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Gene Review

cyc-2.1  -  Protein CYC-2.1

Caenorhabditis elegans

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High impact information on E04A4.7

  • Mitochondria integrate apoptotic signalling by releasing cytochrome c and other proapoptotic cofactors needed for activation of effector caspases [1].
  • Despite these differences, all of the proteins interacted directly with membranes, as determined using a cytochrome c competition assay, although Sj-FABPc interacted to a greater extent than did Ov-FAR-1 or rABA-1A1 [2].
  • Western blot analysis of fractionated protein extracts prepared from granulosa cells before and after in vitro culture without hormonal support to induce apoptosis indicated that mitochondrial cytochrome c release, a biochemical step required for the activation of Apaf-1, occurs in granulosa cells cultured in vitro [3].
  • The complete amino acid sequence of cytochrome c from the nematode Caenorhabditis elegans was determined [4].
  • Recent studies focus on cytochrome c as pivotal in mediating conversion of procaspase-9 as a major initiator for apoptosis [5].

Biological context of E04A4.7

  • Evidence is presented that peptide products of hydrolysis of casein, including some di- and tripeptides, but not the constituent amino acids, can stimulate growth of C. briggsae in defined basal medium supplemented with cytochrome C and B-sitosterol [6].

Anatomical context of E04A4.7


Associations of E04A4.7 with chemical compounds

  • The anti-apoptotic members of this family, such as Bcl-2 and Bcl-XL, prevent apoptosis either by sequestering proforms of death-driving cysteine proteases called caspases (a complex called the apoptosome) or by preventing the release of mitochondrial apoptogenic factors such as cytochrome c and AIF (apoptosis-inducing factor) into the cytoplasm [8].
  • SET domains are protein lysine methyltransferases that methylate diverse proteins, such as, histones, Rubisco and cytochrome C. In particular, they play an important role in the dynamics of the eukaryotic chromatin and are present in several chromatin-associated proteins [9].

Other interactions of E04A4.7


  1. The many shapes of mitochondrial death. Cereghetti, G.M., Scorrano, L. Oncogene (2006) [Pubmed]
  2. How helminth lipid-binding proteins offload their ligands to membranes: differential mechanisms of fatty acid transfer by the ABA-1 polyprotein allergen and Ov-FAR-1 proteins of nematodes and Sj-FABPc of schistosomes. McDermott, L., Kennedy, M.W., McManus, D.P., Bradley, J.E., Cooper, A., Storch, J. Biochemistry (2002) [Pubmed]
  3. Localization, regulation and possible consequences of apoptotic protease-activating factor-1 (Apaf-1) expression in granulosa cells of the mouse ovary. Robles, R., Tao, X.J., Trbovich, A.M., Maravel, D.V., Nahum, R., Perez, G.I., Tilly, K.I., Tilly, J.L. Endocrinology (1999) [Pubmed]
  4. The primary structure of cytochrome c from the nematode Caenorhabditis elegans. Vanfleteren, J.R., Evers, E.A., Van de Werken, G., Van Beeumen, J.J. Biochem. J. (1990) [Pubmed]
  5. Recent advances on neuronal caspases in development and neurodegeneration. Marks, N., Berg, M.J. Neurochem. Int. (1999) [Pubmed]
  6. Stimulatory effects of peptides on growth of the free-living nematode Caenorhabditis briggsae. Pinnock, C., Shane, B., Stokstad, E.L. Proc. Soc. Exp. Biol. Med. (1975) [Pubmed]
  7. Catalase activity during the development of the parasitic nematode, Ascaris suum. Lesoon, A., Komuniecki, P.R., Komuniecki, R. Comp. Biochem. Physiol., B (1990) [Pubmed]
  8. Role of Bcl-2 family proteins in apoptosis: apoptosomes or mitochondria? Tsujimoto, Y. Genes Cells (1998) [Pubmed]
  9. Provenance of SET-domain histone methyltransferases through duplication of a simple structural unit. Aravind, L., Iyer, L.M. Cell Cycle (2003) [Pubmed]
  10. Molecular genealogy of some nematode taxa as based on cytochrome c and globin amino acid sequences. Vanfleteren, J.R., Van de Peer, Y., Blaxter, M.L., Tweedie, S.A., Trotman, C., Lu, L., Van Hauwaert, M.L., Moens, L. Mol. Phylogenet. Evol. (1994) [Pubmed]
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