Subunit Va of human and bovine cytochrome c oxidase is highly conserved.
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Rizzuto R, Nakase H, Zeviani M, DiMauro S, Schon EA
Subunit Va of human and bovine cytochrome c oxidase is highly conserved.
Gene. 1988 Sep 30;69(2):245-56.
- PubMed ID
- 2853101 [ View in PubMed]
- 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.