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. 1985 Jun 11;13(11):4011–4027. doi: 10.1093/nar/13.11.4011

Nucleotide sequence of the yeast ILV2 gene which encodes acetolactate synthase.

S C Falco, K S Dumas, K J Livak
PMCID: PMC341293  PMID: 2989783

Abstract

We have determined the nucleotide sequence of the yeast ILV2 gene which codes for the amino acid biosynthetic enzyme acetolactate synthase (ALS). ALS has recently been shown to be the target in bacteria, yeast and plants, of the potent new herbicide sulfometuron methyl. The coding sequence for the ILV2 polypeptide contains 2061 base pairs. Comparison of deduced amino acid sequences indicates considerable conservation between the yeast protein and the large subunits of the E. coli ALS II and ALS III isozymes. A major distinction between the three proteins is the presence of an additional 90 amino acids at the amino terminal of the yeast protein. The amino acid sequence in this region shows similarities to yeast mitochondrial transit sequences and may function as such, since yeast ALS is localized in the mitochondria. Consensus sequences for initiation and termination of transcription that are consistent with the ends of the ILV2 mRNA, as well as general amino acid control regulatory sequences have been identified.

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Selected References

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  1. Barnes W. M., Bevan M., Son P. H. Kilo-sequencing: creation of an ordered nest of asymmetric deletions across a large target sequence carried on phage M13. Methods Enzymol. 1983;101:98–122. doi: 10.1016/0076-6879(83)01008-3. [DOI] [PubMed] [Google Scholar]
  2. Bennetzen J. L., Hall B. D. Codon selection in yeast. J Biol Chem. 1982 Mar 25;257(6):3026–3031. [PubMed] [Google Scholar]
  3. Breathnach R., Chambon P. Organization and expression of eucaryotic split genes coding for proteins. Annu Rev Biochem. 1981;50:349–383. doi: 10.1146/annurev.bi.50.070181.002025. [DOI] [PubMed] [Google Scholar]
  4. Carlson M., Botstein D. Two differentially regulated mRNAs with different 5' ends encode secreted with intracellular forms of yeast invertase. Cell. 1982 Jan;28(1):145–154. doi: 10.1016/0092-8674(82)90384-1. [DOI] [PubMed] [Google Scholar]
  5. Chaleff R. S., Mauvais C. J. Acetolactate synthase is the site of action of two sulfonylurea herbicides in higher plants. Science. 1984 Jun 29;224(4656):1443–1445. doi: 10.1126/science.224.4656.1443. [DOI] [PubMed] [Google Scholar]
  6. 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]
  7. Donahue T. F., Daves R. S., Lucchini G., Fink G. R. A short nucleotide sequence required for regulation of HIS4 by the general control system of yeast. Cell. 1983 Jan;32(1):89–98. doi: 10.1016/0092-8674(83)90499-3. [DOI] [PubMed] [Google Scholar]
  8. Eoyang L., Silverman P. M. Purification and subunit composition of acetohydroxyacid synthase I from Escherichia coli K-12. J Bacteriol. 1984 Jan;157(1):184–189. doi: 10.1128/jb.157.1.184-189.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Falco S. C., Dumas K. S. Genetic analysis of mutants of Saccharomyces cerevisiae resistant to the herbicide sulfometuron methyl. Genetics. 1985 Jan;109(1):21–35. doi: 10.1093/genetics/109.1.21. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Friden P., Newman T., Freundlich M. Nucleotide sequence of the ilvB promoter-regulatory region: a biosynthetic operon controlled by attenuation and cyclic AMP. Proc Natl Acad Sci U S A. 1982 Oct;79(20):6156–6160. doi: 10.1073/pnas.79.20.6156. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hase T., Riezman H., Suda K., Schatz G. Import of proteins into mitochondria: nucleotide sequence of the gene for a 70-kd protein of the yeast mitochondrial outer membrane. EMBO J. 1983;2(12):2169–2172. doi: 10.1002/j.1460-2075.1983.tb01718.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hinnebusch A. G., Fink G. R. Repeated DNA sequences upstream from HIS1 also occur at several other co-regulated genes in Saccharomyces cerevisiae. J Biol Chem. 1983 Apr 25;258(8):5238–5247. [PubMed] [Google Scholar]
  13. Hu N., Messing J. The making of strand-specific M13 probes. Gene. 1982 Mar;17(3):271–277. doi: 10.1016/0378-1119(82)90143-3. [DOI] [PubMed] [Google Scholar]
