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Gene Review

LYS2  -  L-aminoadipate-semialdehyde dehydrogenase

Saccharomyces cerevisiae S288c

Synonyms: Alpha-AR, Alpha-aminoadipate reductase, YBR0910, YBR115C
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Disease relevance of LYS2

  • Unlike the Lys2p from S. cerevisiae and C. albicans, the Sz. pombe Lys1p was active when expressed in E. coli and exhibited significant AAR activity without the addition of CoA or the Sz. pombe Lys7p intron free PPTase [1].

High impact information on LYS2

  • An act3 mutation also affects expression of the HIS4 and LYS2 genes; thus, Act3p is not a delta element-specific transcriptional regulator [2].
  • Silencing by Sir protein targeting can also be initiated at a telomere-proximal site (ADH4), but is much weaker at an internal chromosomal locus (LYS2) [3].
  • Finally, we tested integrations of CEN DNA into the genome and found a toleration of wild-type CEN6 DNA when present 3' of the LYS2 gene [4].
  • TEF1 maps on chromosome II close to LYS2 [5].
  • Similar results were observed when the accumulation of mutations at frameshift hot spots in the LYS2 gene was analyzed, although mutation of MLH3 did not cause the same extent of affect at every LYS2 frameshift hot spot [6].

Biological context of LYS2

  • The sin4 delta mutant also shows phenotypes common to histone and spt mutants, including suppression of delta insertion mutations in the HIS4 and LYS2 promoters, expression of promoters lacking upstream activation sequence elements, and decreased superhelical density of circular DNA molecules [7].
  • We have cloned the CIF1 gene by complementation of function and located it in a 2.75 kb SphI-BstEII fragment situated at ca. 18 kb centromere distal of LYS2 and ca. 80 kb centromere proximal of TYR1 on chromosome II [8].
  • An open reading frame of 2370 bp was localized between SSN6 and LYS2, which has recently been identified (Schild et al., 1991) to be the RAD16 gene [9].
  • A 3.9 kb internal pSC5 fragment hybridized only to the plasmid pSC5, but no homology was observed with LYS2 DNA or the YEp24 vector [10].
  • The Sz. pombe Lys1p amino acid sequence showed a high degree of similarity to other fungal Lys2p proteins; however, the Lys7p amino acid sequence showed much less similarity to other bacterial, fungal and animal PPTases representing several phylogenetic groups [1].

Anatomical context of LYS2

  • Although the modified tRNA Lys2 was recognized by elongation factor (EF) T, the EFT dependent binding to ribosomes to tRNA Lys2 (CNBr) was markedly decreased [11].

Associations of LYS2 with chemical compounds


Regulatory relationships of LYS2

  • The alpha-aminoadipate reductase activity was repressed in lysine-grown wild-type and Lys5+ transformed cells but not in Lys2+ transformed cells [10].
  • Rev7 mutants are markedly deficient with respect to UV-induced reversion of lys2, are slightly sensitive to UV and appear to be in the RAD6 epistasis group for UV survival [16].

Other interactions of LYS2

  • Furthermore, spt6 and ssn20 mutations fail to complement each other, and ssn20 mutations suppress solo delta insertion mutations at HIS4 and LYS2 [17].
  • Mutations in the SPT5 gene of Saccharomyces cerevisiae were isolated previously as suppressors of delta insertion mutations at HIS4 and LYS2 [18].
  • Results from the revertant analysis and in vitro complementation indicated LYS2 and LYS5 as structural genes, each encoding a subunit of this large enzyme [19].
  • Levels of these enzymes in lys2, lys14, and lys15 mutants were the same or lower than those in wild-type cells [14].
  • The gene ALG1 has been mapped on chromosome II at a distance of 2.1 map units from LYS2 [20].

