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

POX1  -  acyl-CoA oxidase

Saccharomyces cerevisiae S288c

Synonyms: Acyl-CoA oxidase, Acyl-coenzyme A oxidase, FOX1, YGL205W
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 POX1

  • The down-regulating effect of anoxia on the expression of CTA1 and POX1 is even stronger than the effect of haem deficiency and is not reversed by the addition of exogenous haem or the presence of endogenous haem [1].
  • One of the acyl-CoA oxidases from the yeast Yarrowia lipolytica, acyl-CoA oxidase 2 (Aox2p), has been expressed in Escherichia coli as an active, N-terminally tagged (His)(6) fusion protein [2].

High impact information on POX1

  • A significant redistribution of Aox occurs only in mature peroxisomes [3].
  • Peroxisomal targeting of the Aox complex is abolished in a mutant lacking the peroxin Pex5p, a component of the matrix protein targeting machinery [4].
  • Aox2p and Aox3p play a pivotal role in the formation of the Aox complex in the cytosol and can substitute for one another in promoting assembly of the complex [4].
  • Peb1 is a peroxisome biogenesis mutant isolated in Saccharomyces cerevisiae that is selectively defective in the import of thiolase into peroxisomes but has a normal ability to package catalase, luciferase and acyl-CoA oxidase (Zhang, J. W., C. Luckey, and P. B. Lazarow. 1993. Mol. Biol. Cell. 4:1351-1359) [5].
  • Cell-free mRNA translation and RNA dot-blot hybridization analyses demonstrated that, whereas glucose-grown C. tropicalis contained little or no acyl-CoA oxidase mRNA, alkane-grown cells contained so much of this mRNA as to make acyl-CoA oxidase one of the major in vitro translation products [6].

Biological context of POX1

  • The POX1 promoter was shown to contain a canonical Adr1p element (UAS1), within which the oleate response element (ORE) was nested [7].
  • Northern analysis demonstrated that transcriptional up-regulation of both POX1 and PEX11 was abolished in adr1 Delta mutant cells, and immunoblotting confirmed that the abundance of their gene products was dramatically reduced [7].
  • Previously, we characterized regulatory elements in the promoter region of POX1 that are involved in the repression and activation of this gene (Wang, T., Luo, Y., and Small, G. M. (1994) J. Biol. Chem. 269, 24480-24485) [8].
  • Transcription of POX1, the gene encoding peroxisomal acyl-CoA oxidase in the yeast Saccharomyces cerevisiae, is controlled by the carbon source given for cell growth [9].
  • Elimination of this DNA sequence results in constitutive expression of POX1 when S. cerevisiae is grown on a fermentable carbon source or glycerol [10].

Anatomical context of POX1

  • Saccharomyces cerevisiae Adr1p governs fatty acid beta-oxidation and peroxisome proliferation by regulating POX1 and PEX11 [7].
  • To elucidate the molecular mechanism governing fatty acid transport across the cell membrane, we first isolated a Saccharomyces cerevisiae mutant, B-1, that exhibits a reduced acyl-CoA oxidase activity and an increase in free fatty acid accumulation [11].
  • We have synthesized a 125I-peptide with the sequence of the last 12 amino acids of acyl-CoA oxidase, D-Tyr-HKHLKPLQSKL (SKLp), and used it to detect a receptor that recognizes SKL containing proteins targeted to glyoxysomes [12].
  • However, there are also two sites on alkali-stripped glyoxysomal membranes from castor bean (Ricinus communis) endosperm that bind the peptide YHKHLKPLQSKL (SKLp), the sequence of the last 12 amino acids of acyl-coenzyme A oxidase (N.E. Wollins, R.P. Donaldson [1994] J Biol Chem 289: 1149-1153) [13].
  • Under these conditions, catalase, acyl-coenzyme A oxidase, and malate synthase cofractionated at equilibrium close to the mitochondrial peak, indicating smaller, less dense organelles than those from cells grown on oleic acid [14].

