Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1982 Aug;151(2):860–866. doi: 10.1128/jb.151.2.860-866.1982

Altered regulation of isoleucine-valine biosynthesis in a hisW mutant of Salmonella typhimurium.

L Davis, L S Williams
PMCID: PMC220336  PMID: 7047499

Abstract

Control of isoleucine-valine biosynthesis was examined in the cold-sensitive hisW3333 mutant strain of Salmonella typhimurium. During growth at the permissive temperature (37 degrees C), the isoleucine-valine (ilv) biosynthetic enzyme levels of the hisW mutant were two- to fourfold below these levels in an isogenic hisW+ strain. Upon a reduction in growth temperature to partially permissive (30 degrees C), the synthesis of these enzymes in the hisW mutant was further reduced. However, synthesis of the ilv enzymes was responsive to the repression signal(s) caused by the addition of excess amounts of isoleucine, valine, and leucine to the hisW mutants. Such a "super-repressed" phenotype as that observed in this hisW mutant is similar to that previously shown for the hisU1820 mutant, but was different from the regulatory response of the hisT1504 mutant strain. Moreover, by the use of growth-rate-limiting amounts of the branched-chain amino acids, it was shown that this hisW mutant generally did not increase the synthesis of the ilv enzymes as did the hisW+ strain. Overall, these results are in agreement with the hypothesis that the hisW mutant is less responsive to ilv specific attenuation control than is the hisW+ strain and suggest that this limited regulatory response is due to an alteration in the amount or structure of an element essential to attenuation control of the ilv operons.

