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

ELO2  -  fatty acid elongase ELO2

Saccharomyces cerevisiae S288c

Synonyms: 3-keto acyl-CoA synthase ELO2, Elongation of fatty acids protein 2, FEN1, Fenpropimorph resistance protein 1, GNS1, ...
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.

Disease relevance of FEN1


High impact information on FEN1


Biological context of FEN1

  • These phenotypes are exacerbated by the deletion of either the ELO2 or ELO3 gene, both of which have previously been shown to be required for VLCFA synthesis [6].
  • FEN1 removes the last primer ribonucleotide on the lagging strand and it cleaves a 5' flap that may result from strand displacement during replication or during base excision repair [7].
  • Furthermore, a mutant form of FEN1 lacking nuclease function exhibits dominant-negative effects on cell growth and genome instability similar to those seen with the homologous yeast rad27 mutation [7].
  • The fen1-1 mutation permits viability in aerobiosis of yeast disrupted for sterol-14 reductase in absence of exogenous ergosterol supplementation, whereas the corresponding strain bearing the wild type FEN1 allele grows only in anaerobiosis [8].
  • The predicted amino acid sequence of the open reading frame had only 29% identity with the yeast ELO2 sequence, contained a single histidine-rich domain and had six transmembrane-spanning regions, as suggested by hydropathy analysis [9].

Anatomical context of FEN1


Associations of FEN1 with chemical compounds

  • Strains with deletions of SYR3/ELO2 and ELO3 were resistant to syringomycin E, and lipid analyses of both mutants revealed shortened fatty acid chains and lower levels of sphingolipids [12].
  • Disruption of the sterol isomerase-encoding gene is lethal in cells growing in the absence of exogenous ergosterol, except in SR-resistant mutants lacking either the SUR4 or the FEN1 gene product [13].
  • The results suggest that sterol isomerase is the target of SR 31747 and that both the SUR4 and FEN1 gene products are required to mediate the proliferation arrest induced by ergosterol depletion [13].
  • Null mutations in ELO3 result in accumulation of labeled precursors into inositol phosphoceramide, with little labeling in the more complex mannosylated sphingolipids, whereas disruption of ELO2 results in reduced levels of all sphingolipids [14].
  • A sterol C-14 reductase (erg24-1) mutant of Saccharomyces cerevisiae was selected in a fen1, fen2, suppressor background on the basis of nystatin resistance and ignosterol (ergosta-8,14-dienol) production [15].

Physical interactions of FEN1

  • Tsc13p coimmunoprecipitates with Elo2p and Elo3p, suggesting that the elongating proteins are organized in a complex [6].

Other interactions of FEN1

  • YCR521, 522 and 524, have each been disrupted by insertion of a URA3 cassette and are non-essential genes [16].

Analytical, diagnostic and therapeutic context of FEN1

  • Gas chromatography and gas chromatography/mass spectroscopy analyses reveal that null mutations of ELO2 and ELO3 produce defects in the formation of very long chain fatty acids [14].
  • Among several sequences with limited identity with the S. cerevisiae ELO2 gene, a consensus cDNA sequence was identified from the LifeSeq(R) database of Incyte Pharmaceuticals, Inc. Human liver cDNA was amplified by PCR using oligonucleotides complementary to the 5' and 3' ends of the putative human cDNA sequence [9].
  • To assess the roles of the active site residues Glu160 and Asp181 of human FEN-1 nuclease in binding and catalysis of the flap DNA substrate and in vivo biological processes of DNA damage and repair, five different amino acids were replaced at each site through site-directed mutagenesis of the FEN-1 gene [17].