Associations of POX1 with chemical compounds


Physical interactions of POX1

  • Here we demonstrate that peroxisomal import of Pox1p is nevertheless dependent on binding to Pex5p, the PTS1 import receptor [19].

Regulatory relationships of POX1


Other interactions of POX1

  • Respiratory incompetence has no effect on the expression of CTA1 and POX1, whereas in the absence of haem their expression is markedly decreased [1].
  • We recently identified and isolated a transcription factor, Oaf1p, that binds to the UAS1 of POX1 and mediates its induction [15].
  • Here we demonstrate, using different techniques, that in Saccharomyces cerevisiae Pex5p-N alone facilitates the import of the major matrix protein Fox1p [21].
  • Synthesis of polyhydroxyalkanoate was dependent on the beta-oxidation enzymes acyl-CoA oxidase and enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase multifunctional protein, which are involved in generating 3-hydroxyacyl-CoAs, and on the peroxin PEX5, which is involved in the import of proteins into the peroxisome [22].
  • Mutants with no acyl-CoA oxidase activity could not reconsume gamma-decalactone, and mutants with a disruption of pox3, which encodes the short-chain acyl-CoA oxidase, reconsumed it more slowly [16].

Analytical, diagnostic and therapeutic context of POX1


  1. Oxygen and haem regulate the synthesis of peroxisomal proteins: catalase A, acyl-CoA oxidase and Pex1p in the yeast Saccharomyces cerevisiae; the regulation of these proteins by oxygen is not mediated by haem. Skoneczny, M., Rytka, J. Biochem. J. (2000) [Pubmed]
  2. The acyl-CoA oxidases from the yeast Yarrowia lipolytica: characterization of Aox2p. Luo, Y.S., Nicaud, J.M., Van Veldhoven, P.P., Chardot, T. Arch. Biochem. Biophys. (2002) [Pubmed]
  3. Peroxisome division in the yeast Yarrowia lipolytica is regulated by a signal from inside the peroxisome. Guo, T., Kit, Y.Y., Nicaud, J.M., Le Dall, M.T., Sears, S.K., Vali, H., Chan, H., Rachubinski, R.A., Titorenko, V.I. J. Cell Biol. (2003) [Pubmed]
  4. Acyl-CoA oxidase is imported as a heteropentameric, cofactor-containing complex into peroxisomes of Yarrowia lipolytica. Titorenko, V.I., Nicaud, J.M., Wang, H., Chan, H., Rachubinski, R.A. J. Cell Biol. (2002) [Pubmed]
  5. Peb1p (Pas7p) is an intraperoxisomal receptor for the NH2-terminal, type 2, peroxisomal targeting sequence of thiolase: Peb1p itself is targeted to peroxisomes by an NH2-terminal peptide. Zhang, J.W., Lazarow, P.B. J. Cell Biol. (1996) [Pubmed]
  6. Cloning of cDNA coding for peroxisomal acyl-CoA oxidase from the yeast Candida tropicalis pK233. Rachubinski, R.A., Fujiki, Y., Lazarow, P.B. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  7. Saccharomyces cerevisiae Adr1p governs fatty acid beta-oxidation and peroxisome proliferation by regulating POX1 and PEX11. Gurvitz, A., Hiltunen, J.K., Erdmann, R., Hamilton, B., Hartig, A., Ruis, H., Rottensteiner, H. J. Biol. Chem. (2001) [Pubmed]
  8. Purification, identification, and properties of a Saccharomyces cerevisiae oleate-activated upstream activating sequence-binding protein that is involved in the activation of POX1. Luo, Y., Karpichev, I.V., Kohanski, R.A., Small, G.M. J. Biol. Chem. (1996) [Pubmed]
  9. The POX1 gene encoding peroxisomal acyl-CoA oxidase in Saccharomyces cerevisiae is under the control of multiple regulatory elements. Wang, T., Luo, Y., Small, G.M. J. Biol. Chem. (1994) [Pubmed]
