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Gene Review

SCO2  -  Sco2p

Saccharomyces cerevisiae S288c

Synonyms: Protein SCO2, mitochondrial, YBR024W, YBR0308
 
 
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Disease relevance of SCO2

 

High impact information on SCO2

  • Cytochrome c oxidase deficiency due to mutations in SCO2, encoding a mitochondrial copper-binding protein, is rescued by copper in human myoblasts [3].
  • To investigate the extent to which mutations in SCO2 are responsible for this phenotype, a complete sequence analysis of the gene was performed on ten patients in nine families [1].
  • The Sco2/Cox17 protein restores respiratory growth and normal cytochrome oxidase activity in cox17Delta cells [4].
  • The Sco2/Cox17 fusion protein containing the mitochondrial import sequence and transmembrane segment of Sco2 is exclusively localized within the mitochondrion [4].
  • Pathogenic mutations in SCO2, which encodes a cytochrome oxidase assembly factor, were recently described in several cases of fatal infantile cardioencephalomyopathy [5].
 

Biological context of SCO2

 

Anatomical context of SCO2

 

Associations of SCO2 with chemical compounds

 

Physical interactions of SCO2

 

Other interactions of SCO2

  • Although SCO2 can also partially restore respiratory growth in the cox17 null mutant, rescue in this case requires addition of copper to the growth medium [6].
  • Our data suggest that Sco2p is involved in the transfer of copper to Cox2p, but that this activity is insufficient for oxidative growth and not able to substitute for Sco1p activity [7].

References

  1. Mutations in SCO2 are associated with a distinct form of hypertrophic cardiomyopathy and cytochrome c oxidase deficiency. Jaksch, M., Ogilvie, I., Yao, J., Kortenhaus, G., Bresser, H.G., Gerbitz, K.D., Shoubridge, E.A. Hum. Mol. Genet. (2000) [Pubmed]
  2. Homozygosity (E140K) in SCO2 causes delayed infantile onset of cardiomyopathy and neuropathy. Jaksch, M., Horvath, R., Horn, N., Auer, D.P., Macmillan, C., Peters, J., Gerbitz, K.D., Kraegeloh-Mann, I., Muntau, A., Karcagi, V., Kalmanchey, R., Lochmuller, H., Shoubridge, E.A., Freisinger, P. Neurology (2001) [Pubmed]
  3. Cytochrome c oxidase deficiency due to mutations in SCO2, encoding a mitochondrial copper-binding protein, is rescued by copper in human myoblasts. Jaksch, M., Paret, C., Stucka, R., Horn, N., Müller-Höcker, J., Horvath, R., Trepesch, N., Stecker, G., Freisinger, P., Thirion, C., Müller, J., Lunkwitz, R., Rödel, G., Shoubridge, E.A., Lochmüller, H. Hum. Mol. Genet. (2001) [Pubmed]
  4. Cox17 is functional when tethered to the mitochondrial inner membrane. Maxfield, A.B., Heaton, D.N., Winge, D.R. J. Biol. Chem. (2004) [Pubmed]
  5. A human SCO2 mutation helps define the role of Sco1p in the cytochrome oxidase assembly pathway. Dickinson, E.K., Adams, D.L., Schon, E.A., Glerum, D.M. J. Biol. Chem. (2000) [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. Molecular characterization of Saccharomyces cerevisiae Sco2p reveals a high degree of redundancy with Sco1p. Lode, A., Paret, C., Rödel, G. Yeast (2002) [Pubmed]
 
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