Human members of the SCO1 gene family: complementation analysis in yeast and intracellular localization

FEBS Letters

Ostermann, Kai¹  Rödel, Gerhard¹  Rentzsch, Anja¹  Krause-Buchholz, Udo¹  Paret, Claudia¹ 

[1] Institut für Genetik, Technische Universität Dresden, Mommsenstrasse 13, D-01062 Dresden, Germany

关键词: Sco1p;    Copper;    COX;    Mitochondrium;    EGFP fusion;    Human;   

DOI  :  10.1016/S0014-5793(99)00266-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown