ArticleJournal of bioenergetics and biomembranes2005
Rapid nonsynonymous evolution of the iron-sulfur protein in anthropoid primates.
Article in Journal of bioenergetics and biomembranes, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 9 citations in OpenAlex.
- The evolution of the human mitochondrial bc1 complex- adaptation for reduced rate of superoxide production?Journal of bioenergetics and biomembranes · 2023Article
- Exceptional longevity and exceptionally high metabolic rates in anthropoid primates are linked to a major modification of the ubiquinone reduction site of cytochrome b.Journal of bioenergetics and biomembranes · 2014Article
- Evolution of the couple cytochrome c and cytochrome c oxidase in primates.Advances in experimental medicine and biology · 2012Review
- Silencing, positive selection and parallel evolution: busy history of primate cytochromes C.PloS one · 2011Article
- Conservation and evolution of gene coexpression networks in human and chimpanzee brains.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Cytochrome c (CYC) and 9 of the 13 subunits of cytochrome c oxidase (complex IV; COX) were previously shown to have accelerated rates of nonsynonymous substitution in anthropoid primates. Cytochrome b, the mtDNA encoded subunit of ubiquinol-cytochrome c reductase (complex III), also showed an accelerated nonsynonymous substitution rate in anthropoid primates but rate information about the nuclear encoded subunits of complex III has been lacking. We now report that phylogenetic and relative rates analysis of a nuclear encoded catalytically active subunit of complex III, the iron-sulfur protein (ISP), shows an accelerated rate of amino acid replacement similar to cytochrome b. Because both ISP and subunit 9, whose function is not directly related to electron transport, are produced by cleavage into two subunits of the initial translation product of a single gene, it is probable that these two subunits of complex III have essentially identical underlying rates of mutation. Nevertheless, we find that the catalytically active ISP has an accelerated rate of amino acid replacement in anthropoid primates whereas the catalytically inactive subunit 9 does not.
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Registered trials
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