The chromosomal loci corresponding to human cytochrome c oxidase (COX) subunit VIIa Liver (VIIa-L) isoform genes were determined utilizing a combined approach of genomic cloning, in situ hybridization, and somatic hybrid genetics. In contrast to the proposal of E. Arnaudo et al. (Gene (Amst.), 119: 299-305, 1992) that COX VIIa-L sequences are located on chromosomes 4 and 14, we found that COX VIIa-L related sequences reside on chromosome 6, while an additional COX VIIa-L cross-reacting sequence psi-gene) was located on chromosome 4.
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Structural organization and transcription regulation of nuclear genes encoding the mammalian cytochrome c oxidase complex.
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Cytochrome c Oxidase (COX) is the terminal component of the bacterial as well as the mitochondrial respiratory chain complex that catalyzes the conversion of redox energy to ATP. In eukaryotes, the oligomeric enzyme is bound to mitochondrial innermembrane with subunits ranging from 7 to 13. Thus, its biosynthesis involves a coordinate interplay between nuclear and mitochondrial genomes.
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Center for Molecular Medicine and Genetics, Wayne State University School of Medicine, Detroit, Michigan 48201, USA.
We have isolated and examined the gene for the heart isoform of cytochrome c oxidase subunit VIIa (COX VIIa-H) in mouse, an isoform gene previously thought to be lacking in rodents. Interspecies amino acid comparisons indicate that mouse COX VIIa-H protein displays 82.5 and 70.
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June 1997
Centre for Cardiovascular Research, Toronto Hospital, ON, Canada.
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Division of Clinical Neuroscience, University of Newcastle upon Tyne, U.K.
On treatment of human liver Hep G2 cells with thiamphenicol, intramitochondrial levels of cytochrome c oxidase (COX) nuclear gene products were shown to decrease in tandem with the mitochondrially-encoded subunits except, however, for subunit IV which proved to be remarkably stable. This nonspecific decrease in subunit level was utilized to assess the function of subunit VIIa-L. Thiamphenicol-pretreated cells were bathed in anti-VIIa-L oligonucleotides and the recovery rate of COX activity compared to control oligomer-untreated cells or cells with a similar concentration of a randomized oligomer.
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Subunit VIIa of mammalian cytochrome c oxidase (COX; EC 1.9.3.
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