  14. Ikemura T. Correlation between the abundance of yeast transfer RNAs and the occurrence of the respective codons in protein genes. Differences in synonymous codon choice patterns of yeast and Escherichia coli with reference to the abundance of isoaccepting transfer RNAs. J Mol Biol. 1982 Jul 15;158(4):573–597. doi: 10.1016/0022-2836(82)90250-9. [DOI] [PubMed] [Google Scholar]
  15. Kaput J., Goltz S., Blobel G. Nucleotide sequence of the yeast nuclear gene for cytochrome c peroxidase precursor. Functional implications of the pre sequence for protein transport into mitochondria. J Biol Chem. 1982 Dec 25;257(24):15054–15058. [PubMed] [Google Scholar]
  16. Kozak M. Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles. Microbiol Rev. 1983 Mar;47(1):1–45. doi: 10.1128/mr.47.1.1-45.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. LaRossa R. A., Schloss J. V. The sulfonylurea herbicide sulfometuron methyl is an extremely potent and selective inhibitor of acetolactate synthase in Salmonella typhimurium. J Biol Chem. 1984 Jul 25;259(14):8753–8757. [PubMed] [Google Scholar]
  18. LaRossa R. A., Smulski D. R. ilvB-encoded acetolactate synthase is resistant to the herbicide sulfometuron methyl. J Bacteriol. 1984 Oct;160(1):391–394. doi: 10.1128/jb.160.1.391-394.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. 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]
  20. 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]
  21. Lusty C. J., Widgren E. E., Broglie K. E., Nyunoya H. Yeast carbamyl phosphate synthetase. Structure of the yeast gene and homology to Escherichia coli carbamyl phosphate synthetase. J Biol Chem. 1983 Dec 10;258(23):14466–14477. [PubMed] [Google Scholar]
  22. Magee P. T., Robichon-Szulmajster H. The regulation of isoleucine-valine biosynthesis in Saccharomyces cerevisiae. 2. Identification and characterization of mutants lacking the acetohydroxyacid synthetase. Eur J Biochem. 1968 Feb;3(4):502–506. doi: 10.1111/j.1432-1033.1967.tb19559.x. [DOI] [PubMed] [Google Scholar]
  23. Magee P. T., Robichon-Szulmajster H. The regulation of isoleucine-valine biosynthesis in Saccharomyces cerevisiae. 3. Properties and regulation of the activity of acetohydroxyacid synthetase. Eur J Biochem. 1968 Feb;3(4):507–511. doi: 10.1111/j.1432-1033.1967.tb19560.x. [DOI] [PubMed] [Google Scholar]
  24. Ray T. B. Site of action of chlorsulfuron: inhibition of valine and isoleucine biosynthesis in plants. Plant Physiol. 1984 Jul;75(3):827–831. doi: 10.1104/pp.75.3.827. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Ryan E. D., Kohlhaw G. B. Subcellular localization of isoleucine-valine biosynthetic enzymes in yeast. J Bacteriol. 1974 Nov;120(2):631–637. doi: 10.1128/jb.120.2.631-637.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Shaner D. L., Anderson P. C., Stidham M. A. Imidazolinones: potent inhibitors of acetohydroxyacid synthase. Plant Physiol. 1984 Oct;76(2):545–546. doi: 10.1104/pp.76.2.545. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Southern E. M. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol. 1975 Nov 5;98(3):503–517. doi: 10.1016/s0022-2836(75)80083-0. [DOI] [PubMed] [Google Scholar]
  29. Squires C. H., De Felice M., Devereux J., Calvo J. M. Molecular structure of ilvIH and its evolutionary relationship to ilvG in Escherichia coli K12. Nucleic Acids Res. 1983 Aug 11;11(15):5299–5313. doi: 10.1093/nar/11.15.5299. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Stiles J. I., Szostak J. W., Young A. T., Wu R., Consaul S., Sherman F. DNA sequence of a mutation in the leader region of the yeast iso-1-cytochrome c mRNA. Cell. 1981 Jul;25(1):277–284. doi: 10.1016/0092-8674(81)90253-1. [DOI] [PubMed] [Google Scholar]
  31. Viebrock A., Perz A., Sebald W. The imported preprotein of the proteolipid subunit of the mitochondrial ATP synthase from Neurospora crassa. Molecular cloning and sequencing of the mRNA. EMBO J. 1982;1(5):565–571. doi: 10.1002/j.1460-2075.1982.tb01209.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Zalkin H., Yanofsky C. Yeast gene TRP5: structure, function, regulation. J Biol Chem. 1982 Feb 10;257(3):1491–1500. [PubMed] [Google Scholar]
  33. Zaret K. S., Sherman F. DNA sequence required for efficient transcription termination in yeast. Cell. 1982 Mar;28(3):563–573. doi: 10.1016/0092-8674(82)90211-2. [DOI] [PubMed] [Google Scholar]
  34. de Felice M., Lago C. T., Squires C. H., Calvo J. M. Acetohydroxy acid synthase isoenzymes of Escherichia coli K12 and Salmonella typhimurium. Ann Microbiol (Paris) 1982 Mar-Apr;133(2):251–256. [PubMed] [Google Scholar]

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