Full text

PDF
860

Selected References

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

  1. Arfin S. M., Ratzkin B., Umbarger H. E. The metabolism of valine and isoleucine in Escherichia coli. XVII. The role of induction in the derepression of acetohydroxy acid isomeroreductase. Biochem Biophys Res Commun. 1969 Dec 4;37(6):902–908. doi: 10.1016/0006-291x(69)90216-2. [DOI] [PubMed] [Google Scholar]
  2. Bachmann B. J., Low K. B. Linkage map of Escherichia coli K-12, edition 6. Microbiol Rev. 1980 Mar;44(1):1–56. doi: 10.1128/mr.44.1.1-56.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Berg C. M., Shaw K. J., Vender J., Borucka-Mankiewicz M. Physiological characterization of polar Tn5-induced isoleucine-valine auxotrophs in Escherichia coli K.12: evidence for an internal promoter in the ilvOGEDA operon. Genetics. 1979 Oct;93(2):308–319. [PMC free article] [PubMed] [Google Scholar]
  4. Blazey D. L., Kim R., Burns R. O. Molecular cloning and expression of the ilvGEDAY genes from Salmonella typhimurium. J Bacteriol. 1981 Aug;147(2):452–462. doi: 10.1128/jb.147.2.452-462.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bossi L., Ciampi M. S., Cortese R. Characterization of a Salmonella typhimurium hisU mutant defective in tRNA precursor processing. J Bacteriol. 1978 May;134(2):612–620. doi: 10.1128/jb.134.2.612-620.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Brenchley J. E., Ingraham J. L. Characterization of a cold-sensitive hisW mutant of Salmonella typhimurium. J Bacteriol. 1973 May;114(2):528–536. doi: 10.1128/jb.114.2.528-536.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Brenner M., Ames B. N. Histidine regulation in Salmonella typhimurium. IX. Histidine transfer ribonucleic acid of the regulatory mutants. J Biol Chem. 1972 Feb 25;247(4):1080–1088. [PubMed] [Google Scholar]
  8. Cortese R., Landsberg R., Haar R. A., Umbarger H. E., Ames B. N. Pleiotropy of hisT mutants blocked in pseudouridine synthesis in tRNA: leucine and isoleucine-valine operons. Proc Natl Acad Sci U S A. 1974 May;71(5):1857–1861. doi: 10.1073/pnas.71.5.1857. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Davidson J. P., Williams L. S. Regulation of isoleucine and valine biosynthesis in Salmonella typhimurium: the effect of hisU on repression control. J Mol Biol. 1979 Jan 15;127(2):229–235. doi: 10.1016/0022-2836(79)90244-4. [DOI] [PubMed] [Google Scholar]
  10. Davidson J. P., Williams L. S. Relaxed control of RNA synthesis during nutritional shiftdowns of hisU mutant of Salmonella typhimurium. Biochem Biophys Res Commun. 1979 May 28;88(2):682–687. doi: 10.1016/0006-291x(79)92102-8. [DOI] [PubMed] [Google Scholar]
  11. Davis L., Williams L. S. Characterization of a cold-sensitive hisW mutant of Salmonella typhimurium. J Bacteriol. 1982 Aug;151(2):867–878. doi: 10.1128/jb.151.2.867-878.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. De Felice M., Guardiola J., Esposito B., Iaccarino M. Structural genes for a newly recognized acetolactate synthase in Escherichia coli K-12. J Bacteriol. 1974 Dec;120(3):1068–1077. doi: 10.1128/jb.120.3.1068-1077.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. De Felice M., Levinthal M. The acetohydroxy acid synthase III isoenzyme of Escherichia coli K-12: regulation of synthesis by leucine. Biochem Biophys Res Commun. 1977 Nov 7;79(1):82–87. doi: 10.1016/0006-291x(77)90063-8. [DOI] [PubMed] [Google Scholar]
  14. Duggan D. E., Wechsler J. A. An assay for transaminase B enzyme activity in Escherichia coli K-12. Anal Biochem. 1973 Jan;51(1):67–79. doi: 10.1016/0003-2697(73)90453-3. [DOI] [PubMed] [Google Scholar]
  15. FRAENKEL D. G., NEIDHARDT F. C. Use of chloramphenicol to study control of RNA synthesis in bacteria. Biochim Biophys Acta. 1961 Oct 14;53:96–110. doi: 10.1016/0006-3002(61)90797-1. [DOI] [PubMed] [Google Scholar]
  16. 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]
  17. Favre R., Wiater A., Puppo S., Iaccarino M. Expression of a valine-resistant acetolactate synthase activity mediated by the ilv O and ilv G genes of Escherichia coli K-12. Mol Gen Genet. 1976 Feb 2;143(3):243–252. doi: 10.1007/BF00269400. [DOI] [PubMed] [Google Scholar]
  18. LOVELESS A., HOWARTH S. Mutation of bacteria at high levels of survival by ethyl methane sulphonate. Nature. 1959 Dec 5;184:1780–1782. doi: 10.1038/1841780a0. [DOI] [PubMed] [Google Scholar]
  19. 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]
  20. Lawther R. P., Calhoun D. H., Adams C. W., Hauser C. A., Gray J., Hatfield G. W. Molecular basis of valine resistance in Escherichia coli K-12. Proc Natl Acad Sci U S A. 1981 Feb;78(2):922–925. doi: 10.1073/pnas.78.2.922. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Lawther R. P., Hatfield G. W. Multivalent translational control of transcription termination at attenuator of ilvGEDA operon of Escherichia coli K-12. Proc Natl Acad Sci U S A. 1980 Apr;77(4):1862–1866. doi: 10.1073/pnas.77.4.1862. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Nargang F. E., Subrahmanyam C. S., Umbarger H. E. Nucleotide sequence of ilvGEDA operon attenuator region of Escherichia coli. Proc Natl Acad Sci U S A. 1980 Apr;77(4):1823–1827. doi: 10.1073/pnas.77.4.1823. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Newman T. C., Levinthal M. A new map location for the ilvB locus of Escherichia coli. Genetics. 1980 Sep;96(1):59–77. doi: 10.1093/genetics/96.1.59. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Ratzkin B., Arfin S., Umbarger H. E. Isoleucine and valine metabolism in Escherichia coli. 18. Induction of acetohydroxy acid isomeroreductase. J Bacteriol. 1972 Oct;112(1):131–141. doi: 10.1128/jb.112.1.131-141.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Rizzino A. A., Bresalier R. S., Freundlich M. Derepressed levels of the isoleucine-valine and leucine enzymes in his T 1504, a strain of Salmonella typhimurium with altered leucine transfer ribonucleic acid. J Bacteriol. 1974 Feb;117(2):449–455. doi: 10.1128/jb.117.2.449-455.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. 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]
  27. Sanderson K. E., Hartman P. E. Linkage map of Salmonella typhimurium, edition V. Microbiol Rev. 1978 Jun;42(2):471–519. doi: 10.1128/mr.42.2.471-519.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Singer C. E., Smith G. R., Cortese R., Ames B. N. [Mutant tRNA His ineffective in repression and lacking two pseudouridine modifications]. Nat New Biol. 1972 Jul 19;238(81):72–74. doi: 10.1038/newbio238072a0. [DOI] [PubMed] [Google Scholar]
  29. Squires C. H., De Felice M., Wessler S. R., Calvo J. M. Physical characterization of the ilvHI operon of Escherichia coli K-12. J Bacteriol. 1981 Sep;147(3):797–804. doi: 10.1128/jb.147.3.797-804.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Umbarger H. E. Amino acid biosynthesis and its regulation. Annu Rev Biochem. 1978;47:532–606. doi: 10.1146/annurev.bi.47.070178.002533. [DOI] [PubMed] [Google Scholar]
  31. Watson M. D., Wild J., Umbarger H. E. Positive control of ilvC expression in Escherichia coli K-12; identification and mapping of regulatory gene ilvY. J Bacteriol. 1979 Sep;139(3):1014–1020. doi: 10.1128/jb.139.3.1014-1020.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES