Beschreibung:
<jats:p>Cytochrome <jats:italic>c</jats:italic> oxidase is a multiprotein complex in the mitochondrial membrane whose biogenesis requires a number of proteins besides the structural subunits. Several yeast proteins as well as a human disease‐related protein have been reported which are involved in cytochrome <jats:italic>c</jats:italic> oxidase assembly. The <jats:italic>S. cerevisiae</jats:italic> Sco1p protein has been implicated in the transfer of copper to cytochrome <jats:italic>c</jats:italic> oxidase subunits Cox1p and/or Cox2p. Here we report on the complementation behavior in yeast of two recently identified ScSco1p homologs of chromosome 17 and chromosome 22 from human. When allotropically expressed in yeast, both genes fail to complement the lack of the <jats:italic>ScSCO1</jats:italic> gene. However, a chimera of the N‐terminal half of ScSco1p and the C‐terminal half of the chromosome 17 homolog does substitute for the ScSco1p function. Interestingly, the respective chimera with the human homolog of chromosome 22 is not able to complement. Expression of EGFP fusions in HeLa cells shows that both human ScSco1p homologs are located in the mitochondria of human cells.</jats:p>