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Gene Review

ILV2  -  acetolactate synthase catalytic subunit

Saccharomyces cerevisiae S288c

Synonyms: AHAS, ALS, Acetohydroxy-acid synthase catalytic subunit, Acetolactate synthase catalytic subunit, mitochondrial, SMR1, ...
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Disease relevance of ILV2


High impact information on ILV2

  • The yeast interaction trap system allowed us to determine whether these mutations in SOD1 caused novel protein interactions not observed with wild-type SOD1 and which might participate in the generation of the ALS phenotype [6].
  • The instability of rho+ mtDNA in delta ilv5 cells is not simply a consequence of a block in branched-chain amino acid biosynthesis, since mtDNA is stable in cells with a null allele of the ILV2 gene, which encodes another enzyme of that pathway [7].
  • Several of the ALS-associated mutant copper-zinc superoxide dismutases were also found to be reduced by ascorbate at significantly greater rate than the wild-type proteins [4].
  • The ALS (agglutinin-like sequence) gene family encodes proteins that play a role in adherence of the yeast Candida albicans to endothelial and epithelial cells [8].
  • Mutagenesis of this completely conserved residue in Escherichia coli AHAS isozyme II (Arg(276)) confirms that it is required for rapid and specific reaction of the second ketoacid [9].

Chemical compound and disease context of ILV2


Biological context of ILV2

  • FLP-FRT mediated intrachromosomal recombination on a tandemly duplicated YEp integrant at the ILV2 locus of chromosome XIII in Saccharomyces cerevisiae [11].
  • ILV2 upstream deletion analyses and high-copy transformation of the positive regulatory locus LEU3 ruled out the possibility of LEU3 protein binding palindromes mediating the branched chain amino acid dependent auxotrophy [12].
  • Nucleotide sequence of the yeast ILV2 gene which encodes acetolactate synthase [1].
  • 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 [1].
  • The coding sequence for the ILV2 polypeptide contains 2061 base pairs [1].

Anatomical context of ILV2

  • 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 [1].

Associations of ILV2 with chemical compounds

  • Chimaeric genes were constructed containing the 5' upstream and partial coding sequence of SMR1--a sulfometuron methyl resistant allele of the ILV2 locus [13].
  • The yeast ILV2 gene encodes acetolactate synthase, the first enzyme in the biosynthesis of isoleucine and valine [14].
  • Antisense RNA inhibition was enhanced in galactose medium containing sulfometuron methyl and in gcn4 cells deficient for positive regulation of the ILV2 locus [13].
  • Genetic modification of brewers' yeast to reduce diacetyl formation is being carried out by mutation of ILV2 [15].
  • ALS-specific activity in strains carrying the wild-type ILV2 allele exhibited strong feedback inhibition by valine and was sensitive to SM [16].

Regulatory relationships of ILV2

  • Reconstitution studies showed that the ilv6 protein stimulates the catalytic activity of the ilv2 protein by up to 7-fold (from 6.8 +/- 0.7 to 49.0 +/- 1.8 U/mg) and confers upon it sensitivity to inhibition by valine (Ki = 0.16 +/- 0.02 mM) [17].

Other interactions of ILV2

  • Thus in addition to general regulation of ILV2, GCN4 functions in basal level expression when the locus is subject to specific repression by pathway end product [12].
  • The mutations occur in three linkage groups, designated SMR1, smr2 and smr3 [18].
  • The strains, which originally lacked alpha-galactosidase activity (Mel-), had been transformed with a DNA fragment which possessed an ILV1-SMR1 allele of the ILV2 gene and a MEL1 gene [19].
  • Isogenic [cir (o)] and [cir+] diploids formed by crossing the [cir (o)] TD strain to complementary haploids were analyzed for plasmid marker loss and chromosomal DNA alterations in the presence and absence of selection pressure for the URA3 and SMR1 plasmid borne markers [11].

