| 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 |
| Journal | Gene |
| Volume | 69 |
| Issue | 2 |
| Pagination | 245-56 |
| Date Published | 1988 Sep 30 |
| ISSN | 0378-1119 |
| 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 |
| 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. |
| DOI | 10.1016/0378-1119(88)90435-0 |
| Alternate Journal | Gene |
| Citation Key | 10.1016/0378-1119(88)90435-0 |
| PubMed ID | 2853101 |
| Grant List | NS11766 / NS / NINDS NIH HHS / United States |
