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Gene Review

SCO1  -  Sco1p

Saccharomyces cerevisiae S288c

Synonyms: Protein SCO1, mitochondrial, YBR037C, YBR0406
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Disease relevance of SCO1


High impact information on SCO1

  • Cox17 is a 69-residue cysteine-rich, copper-binding protein that has been implicated in the delivery of copper to the Cu(A) and Cu(B) centers of cytochrome c oxidase via the copper-binding proteins Sco1 and Cox11, respectively [2].
  • A number of conserved, positively charged residues may interact with complementary surfaces on Sco1 and Cox11, facilitating docking and copper transfer [2].
  • Purified Sco1p sediments identical to Sco1p in crude extracts of mitochondria from wild type yeast or from a strain transformed with SCO1 on a high copy plasmid [3].
  • The copper is not removed by the treatment of Sco1p with EDTA, indicating that it is bound with high affinity [3].
  • Sco1 is a conserved essential protein, which has been implicated in the delivery of copper to cytochrome c oxidase, the last enzyme of the electron transport chain [4].

Chemical compound and disease context of SCO1

  • The Bacillus subtilis genome contains a homologue of yeast Sco1, YpmQ (hereafter termed BSco), deletion of which leads to a phenotype lacking in caa3 (CuA-containing) oxidase activity but expressing normal levels of aa3 (quinol) oxidase activity [5].

Biological context of SCO1


Anatomical context of SCO1

  • SCO2 is a homologue of SCO1, whose product is also localized in the mitochondrial membrane but is not required for respiration [6].
  • The observation that membrane localization of SCO1 is affected in mitochondria of a rho0 strain, hints at the possible involvement of mitochondrially coded components in ensuring proper membrane insertion [10].
  • Sco1, a protein required for the proper assembly of cytochrome c oxidase, has a soluble domain anchored to the cytoplasmic membrane through a single transmembrane segment [11].

Associations of SCO1 with chemical compounds


Physical interactions of SCO1


Other interactions of SCO1

  • The Saccharomyces cerevisiae gene SCO1 has been shown to play an essential role in the transfer of copper to the Cu(A)-centre of the mitochondrial cytochrome c oxidase subunit Cox2p [13].
  • SCO1 was earlier reported to code for a mitochondrial inner membrane protein with an essential function in cytochrome oxidase assembly (Buchwald, P., Krummeck, G., and Rodel, G. (1991) Mol. Gen. Genet. 229, 413-420) [6].
  • AUG codons in the RNA leader sequences of the yeast PET genes CBS1 and SCO1 have no influence on translation efficiency [9].
  • These amino acids, which are conserved among the members of the Sco1p family, have been suggested to act in the reduction of the cysteines in the copper binding center of Cox2p and are discussed as ligands for copper [12].
  • Its fold places Sco1 in a distinct subgroup of the functionally unrelated thioredoxin proteins [11].
  • Using two in vivo assays that permit monitoring of the transient Sco1-Cox2 interaction, the mutant Sco1 molecules appear compromised in a function with Cox2 [14].

Analytical, diagnostic and therapeutic context of SCO1


  1. Characterization of YpmQ, an accessory protein required for the expression of cytochrome c oxidase in Bacillus subtilis. Mattatall, N.R., Jazairi, J., Hill, B.C. J. Biol. Chem. (2000) [Pubmed]
  2. Yeast cox17 solution structure and Copper(I) binding. Abajian, C., Yatsunyk, L.A., Ramirez, B.E., Rosenzweig, A.C. J. Biol. Chem. (2004) [Pubmed]
  3. Purification and characterization of yeast Sco1p, a mitochondrial copper protein. Beers, J., Glerum, D.M., Tzagoloff, A. J. Biol. Chem. (2002) [Pubmed]
  4. Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein. Nittis, T., George, G.N., Winge, D.R. J. Biol. Chem. (2001) [Pubmed]
  5. Spectroscopic studies of metal binding and metal selectivity in Bacillus subtilis BSco, a Homologue of the Yeast Mitochondrial Protein Sco1p. Andruzzi, L., Nakano, M., Nilges, M.J., Blackburn, N.J. J. Am. Chem. Soc. (2005) [Pubmed]
  6. SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae. Glerum, D.M., Shtanko, A., Tzagoloff, A. J. Biol. Chem. (1996) [Pubmed]
  7. The complete sequence of a 33 kb fragment on the right arm of chromosome II from Saccharomyces cerevisiae reveals 16 open reading frames, including ten new open reading frames, five previously identified genes and a homologue of the SCO1 gene. Smits, P.H., De Haan, M., Maat, C., Grivell, L.A. Yeast (1994) [Pubmed]
  8. Yeast SCO1 protein is required for a post-translational step in the accumulation of mitochondrial cytochrome c oxidase subunits I and II. Krummeck, G., Rödel, G. Curr. Genet. (1990) [Pubmed]
  9. AUG codons in the RNA leader sequences of the yeast PET genes CBS1 and SCO1 have no influence on translation efficiency. Krummeck, G., Gottenöf, T., Rödel, G. Curr. Genet. (1991) [Pubmed]
  10. Immunological identification of yeast SCO1 protein as a component of the inner mitochondrial membrane. Buchwald, P., Krummeck, G., Rödel, G. Mol. Gen. Genet. (1991) [Pubmed]
  11. Solution structure of Sco1: a thioredoxin-like protein Involved in cytochrome c oxidase assembly. Balatri, E., Banci, L., Bertini, I., Cantini, F., Ciofi-Baffoni, S. Structure (Camb.) (2003) [Pubmed]
  12. Mitochondrial copper metabolism in yeast: interaction between Sco1p and Cox2p. Lode, A., Kuschel, M., Paret, C., Rödel, G. FEBS Lett. (2000) [Pubmed]
  13. Molecular characterization of Saccharomyces cerevisiae Sco2p reveals a high degree of redundancy with Sco1p. Lode, A., Paret, C., Rödel, G. Yeast (2002) [Pubmed]
  14. Mapping the functional interaction of Sco1 and Cox2 in cytochrome oxidase biogenesis. Rigby, K., Cobine, P.A., Khalimonchuk, O., Winge, D.R. J. Biol. Chem. (2008) [Pubmed]
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