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SCO1  -  SCO1 cytochrome c oxidase assembly protein

Homo sapiens

Synonyms: Protein SCO1 homolog, mitochondrial, SCOD1
 
 
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Disease relevance of SCO1

 

High impact information on SCO1

  • In the January 3 issue of Cell Metabolism, report that the mitochondrial metallochaperones Sco1 and Sco2, essential for cytochrome c oxidase assembly, are also responsible for maintenance of cell copper homeostasis, thus showing a new function of mitochondria [6].
  • At least one of two extended haplotypes (B44, DR7, FC31 or B8, DR3, SCO1) were detected in 6 of the 9 who did not respond to revaccination, compared with 2 of 11 who responded to a second course of vaccine [7].
  • The pathogenic mutant (P174L) of human Sco1 produces respiratory chain deficiency associated with cytochrome c oxidase (CcO) assembly defects [8].
  • The pathogenic mutation therefore could (i) lessen the Sco1 affinity for copper(I) and hence copper supply for CcO or (ii) decrease the efficiency of reduction of CcO thiols involved in copper binding, or both effects could be produced by the mutation [8].
  • We browsed bacterial genomes to search proteins functionally equivalent to Cox17, and we identified a class of proteins of unknown function displaying a conserved gene neighborhood to bacterial Sco1 genes, all sharing a potential metal binding motif H(M)X10MX21HXM [9].
 

Biological context of SCO1

  • At least three proteins, COX17p, SCO1p, and its homologue SCO2p are thought to be involved in mitochondrial copper transport to cytochrome-c-oxidase (COX), the terminal enzyme of the respiratory chain [1].
  • Overexpression of either wild-type SCO protein in the reciprocal patient background resulted in a dominant-negative phenotype, suggesting a physical interaction between SCO1 and SCO2 [10].
  • The Human Cytochrome c Oxidase Assembly Factors SCO1 and SCO2 Have Regulatory Roles in the Maintenance of Cellular Copper Homeostasis [11].
  • One of the hSCO1 alleles harboured a frame shift mutation resulting in a premature stop codon, the other a missense mutation leading to a substitution of proline(174) by leucine [12].
  • SCOD removal efficiency of 90 +/- 3% was achieved by both systems at an organic loading rate of 25 +/- 1 kg COD/m3 of total sludge bed volume per day, indicating that the installation of an acidification reactor had no effect in terms of the maximum granular activity, biomass granulation and the settleability of granules [13].
 

Anatomical context of SCO1

  • We studied fibroblast cultures from patients carrying mutations in the assembly factors COX10, SCO1, or SURF1 [14].
  • This approach led to the identification of hSCO1, a component of the inner mitochondrial membrane, which is required for the correct assembly, and catalytic function of cytochrome-c oxidase, as a Fas down-regulated gene [5].
 

Associations of SCO1 with chemical compounds

  • This proline, adjacent to the CxxxC copper-binding domain of SCO1, is likely to play a crucial role in the tridimentional structure of the domain [2].
  • In contrast, replacement of Asp238 in human or yeast Sco1 abrogated the Cu(II) visible transitions and in yeast Sco1 attenuated Cu(II), but not Cu(I), binding [15].
  • In Fenton oxidation, the removal efficiencies of SCOD and colour were 67.7% and 84.7%, respectively [16].
  • In this case, the biogas production, methane production and the SCOD removal efficiency were about 5037 l biogas/m3 WAS, 3367 l methane/m3 WAS and 61.4%, respectively [17].
  • Ammonia-nitrogen (NH(4)-N) was almost totally removed in both reactors, apparently by nitrification throughout the run, while denitrification declined with decreasing SCOD in the influent resulting in an increase in the effluent nitrate-nitrogen (NO(3)-N) concentration [18].
 

Other interactions of SCO1

  • SCO1-deficient cells contained accumulated levels of the MTCO1.COX4.COX5A subassembly, suggesting that MTCO2 associates with the MTCO1.COX4.COX5A subassembly after the Cu(A) center of MTCO2 is formed [14].
  • To investigate the molecular function of the SCO proteins, we characterized the mitochondrial copper delivery pathway in SCO1 and SCO2 patient backgrounds [10].
  • A transcript map of MRIII has been generated and contains 25 candidate BOA genes, four of which are the named genes MYH3, SCO1, x006 and MAGOH-LIKE [19].
  • Cox17 is a key copper donor to two accessory proteins, Sco1 and Cox11, to form the two copper centers in the mature CcO complex [20].

References

  1. Characterization of human SCO1 and COX17 genes in mitochondrial cytochrome-c-oxidase deficiency. Horvath, R., Lochmüller, H., Stucka, R., Yao, J., Shoubridge, E.A., Kim, S.H., Gerbitz, K.D., Jaksch, M. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  2. Mutations of the SCO1 gene in mitochondrial cytochrome c oxidase deficiency with neonatal-onset hepatic failure and encephalopathy. Valnot, I., Osmond, S., Gigarel, N., Mehaye, B., Amiel, J., Cormier-Daire, V., Munnich, A., Bonnefont, J.P., Rustin, P., Rötig, A. Am. J. Hum. Genet. (2000) [Pubmed]
  3. Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein. Williams, J.C., Sue, C., Banting, G.S., Yang, H., Glerum, D.M., Hendrickson, W.A., Schon, E.A. J. Biol. Chem. (2005) [Pubmed]
  4. Increased frequency of HLA-DR3 and complotype SCO1 in Mexican mestizo children with amoebic abscess of the liver. Arellano, J., Peŕez-Rodríguez, M., López-Osuna, M., Velázquez, J.R., Granados, J., Justiniani, N., Santos, J.I., Madrazo, A., Muñoz, L., Kretschmer, R. Parasite Immunol. (1996) [Pubmed]
  5. Fas-induced apoptosis of glioma cells is associated with down-regulation of the hSCO1 protein, a subunit of complex IV. Jayanthi, S., Lewis, B.D., Cadet, J.L. Brain Res. Mol. Brain Res. (2001) [Pubmed]
  6. The scoop on sco. Brière, J.J., Tzagoloff, A. Mol. Cell (2007) [Pubmed]
  7. Nonresponsiveness to hepatitis B vaccine in health care workers. Results of revaccination and genetic typings. Craven, D.E., Awdeh, Z.L., Kunches, L.M., Yunis, E.J., Dienstag, J.L., Werner, B.G., Polk, B.F., Syndman, D.R., Platt, R., Crumpacker, C.S. Ann. Intern. Med. (1986) [Pubmed]
  8. Human Sco1 functional studies and pathological implications of the P174L mutant. Banci, L., Bertini, I., Ciofi-Baffoni, S., Leontari, I., Martinelli, M., Palumaa, P., Sillard, R., Wang, S. Proc. Natl. Acad. Sci. U.S.A. (2007) [Pubmed]
  9. A copper(I) protein possibly involved in the assembly of CuA center of bacterial cytochrome c oxidase. Banci, L., Bertini, I., Ciofi-Baffoni, S., Katsari, E., Katsaros, N., Kubicek, K., Mangani, S. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  10. Human SCO1 and SCO2 have independent, cooperative functions in copper delivery to cytochrome c oxidase. Leary, S.C., Kaufman, B.A., Pellecchia, G., Guercin, G.H., Mattman, A., Jaksch, M., Shoubridge, E.A. Hum. Mol. Genet. (2004) [Pubmed]
  11. The Human Cytochrome c Oxidase Assembly Factors SCO1 and SCO2 Have Regulatory Roles in the Maintenance of Cellular Copper Homeostasis. Leary, S.C., Cobine, P.A., Kaufman, B.A., Guercin, G.H., Mattman, A., Palaty, J., Lockitch, G., Winge, D.R., Rustin, P., Horvath, R., Shoubridge, E.A. Cell metabolism (2007) [Pubmed]
  12. The P(174)L mutation in the human hSCO1 gene affects the assembly of cytochrome c oxidase. Paret, C., Lode, A., Krause-Buchholz, U., Rödel, G. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  13. Pre-acidification in anaerobic sludge bed process treating brewery wastewater. Ahn, Y.H., Min, K.S., Speece, R.E. Water Res. (2001) [Pubmed]
  14. Cytochrome c oxidase subassemblies in fibroblast cultures from patients carrying mutations in COX10, SCO1, or SURF1. Williams, S.L., Valnot, I., Rustin, P., Taanman, J.W. J. Biol. Chem. (2004) [Pubmed]
  15. Human Sco1 and Sco2 function as copper-binding proteins. Horng, Y.C., Leary, S.C., Cobine, P.A., Young, F.B., George, G.N., Shoubridge, E.A., Winge, D.R. J. Biol. Chem. (2005) [Pubmed]
  16. Evaluation of predominant reaction mechanisms for the Fenton process in textile dyeing wastewater treatment. Bae, W., Lee, S.H., Ko, G.B. Water Sci. Technol. (2004) [Pubmed]
  17. Effects of various pretreatments for enhanced anaerobic digestion with waste activated sludge. Kim, J., Park, C., Kim, T.H., Lee, M., Kim, S., Kim, S.W., Lee, J. J. Biosci. Bioeng. (2003) [Pubmed]
  18. Removal of bis (2-ethylhexyl) phthalate from reject water in a nitrogen-removing sequencing batch reactor. Marttinen, S.K., Ruissalo, M., Rintala, J.A. J. Environ. Manage. (2004) [Pubmed]
  19. Physical and transcript map of the minimally deleted region III on 17p implicated in the early development of Barrett's oesophageal adenocarcinoma. Dunn, J.R., Risk, J.M., Langan, J.E., Marlee, D., Ellis, A., Campbell, F., Watson, A.J., Field, J.K. Oncogene (2003) [Pubmed]
  20. Copper trafficking to the mitochondrion and assembly of copper metalloenzymes. Cobine, P.A., Pierrel, F., Winge, D.R. Biochim. Biophys. Acta (2006) [Pubmed]
 
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