Characterization of Cox15p, a cytochrome c oxidase assembly factor and component of the eukaryotic heme A synthase
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Abstract
Cytochrome c oxidase (COX) converts oxygen to water as part of oxidative phosphorylation. Studies in yeast estimate that more than forty different genes are required for COX assembly. The heme A prosthetic groups are essential for COX function and defects in heme A synthesis have been shown to underlie human COX deficiencies. The nuclear-encoded Cox15p has been proposed to have a role in heme A synthesis. I have characterized S. cerevisiae cox15 mutant strains with regards to respiratory growth, COX assembly, heme A levels, and stability of the mutant Cox15p. I have identified mutants with a novel phenotype. Initial studies suggest that a cox15 null strain has abnormal mitochondrial morphology and that Cox15p has a role in peroxide metabolism. My results further support the functioning of Cox15p in heme A biosynthesis and provide insight into the variable clinical phenotypes seen in patients with COX15 mutations.