Analytical, diagnostic and therapeutic context of LYS2


  1. Posttranslational activation, site-directed mutation and phylogenetic analyses of the lysine biosynthesis enzymes alpha-aminoadipate reductase Lys1p (AAR) and the phosphopantetheinyl transferase Lys7p (PPTase) from Schizosaccharomyces pombe. Guo, S., Bhattacharjee, J.K. Yeast (2004) [Pubmed]
  2. Epigenetic effects on yeast transcription caused by mutations in an actin-related protein present in the nucleus. Jiang, Y.W., Stillman, D.J. Genes Dev. (1996) [Pubmed]
  3. Silencing of genes at nontelomeric sites in yeast is controlled by sequestration of silencing factors at telomeres by Rap 1 protein. Marcand, S., Buck, S.W., Moretti, P., Gilson, E., Shore, D. Genes Dev. (1996) [Pubmed]
  4. Role of conserved sequence elements in yeast centromere DNA. Panzeri, L., Landonio, L., Stotz, A., Philippsen, P. EMBO J. (1985) [Pubmed]
  5. Identification of two genes coding for the translation elongation factor EF-1 alpha of S. cerevisiae. Schirmaier, F., Philippsen, P. EMBO J. (1984) [Pubmed]
  6. The Saccharomyces cerevisiae MLH3 gene functions in MSH3-dependent suppression of frameshift mutations. Flores-Rozas, H., Kolodner, R.D. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  7. Involvement of the SIN4 global transcriptional regulator in the chromatin structure of Saccharomyces cerevisiae. Jiang, Y.W., Stillman, D.J. Mol. Cell. Biol. (1992) [Pubmed]
  8. Molecular cloning of CIF1, a yeast gene necessary for growth on glucose. González, M.I., Stucka, R., Blázquez, M.A., Feldmann, H., Gancedo, C. Yeast (1992) [Pubmed]
  9. Molecular analysis of yeast chromosome II between CMD1 and LYS2: the excision repair gene RAD16 located in this region belongs to a novel group of double-finger proteins. Mannhaupt, G., Stucka, R., Ehnle, S., Vetter, I., Feldmann, H. Yeast (1992) [Pubmed]
  10. Cloning and biochemical characterization of LYS5 gene of Saccharomyces cerevisiae. Borell, C.W., Bhattacharjee, J.K. Curr. Genet. (1988) [Pubmed]
  11. Role of modified nucleosides in tRNA: effect of modification of the 2-thiouridine derivative located at the 5'-end of the anticodon of yeast transfer RNA Lys2. Sen, G.C., Ghosh, H.P. Nucleic Acids Res. (1976) [Pubmed]
  12. Cloning and sequence of the LYS2 homologue gene from the osmotolerant yeast Pichia sorbitophila. Bleykasten-Grosshans, C., Prior, C., Potier, S. Yeast (2001) [Pubmed]
  13. Molecular analysis of the LYS2 gene of Candida albicans: homology to peptide antibiotic synthetases and the regulation of the alpha-aminoadipate reductase. Suvarna, K., Seah, L., Bhattacherjee, V., Bhattacharjee, J.K. Curr. Genet. (1998) [Pubmed]
  14. Biosynthetic and regulatory role of lys9 mutants of Saccharomyces cerevisiae. Winston, M.K., Bhattacharjee, J.K. Curr. Genet. (1987) [Pubmed]
  15. Novel posttranslational activation of the LYS2-encoded alpha-aminoadipate reductase for biosynthesis of lysine and site-directed mutational analysis of conserved amino acid residues in the activation domain of Candida albicans. Guo, S., Evans, S.A., Wilkes, M.B., Bhattacharjee, J.K. J. Bacteriol. (2001) [Pubmed]
  16. REV7, a new gene concerned with UV mutagenesis in yeast. Lawrence, C.W., Das, G., Christensen, R.B. Mol. Gen. Genet. (1985) [Pubmed]
  17. The SPT6 gene is essential for growth and is required for delta-mediated transcription in Saccharomyces cerevisiae. Clark-Adams, C.D., Winston, F. Mol. Cell. Biol. (1987) [Pubmed]
  18. SPT5, an essential gene important for normal transcription in Saccharomyces cerevisiae, encodes an acidic nuclear protein with a carboxy-terminal repeat. Swanson, M.S., Malone, E.A., Winston, F. Mol. Cell. Biol. (1991) [Pubmed]
  19. Properties of revertants of lys2 and lys5 mutants as well as alpha-aminoadipate-semialdehyde dehydrogenase from Saccharomyces cerevisiae. Storts, D.R., Bhattacharjee, J.K. Biochem. Biophys. Res. Commun. (1989) [Pubmed]
  20. Cloning and expression in Escherichia coli of a yeast mannosyltransferase from the asparagine-linked glycosylation pathway. Couto, J.R., Huffaker, T.C., Robbins, P.W. J. Biol. Chem. (1984) [Pubmed]
  21. Site-directed mutational analysis of the novel catalytic domains of alpha-aminoadipate reductase (Lys2p) from Candida albicans. Guo, S., Bhattacharjee, J.K. Mol. Genet. Genomics (2003) [Pubmed]
  22. Identification of the cloned S. cerevisiae LYS2 gene by an integrative transformation approach. Eibel, H., Philippsen, P. Mol. Gen. Genet. (1983) [Pubmed]
  23. Nitrate regulation of alpha-aminoadipate reductase formation and lysine inhibition of its activity in Penicillium chrysogenum and Acremonium chrysogenum. Hijarrubia, M.J., Aparicio, J.F., Martín, J.F. Appl. Microbiol. Biotechnol. (2002) [Pubmed]
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