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Fatal infantile cardioencephalomyopathy with COX deficiency and mutations in SCO2, a COX assembly gene
Mammalian cytochrome c oxidase (COX) catalyses the transfer of reducing equivalents from cy tochrome c to molecular oxygen and pumps protons across the inner mitochondrial membrane and mutations in the human homologue, SCO2, in three unrelated infants with a newly recognized fatal cardioencephalomyopathy and COX deficiency are identified.
Characterization of COX17, a Yeast Gene Involved in Copper Metabolism and Assembly of Cytochrome Oxidase*
Evidence is presented indicating that Cox17p is not involved in general copper metabolism in yeast but rather has a more specific function in the delivery of copper to mitochondria.
SCO1 and SCO2 Act as High Copy Suppressors of a Mitochondrial Copper Recruitment Defect in Saccharomyces cerevisiae*
The ability of SCO2 to restore respiration in cox17, but not in sco1 mutants, is interpreted to indicate that Sco1p and Sco2p have overlapping but not identical functions.
Mutations in COX15 produce a defect in the mitochondrial heme biosynthetic pathway, causing early-onset fatal hypertrophic cardiomyopathy.
COX15 is established as an additional cause, along with SCO2, of fatal infantile, hypertrophic cardiomyopathy associated with isolated COX deficiency, and results suggest that reduced availability of heme A stalls the assembly of COX.
Purification, Characterization, and Localization of Yeast Cox17p, a Mitochondrial Copper Shuttle*
Results are consistent with the previously proposed function of Cox17p, namely in providing cytoplasmic copper for mitochondrial utilization.
Involvement of mitochondrial ferredoxin and Cox15p in hydroxylation of heme O
SHY1, the Yeast Homolog of the MammalianSURF-1 Gene, Encodes a Mitochondrial Protein Required for Respiration*
- Grigoriy Mashkevich, B. Repetto, D. Glerum, C. Jin, A. Tzagoloff
- BiologyThe Journal of Biological Chemistry
- 30 May 1997
Evidence, together with the ability of a carboxyl-terminal coding sequence starting from the BamHI site to complement a shy1 mutant, suggests that the Shy1p contains two domains that can be separately expressed to form a functional protein.
Mutational Analysis of the Saccharomyces cerevisiae Cytochrome c Oxidase Assembly Protein Cox11p
These studies provide the first evidence at the level of the cytochrome oxidase holoenzyme that Cox1p is the in vivo target for Cox11p and suggest that Cox 11p may also have a role in the response to hydrogen peroxide exposure.
FLX1 Codes for a Carrier Protein Involved in Maintaining a Proper Balance of Flavin Nucleotides in Yeast Mitochondria (*)
Genetic evidence has confirmed that the flavin nucleotide imbalance of G178 mutants is caused by mutations in FLX1, and suggests that Flx1p is involved in flavin transport, a role that is also supported by biochemical evidence indicating more efficient flux of FAD across mitochondrial membrane vesicles prepared from wild-type strains than membraneVesicles from flx1 mutants.