Skip to main content
Log in

Acetohydroxy acid synthase isoenzymes of Escherichia coli K-12: A trans-acting regulatory locus for ilvHI gene expression

  • Published:
Molecular and General Genetics MGG Aims and scope Submit manuscript

Summary

We isolated an Escherichia coli K-12 regulatory mutation affecting the acetohydroxy acid synthase III isoenzyme. This mutation was found to lie outside the structural genes ilvHI for this isoenzyme and was designated lrs-1. A strain carrying this mutation was found to be altered in the leucine-mediated control of ilvHI mRNA and acetohydroxy acid synthase III synthesis observed in the isogenic lrs + strain. These alterations appeared to be a consequence of a reduced intracellular concentration of a single one of five tRNALeu isoaccepting species.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Abrescia P, Guardiola J, Foresti M, Lamberti A, Iaccarino M (1979) Threonine deaminase: autogenous regulator of the ilv genes in Escherichia coli K-12. Mol Gen Genet 171:261–275

    Google Scholar 

  • Andoh T, Ozeki H (1968) Suppressor gene su3 of E. coli, a structural gene for tyrosine tRNA. Proc Natl Acad Sci USA 59:792–799

    Google Scholar 

  • Bachmann BJ, Low KB (1980) Linkage map of Escherichia coli K-12, edition 6. Microbiol Rev 44:1–56

    Google Scholar 

  • Bachmann BJ, Low KB, Taylor AL (1976) Recalibrated linkage map of Escherichia coli K-12. Bacteriol Rev 40:116–167

    Google Scholar 

  • Brenner M, Ames BN (1971) The histidine operon and its regulation. In: Vogel HJ (ed) Metabolic pathways, vol V. Academic Press, London-New York, pp 349–387

    Google Scholar 

  • Brenner M, Ames BN (1972) Histidine regulation in Salmonella typhimurium. IX. Histidine transfer ribonucleic acid of the regulatory mutants. J Biol Chem 247:1080–1088

    Google Scholar 

  • Burns RO, Calvo J, Margolin P, Umbarger HE (1966) Expression of the leucine operon. J Bacteriol 91:1570–1576

    Google Scholar 

  • Cooper TC, Whitney P, Magasanik B (1974) Reaction of lac-specific ribonucleic acid from Escherichia coli with lac deoxyribonucleic acid. J Biol Chem 249:6458–6555

    Google Scholar 

  • Cortese R (1979) The role of tRNA in regulation. In: Goldberger RF (ed) Biological regulation and development, vol 1. Plenum Press, London-New York, pp 401–432

    Google Scholar 

  • De Felice M, Guardiola J, Esposito B, Iaccarino M (1974) Structural genes for a newly recognized acetolactafe synthase in Escherichia coli K-12. J Bacteriol 120:1068–1077

    Google Scholar 

  • de Felice M, Guardiola J, Lamberti A, Iaccarino M (1973) Escherichia coli K-12 mutants altered in the transport systems for oligo- and dipeptides. J Bacteriol 116:751–756

    Google Scholar 

  • De Felice M, Guardiola J, Schreil W, Levinthal M, Iaccarino M (1977) Metabolic interlock between the acetolactate synthase isoenzymes and lysine biosynthesis in Escherichia coli K-12. Mol Gen Genet 156:9–16

    Google Scholar 

  • De Felice M, Levinthal M (1977) The acetohydroxy acid synthase III isoenzyme of Escherichia coli K-12: regulation of synthesis by leucine. Biochem Biophys Res Commun 79:82–87

    Google Scholar 

  • De Felice M, Levinthal M, Iaccarino M, Guardiola J (1979) Growth inhibition as a consequence of antagonism between related amino acids: effect of valine in Escherichia coli K-12. Microbiol Rev 43:42–58

    Google Scholar 

  • De Felice M, Newman T, Levinthal M (1978a) Regulation of synthesis of the acetohydroxy acid synthase I isoenzyme in Escherichia coli K-12. Biochim Biophys Acta 541:1–8

