Mitochondrial copper metabolism in yeast: mutational analysis of Sco1p involved in the biogenesis of cytochrome c oxidase

Curr Genet. 1999 Mar;35(2):103-8. doi: 10.1007/s002940050438.


Saccharomyces cerevisiae Sco1p is believed to be involved in the transfer of copper from the carrier Cox17p to the mitochondrial cytochrome c oxidase subunits 1 and 2. We here report on the results of a mutational analysis of Sco1p. The two cysteine residues of a potential metal-binding motif (CxxxC) are essential for protein function as shown by their substitution by alanines. Chimeras consisting of Sco1p and its homolog S. cerevisiae Sco2p restrict the specificity of Sco1p function to the N-terminal half of the protein. A candidate region for conferring specificity on Sco1p is a stretch of hydrophobic amino acids, which act as a membrane anchor. In line with this suggestion is the result that alterations of individual amino acids within this region impair Sco1p function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites / genetics
  • Copper / metabolism*
  • Electron Transport Complex IV / biosynthesis
  • Fungal Proteins / genetics
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Mitochondria / metabolism*
  • Mitochondrial Proteins
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Mutation
  • Recombinant Fusion Proteins / genetics
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins*
  • Sequence Deletion
  • Sequence Homology, Amino Acid


  • Fungal Proteins
  • Membrane Proteins
  • Mitochondrial Proteins
  • Recombinant Fusion Proteins
  • SCO1 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Copper
  • Electron Transport Complex IV