|Title||Subunit Va of human and bovine cytochrome c oxidase is highly conserved.|
|Publication Type||Journal Article|
|Year of Publication||1988|
|Authors||Rizzuto, R, Nakase, H, Zeviani, M, DiMauro, S, Schon, EA|
|Date Published||1988 Sep 30|
|Keywords||Amino Acid Sequence, Animals, Base Sequence, Biological Evolution, Cattle, Cloning, Molecular, Electron Transport Complex IV, Genes, Humans, Macromolecular Substances, Molecular Sequence Data, Protein Conformation, Restriction Mapping, Species Specificity, Transcription, Genetic|
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 188.8.131.52.). 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.
|Grant List||NS11766 / NS / NINDS NIH HHS / United States|