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Gene Review

CCS1  -  Ccs1p

Saccharomyces cerevisiae S288c

Synonyms: LYS7, Superoxide dismutase 1 copper chaperone, YM9532.03C, YMR038C
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High impact information on CCS1


Biological context of CCS1


Associations of CCS1 with chemical compounds

  • Saccharomyces cerevisiae Lys7p was proposed to be the enzyme catalyzing the dehydratation of homocitrate to cis-homoaconitate, the second step of the lysine biosynthetic pathway [5].
  • Cells deleted for the LYS7 gene displayed, in addition to lysine auxotrophy, methionine auxotrophy, sensitivity to superoxide generating drugs and light irradiation, and diminution of calcineurin activity [5].
  • Somewhat higher AAR activity was obtained with the addition of CoA and the Sz. pombe Lys7p PPTase [9].
  • In the linear analogs, replacement of both Lys7 and Gln10 with a cysteine residue resulted in an over 100-fold loss of the biological activity when compared with the native pheromone [10].
  • Analogs of the Saccharomyces cerevisiae alpha-mating factor, Trp-His-Trp-Leu-Gln-Leu-Lys-Pro-Gly-Gln-Pro-Met-Tyr, where Lys7 and Gln10 were replaced with Cys, Cys(CH3), or Ser, were synthesized using solid-phase procedures on a phenylacetamidomethyl resin [10].

Other interactions of CCS1


Analytical, diagnostic and therapeutic context of CCS1

  • X-ray crystallographic and analytical ultracentrifugation analyses of truncated and full-length yeast copper chaperones for SOD (LYS7): a dimer-dimer model of LYS7-SOD association and copper delivery [14].
  • The data presented here, however, taken together with previously published crystallographic and analytical gel filtration data on full-length LYS7, suggest an alternative model wherein a dimer of LYS7 interacts with a dimer of yeast CuZnSOD [14].
  • A Northern blot experiment demonstrated that LYS7 transcription was not regulated by lysine-specific or general aa control mechanisms [8].


  1. Loss of SOD1 and LYS7 sensitizes Saccharomyces cerevisiae to hydroxyurea and DNA damage agents and downregulates MEC1 pathway effectors. Carter, C.D., Kitchen, L.E., Au, W.C., Babic, C.M., Basrai, M.A. Mol. Cell. Biol. (2005) [Pubmed]
  2. Loss of in vitro metal ion binding specificity in mutant copper-zinc superoxide dismutases associated with familial amyotrophic lateral sclerosis. Goto, J.J., Zhu, H., Sanchez, R.J., Nersissian, A., Gralla, E.B., Valentine, J.S., Cabelli, D.E. J. Biol. Chem. (2000) [Pubmed]
  3. Saccharomyces cerevisiae protein involved in plasmid maintenance is necessary for mating of MAT alpha cells. Passmore, S., Maine, G.T., Elble, R., Christ, C., Tye, B.K. J. Mol. Biol. (1988) [Pubmed]
  4. Cloning by gene amplification of two loci conferring multiple drug resistance in Saccharomyces. Leppert, G., McDevitt, R., Falco, S.C., Van Dyk, T.K., Ficke, M.B., Golin, J. Genetics (1990) [Pubmed]
  5. The Saccharomyces cerevisiae LYS7 gene is involved in oxidative stress protection. Gamonet, F., Lauquin, G.J. Eur. J. Biochem. (1998) [Pubmed]
  6. Localization of the FAR3 gene: genetic mapping and molecular cloning using a chromosome walk-'n'-roll strategy. Horecka, J. Yeast (1995) [Pubmed]
  7. Functional characterization of 4'-phosphopantetheinyl transferase genes of bacterial and fungal origin by complementation of Saccharomyces cerevisiae lys5. Mootz, H.D., Schörgendorfer, K., Marahiel, M.A. FEMS Microbiol. Lett. (2002) [Pubmed]
  8. Cloning and characterization of the Saccharomyces cerevisiae LYS7 gene: evidence for function outside of lysine biosynthesis. Horecka, J., Kinsey, P.T., Sprague, G.F. Gene (1995) [Pubmed]
  9. 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]
  10. Probing the functional conformation of the tridecapeptide mating pheromone of Saccharomyces cerevisiae through study of disulfide-constrained analogs. Xue, C.B., McKinney, A., Lu, H.F., Jiang, Y., Becker, J.M., Naider, F. Int. J. Pept. Protein Res. (1996) [Pubmed]
  11. Overexpressed Sod1p acts either to reduce or to increase the lifespans and stress resistance of yeast, depending on whether it is Cu(2+)-deficient or an active Cu,Zn-superoxide dismutase. Harris, N., Bachler, M., Costa, V., Mollapour, M., Moradas-Ferreira, P., Piper, P.W. Aging Cell (2005) [Pubmed]
  12. Intracellular pathways of copper trafficking in yeast and humans. Culotta, V.C., Lin, S.J., Schmidt, P., Klomp, L.W., Casareno, R.L., Gitlin, J. Adv. Exp. Med. Biol. (1999) [Pubmed]
  13. Conversion of pipecolic acid into lysine in Penicillium chrysogenum requires pipecolate oxidase and saccharopine reductase: characterization of the lys7 gene encoding saccharopine reductase. Naranjo, L., Martin de Valmaseda, E., Bañuelos, O., Lopez, P., Riaño, J., Casqueiro, J., Martin, J.F. J. Bacteriol. (2001) [Pubmed]
  14. X-ray crystallographic and analytical ultracentrifugation analyses of truncated and full-length yeast copper chaperones for SOD (LYS7): a dimer-dimer model of LYS7-SOD association and copper delivery. Hall, L.T., Sanchez, R.J., Holloway, S.P., Zhu, H., Stine, J.E., Lyons, T.J., Demeler, B., Schirf, V., Hansen, J.C., Nersissian, A.M., Valentine, J.S., Hart, P.J. Biochemistry (2000) [Pubmed]
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