  10. A negative regulating element controlling transcription of the gene encoding acyl-CoA oxidase in Saccharomyces cerevisiae. Wang, T.W., Lewin, A.S., Small, G.M. Nucleic Acids Res. (1992) [Pubmed]
  11. Extracellular secretion of free fatty acids by disruption of a fatty acyl-CoA synthetase gene in Saccharomyces cerevisiae. Michinaka, Y., Shimauchi, T., Aki, T., Nakajima, T., Kawamoto, S., Shigeta, S., Suzuki, O., Ono, K. J. Biosci. Bioeng. (2003) [Pubmed]
  12. Specific binding of the peroxisomal protein targeting sequence to glyoxysomal membranes. Wolins, N.E., Donaldson, R.P. J. Biol. Chem. (1994) [Pubmed]
  13. Binding of the peroxisomal targeting sequence SKL is specified by a low-affinity site in castor bean glyoxysomal membranes. A domain next to the SKL binds to a high-affinity site. Wolins, N.E., Donaldson, R.P. Plant Physiol. (1997) [Pubmed]
  14. Association of glyoxylate and beta-oxidation enzymes with peroxisomes of Saccharomyces cerevisiae. McCammon, M.T., Veenhuis, M., Trapp, S.B., Goodman, J.M. J. Bacteriol. (1990) [Pubmed]
  15. A complex containing two transcription factors regulates peroxisome proliferation and the coordinate induction of beta-oxidation enzymes in Saccharomyces cerevisiae. Karpichev, I.V., Luo, Y., Marians, R.C., Small, G.M. Mol. Cell. Biol. (1997) [Pubmed]
  16. Role of beta-oxidation enzymes in gamma-decalactone production by the yeast Yarrowia lipolytica. Waché, Y., Aguedo, M., Choquet, A., Gatfield, I.L., Nicaud, J.M., Belin, J.M. Appl. Environ. Microbiol. (2001) [Pubmed]
  17. Cloning and characterization of the peroxisomal acyl CoA oxidase ACO3 gene from the alkane-utilizing yeast Yarrowia lipolytica. Wang, H., Le Clainche, A., Le Dall, M.T., Wache, Y., Pagot, Y., Belin, J.M., Gaillardin, C., Nicaud, J.M. Yeast (1998) [Pubmed]
  18. Study of the coinduction by fatty acids of catalase A and acyl-CoA oxidase in standard and mutant Saccharomyces cerevisiae strains. Skoneczny, M., Chełstowska, A., Rytka, J. Eur. J. Biochem. (1988) [Pubmed]
  19. Saccharomyces cerevisiae acyl-CoA oxidase follows a novel, non-PTS1, import pathway into peroxisomes that is dependent on Pex5p. Klein, A.T., van den Berg, M., Bottger, G., Tabak, H.F., Distel, B. J. Biol. Chem. (2002) [Pubmed]
  20. Identification of a class of Saccharomyces cerevisiae mutants defective in fatty acid repression of gene transcription and analysis of the frm2 gene. McHale, M.W., Kroening, K.D., Bernlohr, D.A. Yeast (1996) [Pubmed]
  21. Functional similarity between the peroxisomal PTS2 receptor binding protein Pex18p and the N-terminal half of the PTS1 receptor Pex5p. Schäfer, A., Kerssen, D., Veenhuis, M., Kunau, W.H., Schliebs, W. Mol. Cell. Biol. (2004) [Pubmed]
  22. Futile cycling of intermediates of fatty acid biosynthesis toward peroxisomal beta-oxidation in Saccharomyces cerevisiae. Marchesini, S., Poirier, Y. J. Biol. Chem. (2003) [Pubmed]
  23. Peroxisomal acyl-coenzyme A oxidase multigene family of the yeast Candida tropicalis; nucleotide sequence of a third gene and its protein product. Okazaki, K., Tan, H., Fukui, S., Kubota, I., Kamiryo, T. Gene (1987) [Pubmed]
  24. The primary structure of a peroxisomal fatty acyl-CoA oxidase from the yeast Candida tropicalis pK233. Murray, W.W., Rachubinski, R.A. Gene (1987) [Pubmed]
WikiGenes - Universities