Analytical, diagnostic and therapeutic context of ILV2


  1. Nucleotide sequence of the yeast ILV2 gene which encodes acetolactate synthase. Falco, S.C., Dumas, K.S., Livak, K.J. Nucleic Acids Res. (1985) [Pubmed]
  2. Biosynthesis of 2-aceto-2-hydroxy acids: acetolactate synthases and acetohydroxyacid synthases. Chipman, D., Barak, Z., Schloss, J.V. Biochim. Biophys. Acta (1998) [Pubmed]
  3. Identification and sequence determination of the acetohydroxy acid isomeroreductase gene from Brevibacterium flavum MJ233. Inui, M., Vertès, A.A., Kobayashi, M., Kurusu, Y., Yukawa, H. DNA Seq. (1993) [Pubmed]
  4. Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein. Lyons, T.J., Liu, H., Goto, J.J., Nersissian, A., Roe, J.A., Graden, J.A., Café, C., Ellerby, L.M., Bredesen, D.E., Gralla, E.B., Valentine, J.S. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  5. sll1981, An acetolactate synthase homologue of Synechocystis sp. PCC6803, functions as L-myo-inositol 1-phosphate synthase. Chatterjee, A., Dastidar, K.G., Maitra, S., Das-Chatterjee, A., Dihazi, H., Eschrich, K., Majumder, A.L. Planta (2006) [Pubmed]
  6. Mutations in SOD1 associated with amyotrophic lateral sclerosis cause novel protein interactions. Kunst, C.B., Mezey, E., Brownstein, M.J., Patterson, D. Nat. Genet. (1997) [Pubmed]
  7. An enzyme in yeast mitochondria that catalyzes a step in branched-chain amino acid biosynthesis also functions in mitochondrial DNA stability. Zelenaya-Troitskaya, O., Perlman, P.S., Butow, R.A. EMBO J. (1995) [Pubmed]
  8. Sixty alleles of the ALS7 open reading frame in Candida albicans: ALS7 is a hypermutable contingency locus. Zhang, N., Harrex, A.L., Holland, B.R., Fenton, L.E., Cannon, R.D., Schmid, J. Genome Res. (2003) [Pubmed]
  9. Role of a conserved arginine in the mechanism of acetohydroxyacid synthase: catalysis of condensation with a specific ketoacid substrate. Engel, S., Vyazmensky, M., Vinogradov, M., Berkovich, D., Bar-Ilan, A., Qimron, U., Rosiansky, Y., Barak, Z., Chipman, D.M. J. Biol. Chem. (2004) [Pubmed]
  10. Purification and properties of Saccharomyces cerevisiae acetolactate synthase from recombinant Escherichia coli. Poulsen, C., Stougaard, P. Eur. J. Biochem. (1989) [Pubmed]
  11. FLP-FRT mediated intrachromosomal recombination on a tandemly duplicated YEp integrant at the ILV2 locus of chromosome XIII in Saccharomyces cerevisiae. Rank, G.H., Arndt, G.M., Xiao, W. Curr. Genet. (1989) [Pubmed]
  12. Branched chain amino acid regulation of the ILV2 locus in Saccharomyces cerevisiae. Xiao, W., Rank, G.H. Genome (1990) [Pubmed]
  13. Generation of an ilv bradytrophic phenocopy in yeast by antisense RNA. Xiao, W., Rank, G.H. Curr. Genet. (1988) [Pubmed]
  14. The yeast ILV2 gene is under general amino acid control. Xiao, W., Rank, G.H. Genome (1988) [Pubmed]
  15. Towards diacetyl-less brewers' yeast. Influence of ilv2 and ilv5 mutations. Gjermansen, C., Nilsson-Tillgren, T., Petersen, J.G., Kielland-Brandt, M.C., Sigsgaard, P., Holmberg, S. J. Basic Microbiol. (1988) [Pubmed]
  16. Effect of valine and the herbicide sulfometuron methyl on acetolactate synthase activity in nuclear and plasmid-borne sulphometuron methyl resistant Saccharomyces cerevisiae strains. Maiti, S.N., Zink, M.W., Rank, G.H. Can. J. Microbiol. (1988) [Pubmed]
  17. Expression, purification, characterization, and reconstitution of the large and small subunits of yeast acetohydroxyacid synthase. Pang, S.S., Duggleby, R.G. Biochemistry (1999) [Pubmed]
  18. Genetic analysis of mutants of Saccharomyces cerevisiae resistant to the herbicide sulfometuron methyl. Falco, S.C., Dumas, K.S. Genetics (1985) [Pubmed]
  19. Characterization of genetically transformed Saccharomyces cerevisiae baker's yeasts able to metabolize melibiose. Gasent-Ramírez, J.M., Codón, A.C., Benítez, T. Appl. Environ. Microbiol. (1995) [Pubmed]
  20. Molecular cloning of a novel allele of SMR1 which determines sulfometuron methyl resistance in Saccharomyces cerevisiae. Xie, Q., Jiménez, A. FEMS Microbiol. Lett. (1996) [Pubmed]
  21. Thiamin auxotrophy in yeast through altered cofactor dependence of the enzyme acetohydroxyacid synthase. Byrne, K.L., Meacock, P.A. Microbiology (Reading, Engl.) (2001) [Pubmed]
  22. High level activation of vitamin B1 biosynthesis genes in haustoria of the rust fungus Uromyces fabae. Sohn, J., Voegele, R.T., Mendgen, K., Hahn, M. Mol. Plant Microbe Interact. (2000) [Pubmed]
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