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

Gene. 1988 Sep 30;69(2):245-56. doi: 10.1016/0378-1119(88)90435-0.


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 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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Biological Evolution*
  • Cattle
  • Cloning, Molecular
  • Electron Transport Complex IV / genetics*
  • Genes
  • Humans
  • Macromolecular Substances
  • Molecular Sequence Data
  • Protein Conformation
  • Restriction Mapping
  • Species Specificity
  • Transcription, Genetic


  • Macromolecular Substances
  • Electron Transport Complex IV

Associated data

  • GENBANK/M22760