  1. Mutation of MSH3 in endometrial cancer and evidence for its functional role in heteroduplex repair. Risinger, J.I., Umar, A., Boyd, J., Berchuck, A., Kunkel, T.A., Barrett, J.C. Nat. Genet. (1996) [Pubmed]
  2. Mutations in DNA replication genes reduce yeast life span. Hoopes, L.L., Budd, M., Choe, W., Weitao, T., Campbell, J.L. Mol. Cell. Biol. (2002) [Pubmed]
  3. Role of a new mammalian gene family in the biosynthesis of very long chain fatty acids and sphingolipids. Tvrdik, P., Westerberg, R., Silve, S., Asadi, A., Jakobsson, A., Cannon, B., Loison, G., Jacobsson, A. J. Cell Biol. (2000) [Pubmed]
  4. Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast. David, D., Sundarababu, S., Gerst, J.E. J. Cell Biol. (1998) [Pubmed]
  5. Mutations in ABO1/ELO2, a subunit of holo-Elongator, increase abscisic acid sensitivity and drought tolerance in Arabidopsis thaliana. Chen, Z., Zhang, H., Jablonowski, D., Zhou, X., Ren, X., Hong, X., Schaffrath, R., Zhu, J.K., Gong, Z. Mol. Cell. Biol. (2006) [Pubmed]
  6. Tsc13p is required for fatty acid elongation and localizes to a novel structure at the nuclear-vacuolar interface in Saccharomyces cerevisiae. Kohlwein, S.D., Eder, S., Oh, C.S., Martin, C.E., Gable, K., Bacikova, D., Dunn, T. Mol. Cell. Biol. (2001) [Pubmed]
  7. Functional analysis of human FEN1 in Saccharomyces cerevisiae and its role in genome stability. Greene, A.L., Snipe, J.R., Gordenin, D.A., Resnick, M.A. Hum. Mol. Genet. (1999) [Pubmed]
  8. General resistance to sterol biosynthesis inhibitors in Saccharomyces cerevisiae. Ladevèze, V., Marcireau, C., Delourme, D., Karst, F. Lipids (1993) [Pubmed]
  9. Cloning of a human cDNA encoding a novel enzyme involved in the elongation of long-chain polyunsaturated fatty acids. Leonard, A.E., Bobik, E.G., Dorado, J., Kroeger, P.E., Chuang, L.T., Thurmond, J.M., Parker-Barnes, J.M., Das, T., Huang, Y.S., Mukerji, P. Biochem. J. (2000) [Pubmed]
  10. Novel function of Rad27 (FEN-1) in restricting short-sequence recombination. Negritto, M.C., Qiu, J., Ratay, D.O., Shen, B., Bailis, A.M. Mol. Cell. Biol. (2001) [Pubmed]
  11. Endonucleolytic cleavage of RNA at 5' endogenous stem structures by human flap endonuclease 1. Stevens, A. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  12. Syringomycin E inhibition of Saccharomyces cerevisiae: requirement for biosynthesis of sphingolipids with very-long-chain fatty acids and mannose- and phosphoinositol-containing head groups. Stock, S.D., Hama, H., Radding, J.A., Young, D.A., Takemoto, J.Y. Antimicrob. Agents Chemother. (2000) [Pubmed]
  13. The immunosuppressant SR 31747 blocks cell proliferation by inhibiting a steroid isomerase in Saccharomyces cerevisiae. Silve, S., Leplatois, P., Josse, A., Dupuy, P.H., Lanau, C., Kaghad, M., Dhers, C., Picard, C., Rahier, A., Taton, M., Le Fur, G., Caput, D., Ferrara, P., Loison, G. Mol. Cell. Biol. (1996) [Pubmed]
  14. ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation. Oh, C.S., Toke, D.A., Mandala, S., Martin, C.E. J. Biol. Chem. (1997) [Pubmed]
  15. Cloning, sequencing, and disruption of the gene encoding sterol C-14 reductase in Saccharomyces cerevisiae. Lorenz, R.T., Parks, L.W. DNA Cell Biol. (1992) [Pubmed]
  16. The complete sequence of the 8.2 kb segment left of MAT on chromosome III reveals five ORFs, including a gene for a yeast ribokinase. Thierry, A., Fairhead, C., Dujon, B. Yeast (1990) [Pubmed]
  17. Partial functional deficiency of E160D flap endonuclease-1 mutant in vitro and in vivo is due to defective cleavage of DNA substrates. Frank, G., Qiu, J., Somsouk, M., Weng, Y., Somsouk, L., Nolan, J.P., Shen, B. J. Biol. Chem. (1998) [Pubmed]
WikiGenes - Universities