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Gene Review

ACC1  -  acetyl-CoA carboxylase ACC1

Saccharomyces cerevisiae S288c

Synonyms: ABP2, ACC, Acetyl-CoA carboxylase, FAS3, Fatty acid synthetase 3, ...
 
 
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Disease relevance of ACC1

  • In the first group, as represented by acetyl CoA-carboxylase of Achromobacter, the active enzyme could be resolved in three types of functional components: (1) the biotin-carboxyl carrier protein, (2) the biotin carboxylase, and (3) the carboxyl transferase [1].
 

High impact information on ACC1

  • Aberrant mitosis in fission yeast mutants defective in fatty acid synthetase and acetyl CoA carboxylase [2].
  • We have determined the crystal structures at up to 2.5-A resolution of the CT domain of yeast ACC in complex with the herbicide haloxyfop or diclofop [3].
  • The carboxyltransferase (CT) domain of ACC is the site of action of commercial herbicides, such as haloxyfop, diclofop, and sethoxydim [3].
  • Shifting the acc1(ts) cells to 24 degrees C after 2 h of incubation at 37 degrees C resulted in reactivation of the ACC and elevation of the ceramides and very long-chain fatty acid syntheses with normal cell-cycle progression [4].
  • A Saccharomyces cerevisiae mutant strain defective in acetyl-CoA carboxylase arrests at the G2/M phase of the cell cycle [4].
 

Biological context of ACC1

  • Whereas ACC1 is involved in cytoplasmic fatty acid synthesis, the phenotype of hfa1Delta disruptants resembles that of mitochondrial fatty-acid synthase mutants [5].
  • Disruption of one ACC1 allele in a diploid wild-type strain resulted in 50% reduction of ACC1-specific mRNA and acetyl-CoA carboxylase specific activity and a marked decrease of biotin associated with a 250-kDa protein, compared to wild-type [6].
  • Correspondingly, ACC biotinylation is severely reduced though not completely absent in the two bpl1 mutants studied in this work [7].
  • An aryloxyphenoxypropionate and two cyclohexanediones do not inhibit growth of haploid yeast strains containing the yeast ACC1 gene, but one cyclohexanedione inhibits growth of the gene-replacement strains at concentrations below 0.2 mM [8].
  • The ACC1/FAS3 gene has been mapped to the right arm of chromosome XIV by both genetic and physical methods [9].
 

Anatomical context of ACC1

 

Associations of ACC1 with chemical compounds

  • The 5'-untranslated region of the ACC1 gene contains a sequence reminiscent of an inositol/choline-responsive element identified in genes encoding phospholipid biosynthetic enzymes [6].
  • Since lipoic acid levels of ACC1 and BPL1 mutants are essentially normal, an unknown product of mitochondrial fatty acid synthesis appears to be critically reduced in malonyl-CoA-deficient yeast cells [7].
  • It is concluded that the lethality of BPL1 deletants is due to the lack of malonyl-CoA-dependent VLCFA synthesis and that the viability of distinct ACC-defective point mutants is due to their maintenance of a critical level of malonyl-CoA and, hence, VLCFA production [7].
  • In addition to ACC pyruvate carboxylase and an additional biotin-containing protein of unknown function fail to be biotinylated in BPL1-defective yeast mutants [7].
  • Taken together these data strongly suggest that the ACC1 gene product is the primary target for soraphen A in vivo [14].
 

Enzymatic interactions of ACC1

 

Regulatory relationships of ACC1

 

Other interactions of ACC1

  • Nevertheless, HFA1 and ACC1 functions are not overlapping because mutants of the two genes have different phenotypes and do not complement each other [5].
  • The overexpression of FAS1 considerably stimulated MCFA formation while that of ASC2, ACC1 and FAS2 genes was not effective [17].
  • Spores harboring an ACC1 deletion derived from a diploid Saccharomyces cerevisiae strain, in which one copy of the entire ACC1 gene is replaced with a LEU2 cassette, fail to grow [8].
  • In Saccharomyces cerevisiae, FAS1, FAS2, and FAS3 are the genes involved in saturated fatty acid biosynthesis [18].
  • The gene is closely linked to RNA2 and is allelic to the ABP2 gene of chromosome XIV [9].
 

