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Gene Review

Cyt-c-d  -  Cytochrome c distal

Drosophila melanogaster

Synonyms: CG13263, Cyt C, Cyt c, Cyt-c1, CytC, ...
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Disease relevance of Cyt-c-d

  • As the biological action linked to heat stress, 14-3-3zeta interacted with apocytochrome c, a mitochondrial precursor protein of cytochrome c, in heat-treated cells, and the suppression of 14-3-3zeta expression by RNA interference resulted in the formation of significant amounts of aggregated apocytochrome c in the cytosol [1].

High impact information on Cyt-c-d

  • Loss of Dapaf-1 function resulted in defective cytochrome c-dependent caspase activities and reduced apoptosis in embryo and in larval brain [2].
  • These data suggest that Dapaf-1/cytochrome c-dependent cell death-inducing machinery is present in Drosophila, and the requirement of Dapaf-1/Apaf-1 in neural cell death is conserved through evolution [2].
  • While a role of the mitochondria and cytochrome C in the assembly of the apoptosome and caspase activation has been established for mammalian cells, the existence of a comparable function for cytochrome C in invertebrates remains controversial [3].
  • However, both cytochrome C proteins can function interchangeably in respiration and caspase activation, and the difference in their genetic requirements can be attributed to differential expression in the soma and testes [3].
  • In cell-free studies, recombinant DC3 or DC4 failed to activate caspases in Drosophila cell lysates, but remarkably induced caspase activation in extracts from human cells [4].

Biological context of Cyt-c-d

  • Cytochrome C has two apparently separable cellular functions: respiration and caspase activation during apoptosis [3].
  • The Drosophila genome contains distinct cyt c genes: cyt c-p and cyt c-d. Loss of cyt c-p function causes embryonic lethality owing to a requirement of the gene for mitochondrial respiration [5].
  • These two sequences, DC3 and DC4, have been isolated from a Charon 4A-D. melanogaster genomic library [6].
  • DC3 and DC4 are located within a 4 kb region of DNA, at position 36A 10-11, on the left arm of chromosome 2 [6].
  • Recent work demonstrates that cytochrome c and caspases function in Drosophila sperm cell differentiation and indicates that caspase activity can be regulated in a subcellular manner in cells that live [7].

Anatomical context of Cyt-c-d

  • We further identified loss-of-function mutations in one of the two Drosophila cyt-c genes, cyt-c-d, which block caspase activation and subsequent spermatid terminal differentiation [8].
  • The T-cell response to Ia purified from cytochrome c-pulsed APCs shows the same MHC restriction and antigen fine specificity as the response to antigen-pulsed APCs [9].
  • The final membrane fraction is enriched by 6 to 8 fold with respect to the plasma membrane enzyme marker Na+/K+ ATPase and substantially depleted of the mitochondrial enzyme marker cytochrome C oxidase [10].
  • The cytochrome P-450 content and the benzo[a]pyrene (BP) hydroxylation, p-nitroanisole demethylation and 3- and 4-hydroxylation of biphenyl were 4-20-fold higher in microsomes from adult flies, while 7-ethoxycoumarin deethylase activity and cytochrome c reductase activity were about the same in the two stages [11].

Associations of Cyt-c-d with chemical compounds

  • In addition, under hyperoxia cytochrome c undergoes a conformational change, manifested by display of an otherwise hidden epitope [12].
  • A purified RNA coded for by the gene is covalently attached to biotin via the protein, cytochrome c. This modified RNA is hybridized to total nuclear, double-stranded DNA under conditions that allow the formation of R-loops [13].
  • The modification consists of coupling cytochrome-c instead of pentane diamine to the oxidized 2', 3' terminus of an RNA by Schiff base formation and BH-4 reduction [14].
  • RESULTS: In muscle biopsy specimens, a significant decrease was found in the activity of complex I (NADH [reduced form of nicotinamide adenine dinucleotide] dehydrogenase), and in one patient, histochemical analysis showed the presence of ragged-red fibers with abnormal cytochrome c oxidase staining [15].
  • Cytochrome c, potassium-ferricyanide, and oxygen can serve as electron acceptors in the oxidation of sulfite by the enzyme [16].

Other interactions of Cyt-c-d

  • Collectively, our results indicate a role of Cyt c in caspase regulation of Drosophila somatic cells [5].

