Subunit Va of human and bovine cytochrome c oxidase is highly conserved.

TitleSubunit Va of human and bovine cytochrome c oxidase is highly conserved.
Publication TypeJournal Article
Year of Publication1988
AuthorsRizzuto, R, Nakase, H, Zeviani, M, DiMauro, S, Schon, EA
JournalGene
Volume69
Issue2
Pagination245-56
Date Published1988 Sep 30
ISSN0378-1119
KeywordsAmino 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.

DOI10.1016/0378-1119(88)90435-0
Alternate JournalGene
Citation Key10.1016/0378-1119(88)90435-0
PubMed ID2853101
Grant ListNS11766 / NS / NINDS NIH HHS / United States