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

Rosario Rizzuto, Hirofumi Nakase, Massimo Zeviani, Salvatore DiMauro, Eric A. Schon

Research output: Contribution to journalArticle

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, identicallysized transcript in RNA from human muscle, liver, and brain, while cox Va cDNAs isolated from both endothelial and fetal muscle cDNA libraries had identical nucleotide sequences.

Original languageEnglish
Pages (from-to)245-256
Number of pages12
JournalGene
Volume69
Issue number2
DOIs
Publication statusPublished - Sep 30 1988

Keywords

  • brain
  • leader peptide
  • liver
  • Mitochondrial protein
  • muscle
  • nuclear gene
  • nucleotide sequence analysis
  • presequence
  • recombinant DNA
  • respiratory chain

ASJC Scopus subject areas

  • Genetics

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    Rizzuto, R., Nakase, H., Zeviani, M., DiMauro, S., & Schon, E. A. (1988). Subunit Va of human and bovine cytochrome c oxidase is highly conserved. Gene, 69(2), 245-256. https://doi.org/10.1016/0378-1119(88)90435-0