Analytical, diagnostic and therapeutic context of Cyt-c-d

  • The role of cytochrome c (Cyt c) in caspase activation has largely been established from mammalian cell-culture studies, but much remains to be learned about its physiological relevance in situ [5].
  • Gene mapping and gene enrichment by the avidin-biotin interaction: use of cytochrome-c as a polyamine bridge [14].
  • The complete amino acid sequence of cytochrome c from the Dipterous Ceratitis capitata (serie Acalypterae) has been determined by combining automatic and manual methods of sequence analysis [17].


  1. A Novel Function of 14-3-3 Protein: 14-3-3{zeta} Is a Heat-Shock-related Molecular Chaperone That Dissolves Thermal-aggregated Proteins. Yano, M., Nakamuta, S., Wu, X., Okumura, Y., Kido, H. Mol. Biol. Cell (2006) [Pubmed]
  2. Control of the cell death pathway by Dapaf-1, a Drosophila Apaf-1/CED-4-related caspase activator. Kanuka, H., Sawamoto, K., Inohara, N., Matsuno, K., Okano, H., Miura, M. Mol. Cell (1999) [Pubmed]
  3. The two Drosophila cytochrome C proteins can function in both respiration and caspase activation. Arama, E., Bader, M., Srivastava, M., Bergmann, A., Steller, H. EMBO J. (2006) [Pubmed]
  4. The two cytochrome c species, DC3 and DC4, are not required for caspase activation and apoptosis in Drosophila cells. Dorstyn, L., Mills, K., Lazebnik, Y., Kumar, S. J. Cell Biol. (2004) [Pubmed]
  5. Cytochrome c-d regulates developmental apoptosis in the Drosophila retina. Mendes, C.S., Arama, E., Brown, S., Scherr, H., Srivastava, M., Bergmann, A., Steller, H., Mollereau, B. EMBO Rep. (2006) [Pubmed]
  6. Characterization of two Drosophila melanogaster cytochrome c genes and their transcripts. Limbach, K.J., Wu, R. Nucleic Acids Res. (1985) [Pubmed]
  7. Caspase activation finds fertile ground. Baehrecke, E.H. Dev. Cell (2003) [Pubmed]
  8. Caspase activity and a specific cytochrome C are required for sperm differentiation in Drosophila. Arama, E., Agapite, J., Steller, H. Dev. Cell (2003) [Pubmed]
  9. Isolation of a functional antigen-Ia complex. Srinivasan, M., Pierce, S.K. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  10. Isolation of plasma membranes from Drosophila embryos. Jiang, Q.Y., Gnagey, A., Tandler, B., Jacobs-Lorena, M. Mol. Biol. Rep. (1986) [Pubmed]
  11. Comparison of cytochrome P-450-dependent metabolism in different developmental stages of Drosophila melanogaster. Hällstöm, I., Blanck, A., Atuma, S. Chem. Biol. Interact. (1983) [Pubmed]
  12. Mitochondrial "swirls" induced by oxygen stress and in the Drosophila mutant hyperswirl. Walker, D.W., Benzer, S. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  13. Application of the avidin-biotin method of gene enrichment to the isolation of long double-stranded DNA containing specific gene sequences. Pellegrini, M., Holmes, D.S., Manning, J. Nucleic Acids Res. (1977) [Pubmed]
  14. Gene mapping and gene enrichment by the avidin-biotin interaction: use of cytochrome-c as a polyamine bridge. Sodja, A., Davidson, N. Nucleic Acids Res. (1978) [Pubmed]
  15. Mitochondrial dysfunction associated with a mutation in the Notch3 gene in a CADASIL family. de la Peña, P., Bornstein, B., del Hoyo, P., Fernández-Moreno, M.A., Martín, M.A., Campos, Y., Gómez-Escalonilla, C., Molina, J.A., Cabello, A., Arenas, J., Garesse, R. Neurology (2001) [Pubmed]
  16. The molybdoenzyme system of Drosophila melanogaster. I. Sulfite oxidase: identification and properties. Expression of the enzyme in maroon-like (mal), low-xanthine dehydrogenase (lxd), and cinnamon (cin) flies. Bogaart, A.M., Bernini, L.F. Biochem. Genet. (1981) [Pubmed]
  17. Primary structure of cytochrome c from the insect Ceratitis capitata. Fernández-Sousa, J.M., Gavilanes, J.G., Municio, A.M., Paredes, J.A., Pérez-Aranda, A., Rodriguez, R. Biochim. Biophys. Acta (1975) [Pubmed]
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