Molecular evolution of the cytochrome c oxidase subunit <it>5</it>A gene in primates

<p>Abstract</p> <p>Background</p> <p>Many electron transport chain (ETC) genes show accelerated rates of nonsynonymous nucleotide substitutions in anthropoid primate lineages, yet in non-anthropoid lineages the ETC proteins are typically highly conserved. Here, we test...

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Main Authors: Wildman Derek E, Opazo Juan C, Uddin Monica, Sherwood Chet C, Hof Patrick R, Goodman Morris, Grossman Lawrence I
Format: Article
Language:English
Published: BMC 2008-01-01
Series:BMC Evolutionary Biology
Online Access:http://www.biomedcentral.com/1471-2148/8/8
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author Wildman Derek E
Opazo Juan C
Uddin Monica
Sherwood Chet C
Hof Patrick R
Goodman Morris
Grossman Lawrence I
author_facet Wildman Derek E
Opazo Juan C
Uddin Monica
Sherwood Chet C
Hof Patrick R
Goodman Morris
Grossman Lawrence I
author_sort Wildman Derek E
collection DOAJ
description <p>Abstract</p> <p>Background</p> <p>Many electron transport chain (ETC) genes show accelerated rates of nonsynonymous nucleotide substitutions in anthropoid primate lineages, yet in non-anthropoid lineages the ETC proteins are typically highly conserved. Here, we test the hypothesis that <it>COX5A</it>, the ETC gene that encodes cytochrome <it>c </it>oxidase subunit 5A, shows a pattern of anthropoid-specific adaptive evolution, and investigate the distribution of this protein in catarrhine brains.</p> <p>Results</p> <p>In a dataset comprising 29 vertebrate taxa, including representatives from all major groups of primates, there is nearly 100% conservation of the <it>COX5A </it>amino acid sequence among extant, non-anthropoid placental mammals. The most recent common ancestor of these species lived about 100 million years (MY) ago. In contrast, anthropoid primates show markedly elevated rates of nonsynonymous evolution. In particular, branch site tests identify five positively selected codons in anthropoids, and ancestral reconstructions infer that substitutions in these codons occurred predominantly on stem lineages (anthropoid, ape and New World monkey) and on the human terminal branch. Examination of catarrhine brain samples by immunohistochemistry characterizes for the first time COX5A protein distribution in the primate neocortex, and suggests that the protein is most abundant in the mitochondria of large-size projection neurons. Real time quantitative PCR supports previous microarray results showing <it>COX5A </it>is expressed in cerebral cortical tissue at a higher level in human than in chimpanzee or gorilla.</p> <p>Conclusion</p> <p>Taken together, these results suggest that both protein structural and gene regulatory changes contributed to <it>COX5A </it>evolution during humankind's ancestry. Furthermore, these findings are consistent with the hypothesis that adaptations in ETC genes contributed to the emergence of the energetically expensive anthropoid neocortex.</p>
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spelling doaj.art-badd94f5a6054c02b242ee5973d30f812022-12-21T20:47:54ZengBMCBMC Evolutionary Biology1471-21482008-01-0181810.1186/1471-2148-8-8Molecular evolution of the cytochrome c oxidase subunit <it>5</it>A gene in primatesWildman Derek EOpazo Juan CUddin MonicaSherwood Chet CHof Patrick RGoodman MorrisGrossman Lawrence I<p>Abstract</p> <p>Background</p> <p>Many electron transport chain (ETC) genes show accelerated rates of nonsynonymous nucleotide substitutions in anthropoid primate lineages, yet in non-anthropoid lineages the ETC proteins are typically highly conserved. Here, we test the hypothesis that <it>COX5A</it>, the ETC gene that encodes cytochrome <it>c </it>oxidase subunit 5A, shows a pattern of anthropoid-specific adaptive evolution, and investigate the distribution of this protein in catarrhine brains.</p> <p>Results</p> <p>In a dataset comprising 29 vertebrate taxa, including representatives from all major groups of primates, there is nearly 100% conservation of the <it>COX5A </it>amino acid sequence among extant, non-anthropoid placental mammals. The most recent common ancestor of these species lived about 100 million years (MY) ago. In contrast, anthropoid primates show markedly elevated rates of nonsynonymous evolution. In particular, branch site tests identify five positively selected codons in anthropoids, and ancestral reconstructions infer that substitutions in these codons occurred predominantly on stem lineages (anthropoid, ape and New World monkey) and on the human terminal branch. Examination of catarrhine brain samples by immunohistochemistry characterizes for the first time COX5A protein distribution in the primate neocortex, and suggests that the protein is most abundant in the mitochondria of large-size projection neurons. Real time quantitative PCR supports previous microarray results showing <it>COX5A </it>is expressed in cerebral cortical tissue at a higher level in human than in chimpanzee or gorilla.</p> <p>Conclusion</p> <p>Taken together, these results suggest that both protein structural and gene regulatory changes contributed to <it>COX5A </it>evolution during humankind's ancestry. Furthermore, these findings are consistent with the hypothesis that adaptations in ETC genes contributed to the emergence of the energetically expensive anthropoid neocortex.</p>http://www.biomedcentral.com/1471-2148/8/8
spellingShingle Wildman Derek E
Opazo Juan C
Uddin Monica
Sherwood Chet C
Hof Patrick R
Goodman Morris
Grossman Lawrence I
Molecular evolution of the cytochrome c oxidase subunit <it>5</it>A gene in primates
BMC Evolutionary Biology
title Molecular evolution of the cytochrome c oxidase subunit <it>5</it>A gene in primates
title_full Molecular evolution of the cytochrome c oxidase subunit <it>5</it>A gene in primates
title_fullStr Molecular evolution of the cytochrome c oxidase subunit <it>5</it>A gene in primates
title_full_unstemmed Molecular evolution of the cytochrome c oxidase subunit <it>5</it>A gene in primates
title_short Molecular evolution of the cytochrome c oxidase subunit <it>5</it>A gene in primates
title_sort molecular evolution of the cytochrome c oxidase subunit it 5 it a gene in primates
url http://www.biomedcentral.com/1471-2148/8/8
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