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Gene Review

ICL1  -  isocitrate lyase 1

Saccharomyces cerevisiae S288c

Synonyms: ICL, Isocitrase, Isocitratase, Isocitrate lyase, Threo-D(S)-isocitrate glyoxylate-lyase, ...
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Disease relevance of ICL1


High impact information on ICL1

  • The facB gene is required for acetate induction of acetamidase (amdS) and the acetate utilization enzymes acetyl-CoA synthase (facA), isocitrate lyase (acuD) and malate synthase (acuE) in Aspergillus nidulans [5].
  • Deletion analysis of the ICL1 promoter led to the identification of an upstream activating sequence element, UASICL1 (5' CATTCATCCG 3'), necessary and sufficient for conferring carbon source-dependent regulation on a heterologous reporter gene [6].
  • The GAL82 and GAL83 mutations are probably specific for expression of the Leloir pathway and related enzymes, because they do not affect the synthesis of alpha-D-glucosidase, invertase, or isocitrate lyase [7].
  • All mutant strains show in addition a defect in catabolite inactivation of three other gluconeogenic enzymes: cytosolic malate dehydrogenase, isocitrate lyase, and phosphoenolpyruvate carboxykinase [8].
  • To investigate acetate and fatty acid utilization, the acuD gene encoding a key glyoxylate cycle enzyme (isocitrate lyase) was cloned [9].

Biological context of ICL1


Anatomical context of ICL1


Associations of ICL1 with chemical compounds


Physical interactions of ICL1

  • The peptide corresponding to wild-type ICL interacted with all three Pex5p proteins to differing extents, but neither mutant could interact with Pex5p from any species [13].

Other interactions of ICL1

  • Northern-blot analysis showed that this can be ascribed to no increase in transcription of ICL1 and FBP1 encoding fructose 1,6-bisphosphatase [14].
  • Expression of the ICL gene with full-length UPR-ICL increased about tenfold in mig1 cells grown on glucose, while little difference was observed in acetate-grown cells [12].
  • By deletion analyses as well as by studying the influence on expression of different fragments cloned into the heterologous CYC1 promoter lacking its own UAS sequences, we defined UAS and URS elements in the ICL1 promoter [19].
  • Mutations in gene ICL1, which encodes isocitrate lyase, resulted in overproduction of ACS without any growth on acetate [20].
  • The latter is not capable of complementing an icl1 deletion for growth on ethanol neither in its original context, nor when expressed under the control of the glycolytic PFK2 promoter [11].

Analytical, diagnostic and therapeutic context of ICL1

  • In Northern blot analyses we first showed that the steady-state ICL1 mRNA levels depend on the carbon source used for growth [19].
  • No label was found in the band corresponding to the isocitrate lyase when immunoprecipitation was done with a control pre-immune serum or in the presence of excess pure unlabelled enzyme [21].
  • In contrast, mutations T250R-R251N and L255F-K256R located in the C-terminus of the 3rd ICL of AT2 retained ligand-binding properties of the wild-type AT2, and its ability to interact with the ErbB3 in yeast two-hybrid assay, but abolished AT2-mediated cGMP reduction [22].
  • We observed subcellular localization of expressed products of the mutant CT-ICL genes by immunoelectron microscopy [23].


