The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

OPI3  -  bifunctional phosphatidyl-N...

Saccharomyces cerevisiae S288c

Synonyms: J1824, Overproducer of inositol protein 3, PEM2, PLMT, Phosphatidyl-N-methylethanolamine N-methyltransferase, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on OPI3


Biological context of OPI3


Anatomical context of OPI3


Associations of OPI3 with chemical compounds


Regulatory relationships of OPI3

  • When present in multiple copies the OPI3 gene efficiently suppresses the phospholipid methylation defect of a cho2 mutation [12].

Other interactions of OPI3

  • The mutant was identified by its disability to regulate expression of structural genes involved in phospholipid biosynthesis, INO1, CHO1 and OPI3, in response to supplementation with soluble lipid precursors [13].
  • The regulation of CHO2 mRNA and OPI3 mRNA abundance generally correlated with the activities of PEMT and PLMT, respectively [5].

Analytical, diagnostic and therapeutic context of OPI3


  1. Inositol regulates phosphatidylglycerolphosphate synthase expression in Saccharomyces cerevisiae. Greenberg, M.L., Hubbell, S., Lam, C. Mol. Cell. Biol. (1988) [Pubmed]
  2. Dimethyl sulfoxide exposure facilitates phospholipid biosynthesis and cellular membrane proliferation in yeast cells. Murata, Y., Watanabe, T., Sato, M., Momose, Y., Nakahara, T., Oka, S., Iwahashi, H. J. Biol. Chem. (2003) [Pubmed]
  3. Yeast phosphatidylethanolamine methylation pathway. Cloning and characterization of two distinct methyltransferase genes. Kodaki, T., Yamashita, S. J. Biol. Chem. (1987) [Pubmed]
  4. Lithium and valproate decrease the membrane phosphatidylinositol/phosphatidylcholine ratio. Ding, D., Greenberg, M.L. Mol. Microbiol. (2003) [Pubmed]
  5. Regulation of phosphatidylethanolamine methyltransferase and phospholipid methyltransferase by phospholipid precursors in Saccharomyces cerevisiae. Gaynor, P.M., Gill, T., Toutenhoofd, S., Summers, E.F., McGraw, P., Homann, M.J., Henry, S.A., Carman, G.M. Biochim. Biophys. Acta (1991) [Pubmed]
  6. Regulatory mutations of inositol biosynthesis in yeast: isolation of inositol-excreting mutants. Greenberg, M.L., Reiner, B., Henry, S.A. Genetics (1982) [Pubmed]
  7. Mutations in the Saccharomyces cerevisiae opi3 gene: effects on phospholipid methylation, growth and cross-pathway regulation of inositol synthesis. McGraw, P., Henry, S.A. Genetics (1989) [Pubmed]
  8. Identification of the upstream activation sequences responsible for the expression and regulation of the PEM1 and PEM2 genes encoding the enzymes of the phosphatidylethanolamine methylation pathway in Saccharomyces cerevisiae. Kodaki, T., Hosaka, K., Nikawa, J., Yamashita, S. J. Biochem. (1991) [Pubmed]
  9. Anomalously slow mobility of fluorescent lipid probes in the plasma membrane of the yeast Saccharomyces cerevisiae. Greenberg, M.L., Axelrod, D. J. Membr. Biol. (1993) [Pubmed]
  10. The yeast phospholipid N-methyltransferases catalyzing the synthesis of phosphatidylcholine preferentially convert di-C16:1 substrates both in vivo and in vitro. Boumann, H.A., Chin, P.T., Heck, A.J., De Kruijff, B., De Kroon, A.I. J. Biol. Chem. (2004) [Pubmed]
  11. Genomic analysis of the Opi- phenotype. Hancock, L.C., Behta, R.P., Lopes, J.M. Genetics (2006) [Pubmed]
  12. Molecular cloning of the yeast OPI3 gene as a high copy number suppressor of the cho2 mutation. Preitschopf, W., Lückl, H., Summers, E., Henry, S.A., Paltauf, F., Kohlwein, S.D. Curr. Genet. (1993) [Pubmed]
  13. Isolation and characterization of a mutant of Saccharomyces cerevisiae with pleiotropic deficiencies in transcriptional activation and repression. Lamping, E., Lückl, J., Paltauf, F., Henry, S.A., Kohlwein, S.D. Genetics (1994) [Pubmed]
  14. Characterization of the methyltransferases in the yeast phosphatidylethanolamine methylation pathway by selective gene disruption. Kodaki, T., Yamashita, S. Eur. J. Biochem. (1989) [Pubmed]
WikiGenes - Universities