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J Biol Chem. 1987 Oct 15;262(29):14014-21.

Structure and evolution of primate cytochrome c oxidase subunit II gene.

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Department of Biochemistry, Queen's University, Kingston, Ontario, Canada.


The sequence of cytochrome oxidase subunit II (COII) mRNA from the cynomolgus macaque has been determined. Availability of the sequence from a non-human primate has allowed examination of the evolution of the COII gene and protein along the primate lineage. Comparison with existing protein and DNA sequences, combined with estimates of divergence derived from calculations designed to compensate for multiple mutation and reversion events, indicates that although the rate of fixation of nucleotide substitutions at silent sites is somewhat lower in primates than non-primates, the rate of fixation at replacement sites is 4-5-fold higher. The data also suggest that the rate of divergence at replacement sites along the primate lineage has not been uniform, but has decreased 2-2.5-fold since the higher primate branch point, in the absence of a comparable change in the rate substitution at silent sites. Both primate mRNAs differ from their non-primate homologues in having 3'-untranslated regions of 20-25 nucleotides. Examination of the monkey and human untranslated sequences suggests that these regions have evolved by duplication events occurring in both cases within 2-3 nucleotides following the translational stop codon. The primate mRNAs are also exceptional in that both can form stable stem and loop structures immediately preceding the postulated duplication site that may have played a role in facilitating the mutational events involved. Comparison of the human and monkey protein sequences has revealed regions conserved in primates that are significantly more hydrophobic than their non-primate counterparts. The possible effects of these alterations on the interaction between COII and cytochrome c are discussed.

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