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Accelerated evolution of the electron transport chain in anthropoid primates
Abstract
Mitochondria are both the power plant of the cell and a central integrator of signals that govern the lifespan, replication and death of the cell. Perhaps as a consequence, genes that encode components of the mitochondrial electron transport chain (ETC) are generally conserved. Therefore, it is surprising that many of these genes in anthropoid primates (New World monkeys, Old World monkeys and apes, including humans) have been major targets of darwinian positive selection. Sequence comparisons have provided evidence that marked increases of non-synonymous substitution rates occurred in anthropoid ETC genes that encode subunits of Complex III and IV, and the electron carrier molecule cytochrome c (CYC). Two important questions are: (i) how has evolution altered ETC function? and; (ii) how might functional changes in the ETC be linked to evolution of an expanded neocortical brain?
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“Furthermore, evidence for positive selection in the human lineage for genes that encode components of the mitochondrial electron-transport chain suggests that there has been evolutionary pressure for high rates of aerobic energy consumption in metabolically active cells, such as neurons (6).”
From Evolution of increased glia–neuron ratios in the human frontal cortex (2006) · cites this paper as [6]
In the citing paper
“Second, the process of mitochondrial electron transport shows accelerated evolution of multiple subunits of complex III, complex IV, and cytochrome c (6, 38), suggesting that the engine of energy generation has been a prominent target of Darwinian positive selection in anthropoid primates.”
From Evolution of increased glia–neuron ratios in the human frontal cortex (2006) · cites this paper as [6]
In the citing paper
“Second, the process of mitochondrial electron transport shows accelerated evolution of multiple subunits of complex III, complex IV, and cytochrome c (6, 38), suggesting that the engine of energy generation has been a prominent target of Darwinian positive selection in anthropoid primates.”
From Evolution of increased glia–neuron ratios in the human frontal cortex (2006) · cites this paper as [6]
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“Indeed, considerable evidence indicates that the biochemical mechanism of generating energy has been under evolutionary selection going back at least to the anthropoid primate stem, presumably to fuel increases in brain size.”
From Evolution of increased glia–neuron ratios in the human frontal cortex (2006) · cites this paper as [6]
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Metadata
- Authors
- Grossman, L. I., Wildman, D. E., Schmidt, T. R., & Goodman, M.
- Affiliations
- Wayne State University (US)
- Corresponding author
- Grossman, Lawrence I.
- Venue
- Trends in Genetics
- Publisher
- Elsevier BV
- Published
- 2004-11
- Volume
- 20
- Issue
- 11
- Pages
- 578-585
- ISSN
- 0168-9525 (ISSN-L)
- OpenAlex
- W2006786379
- Cited by
- 186
- References
- 74
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 3 · 2023: 3 · 2022: 8 · 2021: 7 · 2020: 4 · 2019: 2 · 2018: 6 · 2017: 6 · 2016: 10 · 2015: 7 · 2014: 13 · 2013: 19 · 2012: 9
- FWCI
- 3.32
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Genetics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Evolution and Genetic Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
- Keywords
- electron transport chain, mitochondrial evolution, anthropoid primates, positive selection, nonsynonymous substitution rate, cytochrome bc1 complex, cytochrome c oxidase, cytochrome c, brain evolution, neocortex, human evolution
- MeSH terms
- Animals, Haplorhini, Electron Transport Complex IV, Humans, Phylogeny, Electron Transport Complex III, Evolution, Molecular, Electron Transport Chain Complex Proteins
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