. RAMAKRISHNAN T., ADELBERG E. A. REGULATORY MECHANISMS IN THE BIOSYNTHESIS OF ISOLEUCINE AND VALINE. 3. MAP ORDER OF THE STRUCTURAL GENES AND OPERATOR GENES. J Bacteriol. 1965 Mar;89:661–664. doi: 10.1128/jb.89.3.661-664.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. RAMAKRISHNAN T., ADELBERG E. A. REGULATORY MECHANISMS IN THE BIOSYNTHESIS OF ISOLEUCINE AND VALINE. I. GENETIC DEREPRESSION OF ENZYME FORMATION. J Bacteriol. 1964 Mar;87:566–573. doi: 10.1128/jb.87.3.566-573.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. RAMAKRISHNAN T., ADELBERG E. A. REGULATORY MECHANISMS IN THE BIOSYNTHESIS OF ISOLEUCINE AND VALINE. II. IDENTIFICATION OF TWO OPERATOR GENES. J Bacteriol. 1965 Mar;89:654–660. doi: 10.1128/jb.89.3.654-660.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. RENNERT O. M., ANKER H. S. ON THE INCORPORATION OF 5',5',5'-TRIFLUOROLEUCINE INTO PROTEINS OF E. COLI. Biochemistry. 1963 May-Jun;2:471–476. doi: 10.1021/bi00903a013. [DOI] [PubMed] [Google Scholar]
  33. Roth J. R., Ames B. N. Histidine regulatory mutants in Salmonella typhimurium II. Histidine regulatory mutants having altered histidyl-tRNA synthetase. J Mol Biol. 1966 Dec 28;22(2):325–333. doi: 10.1016/0022-2836(66)90135-5. [DOI] [PubMed] [Google Scholar]
  34. Roth J. R., Sanderson K. E. Orientation of the isoleucine-valine genes in the Salmonella typhimurium linkage map. Genetics. 1966 May;53(5):971–976. doi: 10.1093/genetics/53.5.971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Sheppard D. E., Englesberg E. Further evidence for positive control of the L-arabinose system by gene araC. J Mol Biol. 1967 May 14;25(3):443–454. doi: 10.1016/0022-2836(67)90197-0. [DOI] [PubMed] [Google Scholar]
  36. Szentirmai A., Szentirmai M., Umbarger H. E. Isoleucine and valine metabolism of Escherichia coli. XV. Biochemical properties of mutants resistant to thiaisoleucine. J Bacteriol. 1968 May;95(5):1672–1679. doi: 10.1128/jb.95.5.1672-1679.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Taylor A. L. Current linkage map of Escherichia coli. Bacteriol Rev. 1970 Jun;34(2):155–175. doi: 10.1128/br.34.2.155-175.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Wechsler J. A., Adelberg E. A. Antipolarity in the ilv operon of Escherichia coli K-12. J Bacteriol. 1969 Jun;98(3):1179–1194. doi: 10.1128/jb.98.3.1179-1194.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]

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