    Google Scholar 

  • De Felice M, Squires C, Levinthal M (1978b) A comparative study of the acetohydroxy acid synthase isoenzymes of Escherichia coli K-12. Biochim Biophys Acta 541:9–17

    Google Scholar 

  • Fayerman JT, Vann MC, Williams LS, Umbarger HE (1979) ilvU, a locus in Escherichia coli affecting the derepression of isoleucyl-tRNA synthetase and the RPC-5 chromatographic prophiles of tRNAIle and tRNAVal. J Biol Chem 254:9429–9440

    Google Scholar 

  • Freundlich M, Clarke LP (1968) Control of isoleucine, valine and leucine biosynthesis. V. Dual effect of α-aminobutyric acid on repression and end product inhibition in Escherichia coli. Biochim Biophys Acta 170:271–281

    Google Scholar 

  • Groves WE, Davis FC Jr, Sells B (1968) Spectrophotometric determination of microgram quantities of protein without nucleic acid interference. Anal Biochem 22:195–210

    Google Scholar 

  • Holmes WM, Goldman E, Miner TA, Hatfield GW (1977) Differential utilization of leucyl-tRNAs by Escherichia coli. Proc Natl Acad Sci USA 74:1393–1397

    Google Scholar 

  • Iaccarino M, Berg P (1971) Isoleucine auxotrophy as a consequence of a mutationally altered isoleucyl-transfer ribonucleic acid synthetase. J Bacteriol 105:527–537

    Google Scholar 

  • La Cara F, De Felice M (1979) Chromatographic detection of the acetohydroxy acid synthase isoenzymes of Escherichia coli K-12. Biochem Biophys Res Commun 91:319–326

    Google Scholar 

  • Miller JH (1972) Experiments in molecular genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y., pp 101–103

    Google Scholar 

  • Muench KH, Berg P (1966) Fractionation of transfer ribonucleic acid by gradient partition chromatography on sephadex columns. Biochemistry 5:970–981

    Google Scholar 

  • Pearson RL, Weiss JF, Kelmers AD (1971) Improved separation of transfer RNAs on polychlorotrifluoroethylene-supported reversedphase chromatography columns. Biochim Biophys Acta 228:770–774

    Google Scholar 

  • Rizzino A, Mastanduno M, Freundlich M (1977) Partial derepression of the isoleucine-valine enzymes during methionine starvation in Salmonella typhimurium. Biochim Biophys Acta 475:267–275

    Google Scholar 

  • Rosner JL (1972) Formation, induction and curing of bacteriophage P1 lysogens. Virology 48:679–689

    Google Scholar 

  • Smith DR, Calvo JM (1979) Regulation of dihydrofolate reductase synthesis in Escherichia coli. Mol Gen Genet 175:31–38

    Google Scholar 

  • Størmer FC, Umbarger HE (1964) The requirement for flavine adenine dinucleotide in the formation of acetolactate by Salmonella typhimurium extracts. Biochem Biophys Res Commun 17:587–592

    Google Scholar 

  • Umbarger HE (1978) Amino acid biosynthesis and its regulation. Annu Rev Biochem 47:533–606

    Google Scholar 

  • Umbarger HE, Freundlich M (1965) Isoleucine and valine metabolism in Escherichia coli. XIII. The role of repression in the sensitivity of strain K-12 to valine. Biochem Biophys Res Commun 18:889–897

    Google Scholar 

  • Vogel HJ, Bonner DM (1956) Acetylornitase of Escherichia coli: partial purification and some properties. J Biol Chem 218:97–106

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

Communicated by A. Böck

Rights and permissions

Reprints and permissions

About this article

Cite this article

Ursini, M.V., Arcari, P. & De Felice, M. Acetohydroxy acid synthase isoenzymes of Escherichia coli K-12: A trans-acting regulatory locus for ilvHI gene expression. Molec. Gen. Genet. 181, 491–496 (1981). https://doi.org/10.1007/BF00428741

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00428741

Keywords

Navigation