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Gene Review

SCT1  -  bifunctional glycerol-3...

Saccharomyces cerevisiae S288c

Synonyms: DHAP-AT 1, Dihydroxyacetone phosphate acyltransferase 1, G-3-P acyltransferase 1, GAT2, GPT1, ...
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Disease relevance of SCT1


High impact information on SCT1

  • We find that the G1-specific transcription factor p65cdc10-p72res1/sct1 which controls the expression of S-phase genes is fully activated in pheromone, unlike the analogous control in budding yeast [2].
  • Mutant SCT1 cells expressed DNA topoisomerase I protein of similar specific activity and camptothecin sensitivity to that of congenic, drug-sensitive sct1 cells, yet were resistant to camptothecin-mediated lethality [1].
  • SCT1 cell sensitivity to other DNA-damaging agents suggests that alterations in SCT1 function suppress camptothecin-induced DNA damage produced in the presence of yeast DNA topoisomerase I [1].
  • Moreover, camptothecin-treated SCT1 cells did not exhibit the G2-arrested, terminal phenotype characteristic of drug-treated wild-type cells [1].
  • To address why we observed alterations in phospholipid turnover specific to phosphatidylcholine produced through the CDP-choline pathway in gat1 and gat2 yeast we tested their sensitivity to various cytotoxic lysolipids and observed that gat2 cells were more sensitive to lysophosphatidylcholine, but not other lysolipids [3].

Biological context of SCT1


Associations of SCT1 with chemical compounds


Regulatory relationships of SCT1


Other interactions of SCT1

  • Yeast SCT1 mutants were isolated in a screen for mutations in genes other than TOP1 that result in camptothecin resistance [5].


  1. SCT1 mutants suppress the camptothecin sensitivity of yeast cells expressing wild-type DNA topoisomerase I. Kauh, E.A., Bjornsti, M.A. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  2. Fission yeast pheromone blocks S-phase by inhibiting the G1 cyclin B-p34cdc2 kinase. Stern, B., Nurse, P. EMBO J. (1997) [Pubmed]
  3. Differential partitioning of lipids metabolized by separate yeast glycerol-3-phosphate acyltransferases reveals that phospholipase D generation of phosphatidic acid mediates sensitivity to choline-containing lysolipids and drugs. Zaremberg, V., McMaster, C.R. J. Biol. Chem. (2002) [Pubmed]
  4. The initial step of the glycerolipid pathway: identification of glycerol 3-phosphate/dihydroxyacetone phosphate dual substrate acyltransferases in Saccharomyces cerevisiae. Zheng, Z., Zou, J. J. Biol. Chem. (2001) [Pubmed]
  5. Camptothecin sensitivity is mediated by the pleiotropic drug resistance network in yeast. Reid, R.J., Kauh, E.A., Bjornsti, M.A. J. Biol. Chem. (1997) [Pubmed]
  6. Isolation and characterization of a SCT1 gene which can suppress a choline-transport mutant of Saccharomyces cerevisiae. Matsushita, M., Nikawa, J. J. Biochem. (1995) [Pubmed]
  7. Mutants of Saccharomyces cerevisiae defective in sn-glycerol-3-phosphate acyltransferase. Simultaneous loss of dihydroxyacetone phosphate acyltransferase indicates a common gene. Tillman, T.S., Bell, R.M. J. Biol. Chem. (1986) [Pubmed]
  8. Regulation of phosphatidic acid biosynthetic enzymes in Saccharomyces cerevisiae. Minskoff, S.A., Racenis, P.V., Granger, J., Larkins, L., Hajra, A.K., Greenberg, M.L. J. Lipid Res. (1994) [Pubmed]
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