  1. Cloning of the isocitrate lyase gene (ICL1) from Yarrowia lipolytica and characterization of the deduced protein. Barth, G., Scheuber, T. Mol. Gen. Genet. (1993) [Pubmed]
  2. Relationship of the glyoxylate pathway to the pathogenesis of Cryptococcus neoformans. Rude, T.H., Toffaletti, D.L., Cox, G.M., Perfect, J.R. Infect. Immun. (2002) [Pubmed]
  3. The glyoxylate cycle is required for fungal virulence. Lorenz, M.C., Fink, G.R. Nature (2001) [Pubmed]
  4. Development of novel whole-cell immunoadsorbents by yeast surface display of the IgG-binding domain. Nakamura, Y., Shibasaki, S., Ueda, M., Tanaka, A., Fukuda, H., Kondo, A. Appl. Microbiol. Biotechnol. (2001) [Pubmed]
  5. FacB, the Aspergillus nidulans activator of acetate utilization genes, binds dissimilar DNA sequences. Todd, R.B., Andrianopoulos, A., Davis, M.A., Hynes, M.J. EMBO J. (1998) [Pubmed]
  6. A carbon source-responsive promoter element necessary for activation of the isocitrate lyase gene ICL1 is common to genes of the gluconeogenic pathway in the yeast Saccharomyces cerevisiae. Schöler, A., Schüller, H.J. Mol. Cell. Biol. (1994) [Pubmed]
  7. Isolation and characterization of dominant mutations resistant to carbon catabolite repression of galactokinase synthesis in Saccharomyces cerevisiae. Matsumoto, K., Toh-e, A., Oshima, Y. Mol. Cell. Biol. (1981) [Pubmed]
  8. Proteins of newly isolated mutants and the amino-terminal proline are essential for ubiquitin-proteasome-catalyzed catabolite degradation of fructose-1,6-bisphosphatase of Saccharomyces cerevisiae. Hämmerle, M., Bauer, J., Rose, M., Szallies, A., Thumm, M., Düsterhus, S., Mecke, D., Entian, K.D., Wolf, D.H. J. Biol. Chem. (1998) [Pubmed]
  9. Developmental regulation of the glyoxylate cycle in the human pathogen Penicillium marneffei. C??novas, D., Andrianopoulos, A. Mol. Microbiol. (2006) [Pubmed]
  10. Constitutive and carbon source-responsive promoter elements are involved in the regulated expression of the Saccharomyces cerevisiae malate synthase gene MLS1. Caspary, F., Hartig, A., Schüller, H.J. Mol. Gen. Genet. (1997) [Pubmed]
  11. Molecular genetics of ICL2, encoding a non-functional isocitrate lyase in Saccharomyces cerevisiae. Heinisch, J.J., Valdés, E., Alvarez, J., Rodicio, R. Yeast (1996) [Pubmed]
  12. Derepression of gene expression mediated by the 5' upstream region of the isocitrate lyase gene of Candida tropicalis is controlled by two distinct regulatory pathways in Saccharomyces cerevisiae. Umemura, K., Atomi, H., Kanai, T., Takeshita, S., Kanayama, N., Ueda, M., Tanaka, A. Eur. J. Biochem. (1997) [Pubmed]
  13. PTS1-independent targeting of isocitrate lyase to peroxisomes requires the PTS1 receptor Pex5p. Parkes, J.A., Langer, S., Hartig, A., Baker, A. Mol. Membr. Biol. (2003) [Pubmed]
  14. A regulatory factor, Fil1p, involved in derepression of the isocitrate lyase gene in Saccharomyces cerevisiae--a possible mitochondrial protein necessary for protein synthesis in mitochondria. Kanai, T., Takeshita, S., Atomi, H., Umemura, K., Ueda, M., Tanaka, A. Eur. J. Biochem. (1998) [Pubmed]
  15. Impairment of peroxisome degradation in Pichia methanolica mutants defective in acetyl-CoA synthetase or isocitrate lyase. Kulachkovsky, A.R., Moroz, O.M., Sibirny, A.A. Yeast (1997) [Pubmed]
  16. Characterization of Aspergillus nidulans peroxisomes by immunoelectron microscopy. Valenciano, S., De Lucas, J.R., Van der Klei, I., Veenhuis, M., Laborda, F. Arch. Microbiol. (1998) [Pubmed]
  17. The Saccharomyces cerevisiae ICL2 gene encodes a mitochondrial 2-methylisocitrate lyase involved in propionyl-coenzyme A metabolism. Luttik, M.A., Kötter, P., Salomons, F.A., van der Klei, I.J., van Dijken, J.P., Pronk, J.T. J. Bacteriol. (2000) [Pubmed]
  18. A mutation affecting carbon catabolite repression suppresses growth defects in pyruvate carboxylase mutants from Saccharomyces cerevisiae. Blázquez, M.A., Gamo, F.J., Gancedo, C. FEBS Lett. (1995) [Pubmed]
  19. Transcriptional regulation of the isocitrate lyase encoding gene in Saccharomyces cerevisiae. Fernandez, E., Fernandez, M., Moreno, F., Rodicio, R. FEBS Lett. (1993) [Pubmed]
  20. Characterization of mutants of the yeast Yarrowia lipolytica defective in acetyl-coenzyme A synthetase. Kujau, M., Weber, H., Barth, G. Yeast (1992) [Pubmed]
  21. Glucose-stimulated phosphorylation of yeast isocitrate lyase in vivo. López-Boado, Y.S., Herrero, P., Fernández, T., Fernández, R., Moreno, F. J. Gen. Microbiol. (1988) [Pubmed]
  22. Roles of the intracellular regions of angiotensin II receptor AT2 in mediating reduction of intracellular cGMP levels. Pulakat, L., Rahman, S., Gray, A., Knowle, D., Gavini, N. Cell. Signal. (2005) [Pubmed]
  23. Three-dimensional analysis of protein aggregate body in Saccharomyces cerevisiae cells. Kamasawa, N., Yoshida, T., Ueda, M., Tanaka, A., Osumi, M. Journal of electron microscopy. (1999) [Pubmed]
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