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Subunit Va of human and bovine cytochrome c oxidase is highly conserved
Authors:R Rizzuto  H Nakase  M Zeviani  S DiMauro  E A Schon
Affiliation:H. Houston Merritt Clinical Research Center for Muscular Dystrophy and Related Disorders, Columbia University College of Physicians and Surgeons, New York, NY 10032.
Abstract:We have isolated a full-length cDNA clone specifying the nuclear-encoded subunit Va of the human mitochondrial respiratory enzyme cytochrome c oxidase (COX; EC 1.9.3.1.). The deduced sequence of the polypeptide is 95% identical to that of the corresponding subunit of bovine COX, which makes it the most conserved polypeptide among the known bovine/human pairs of COX subunits. This polypeptide contains an N-terminal presequence which is rich in basic and hydroxylated residues, but differs from the deduced presequences of all other previously isolated COX subunits in that it also contains a negatively charged residue. We find no evidence of tissue-specific isoforms of subunit Va, as Northern analysis showed a single, identically-sized transcript in RNA from human muscle, liver, and brain, while coxVa cDNAs isolated from both endothelial and fetal muscle cDNA libraries had identical nucleotide sequences.
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