Analytical, diagnostic and therapeutic context of ACC1

References

  1. New experiments of biotin enzymes. Lynen, F. CRC Crit. Rev. Biochem. (1979) [Pubmed]
  2. Aberrant mitosis in fission yeast mutants defective in fatty acid synthetase and acetyl CoA carboxylase. Saitoh, S., Takahashi, K., Nabeshima, K., Yamashita, Y., Nakaseko, Y., Hirata, A., Yanagida, M. J. Cell Biol. (1996) [Pubmed]
  3. Molecular basis for the inhibition of the carboxyltransferase domain of acetyl-coenzyme-A carboxylase by haloxyfop and diclofop. Zhang, H., Tweel, B., Tong, L. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  4. A Saccharomyces cerevisiae mutant strain defective in acetyl-CoA carboxylase arrests at the G2/M phase of the cell cycle. Al-Feel, W., DeMar, J.C., Wakil, S.J. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  5. HFA1 encoding an organelle-specific acetyl-CoA carboxylase controls mitochondrial fatty acid synthesis in Saccharomyces cerevisiae. Hoja, U., Marthol, S., Hofmann, J., Stegner, S., Schulz, R., Meier, S., Greiner, E., Schweizer, E. J. Biol. Chem. (2004) [Pubmed]
  6. Acetyl-CoA carboxylase from yeast is an essential enzyme and is regulated by factors that control phospholipid metabolism. Hasslacher, M., Ivessa, A.S., Paltauf, F., Kohlwein, S.D. J. Biol. Chem. (1993) [Pubmed]
  7. Pleiotropic phenotype of acetyl-CoA-carboxylase-defective yeast cells--viability of a BPL1-amber mutation depending on its readthrough by normal tRNA(Gln)(CAG). Hoja, U., Wellein, C., Greiner, E., Schweizer, E. Eur. J. Biochem. (1998) [Pubmed]
  8. Wheat cytosolic acetyl-CoA carboxylase complements an ACC1 null mutation in yeast. Joachimiak, M., Tevzadze, G., Podkowinski, J., Haselkorn, R., Gornicki, P. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  9. Mapping of the ACC1/FAS3 gene to the right arm of chromosome XIV of Saccharomyces cerevisiae. Guerra, C.E., Klein, H.L. Yeast (1995) [Pubmed]
  10. A novel cold-sensitive allele of the rate-limiting enzyme of fatty acid synthesis, acetyl coenzyme A carboxylase, affects the morphology of the yeast vacuole through acylation of Vac8p. Schneiter, R., Guerra, C.E., Lampl, M., Tatzer, V., Zellnig, G., Klein, H.L., Kohlwein, S.D. Mol. Cell. Biol. (2000) [Pubmed]
  11. Herbicide sensitivity determinant of wheat plastid acetyl-CoA carboxylase is located in a 400-amino acid fragment of the carboxyltransferase domain. Nikolskaya, T., Zagnitko, O., Tevzadze, G., Haselkorn, R., Gornicki, P. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  12. Yeast acetyl-CoA carboxylase is associated with the cytoplasmic surface of the endoplasmic reticulum. Ivessa, A.S., Schneiter, R., Kohlwein, S.D. Eur. J. Cell Biol. (1997) [Pubmed]
  13. Identification and biophysical characterization of a very-long-chain-fatty-acid-substituted phosphatidylinositol in yeast subcellular membranes. Schneiter, R., Brügger, B., Amann, C.M., Prestwich, G.D., Epand, R.F., Zellnig, G., Wieland, F.T., Epand, R.M. Biochem. J. (2004) [Pubmed]
  14. Identification of the yeast ACC1 gene product (acetyl-CoA carboxylase) as the target of the polyketide fungicide soraphen A. Vahlensieck, H.F., Pridzun, L., Reichenbach, H., Hinnen, A. Curr. Genet. (1994) [Pubmed]
  15. Mammalian AMP-activated protein kinase shares structural and functional homology with the catalytic domain of yeast Snf1 protein kinase. Mitchelhill, K.I., Stapleton, D., Gao, G., House, C., Michell, B., Katsis, F., Witters, L.A., Kemp, B.E. J. Biol. Chem. (1994) [Pubmed]
  16. Yeast SNF1 is functionally related to mammalian AMP-activated protein kinase and regulates acetyl-CoA carboxylase in vivo. Woods, A., Munday, M.R., Scott, J., Yang, X., Carlson, M., Carling, D. J. Biol. Chem. (1994) [Pubmed]
  17. Increased ethyl caproate production by inositol limitation in Saccharomyces cerevisiae. Furukawa, K., Yamada, T., Mizoguchi, H., Hara, S. J. Biosci. Bioeng. (2003) [Pubmed]
  18. Coordinated regulation and inositol-mediated and fatty acid-mediated repression of fatty acid synthase genes in Saccharomyces cerevisiae. Chirala, S.S. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  19. Arabidopsis ETO1 specifically interacts with and negatively regulates type 2 1-aminocyclopropane-1-carboxylate synthases. Yoshida, H., Nagata, M., Saito, K., Wang, K.L., Ecker, J.R. BMC Plant Biol. (2005) [Pubmed]
  20. Molecular cloning, characterization, and elicitation of acetyl-CoA carboxylase from alfalfa. Shorrosh, B.S., Dixon, R.A., Ohlrogge, J.B. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  21. Wheat acetyl-coenzyme A carboxylase: cDNA and protein structure. Gornicki, P., Podkowinski, J., Scappino, L.A., DiMaio, J., Ward, E., Haselkorn, R. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
 
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