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Human members of the SCO1 gene family: complementation analysis in yeast and intracellular localization
Author(s) -
Paret Claudia,
Ostermann Kai,
Krause-Buchholz Udo,
Rentzsch Anja,
Rödel Gerhard
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00266-5
Subject(s) - complementation , biology , gene , fusion protein , cytochrome c oxidase , yeast , genetics , microbiology and biotechnology , mitochondrion , recombinant dna , mutant
Cytochrome c 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 c oxidase assembly. The S. cerevisiae Sco1p protein has been implicated in the transfer of copper to cytochrome c 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 ScSCO1 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.