Molecular Biology and Evolution, Vol 14, 595-601, Copyright © 1997 by Society for Molecular Biology and Evolution
TR Schmidt, SA Jaradat, M Goodman, MI Lomax and LI Grossman
Cytochrome c oxidase (COX) consists of 13 subunits, 3 encoded in the
mitochondrial genome and 10 in the nucleus. Little is known of the role of
the nuclear-encoded subunits, some of which exhibit tissue-specific
isoforms. Subunit VIa is unique in having tissue-specific isoforms in all
mammalian species examined. We examined relative evolutionary rates for the
COX6A heart (H) and liver (L) isoform genes along the length of the
molecule, specifically in relation to the tissue-specific function(s) of
the two isoforms. Nonsynonymous (amino acid replacement) substitutions in
the COX6AH gene occurred more frequently than in the ubiquitously expressed
COX6AL gene. Maximum-parsimony analysis and sequence divergences from
reconstructed ancestral sequences revealed that after the ancestral COX6A
gene duplicated to yield the genes for the H and L isoforms, the sequences
encoding the mitochondrial matrix region of the COX VIa protein experienced
an elevated rate of nonsynonymous substitutions relative to synonymous
substitutions. This is expected for relaxed selective constraints after
gene duplication followed by purifying selection to preserve the
replacements with tissue-specific functions.
ORIGINAL ARTICLE
Molecular evolution of cytochrome c oxidase: rate variation among subunit VIa isoforms
Center for Molecular Medicine and Genetics, Wayne State University School of Medicine, Detroit, Michigan 48201, USA.
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