Source:http://linkedlifedata.com/resource/pubmed/id/11018157
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
2000-11-13
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pubmed:abstractText |
Respiring mitochondria require many interactions between nuclear and mitochondrial genomes. Although mitochondrial DNA (mtDNA) from the gorilla and the chimpanzee are able to restore oxidative phosphorylation in a human cell, mtDNAs from more distant primate species are functionally incompatible with human nuclear genes. Using microcell-mediated chromosome and mitochondria transfer, we introduced and maintained a functional orangutan mtDNA in a human nuclear background. However, partial oxidative phosphorylation function was restored only in the presence of most orangutan chromosomes, suggesting that human oxidative phosphorylation-related nuclear-coded genes are not able to replace many orangutan ones. The respiratory capacity of these hybrids was decreased by 65%-80%, and cytochrome c oxidase (COX) activity was decreased by 85%-95%. The function of other respiratory complexes was not significantly altered. The translation of mtDNA-coded COX subunits was normal, but their steady-state levels were approximately 10% of normal ones. Nuclear-coded COX subunits were loosely associated with mitochondrial membranes, a characteristic of COX assembly-defective mutants. Our results suggest that many human nuclear-coded genes not only cannot replace the orangutan counterparts, but also exert a specific interference at the level of COX assembly. This cellular model underscores the precision of COX assembly in mammals and sheds light on the nature of nuclear-mtDNA coevolutionary constraints.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0737-4038
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1508-19
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11018157-Animals,
pubmed-meshheading:11018157-Cell Fusion,
pubmed-meshheading:11018157-Cell Nucleus,
pubmed-meshheading:11018157-Chick Embryo,
pubmed-meshheading:11018157-Electron Transport Complex IV,
pubmed-meshheading:11018157-Evolution, Molecular,
pubmed-meshheading:11018157-Gorilla gorilla,
pubmed-meshheading:11018157-Haplorhini,
pubmed-meshheading:11018157-Hominidae,
pubmed-meshheading:11018157-Humans,
pubmed-meshheading:11018157-Hybrid Cells,
pubmed-meshheading:11018157-In Situ Hybridization, Fluorescence,
pubmed-meshheading:11018157-Karyotyping,
pubmed-meshheading:11018157-Mitochondria,
pubmed-meshheading:11018157-Oxidative Phosphorylation,
pubmed-meshheading:11018157-Pongo pygmaeus,
pubmed-meshheading:11018157-Species Specificity
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pubmed:year |
2000
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pubmed:articleTitle |
Cytochrome c oxidase assembly in primates is sensitive to small evolutionary variations in amino acid sequence.
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pubmed:affiliation |
Department of Neurology, University of Miami, School of Medicine, Miami, FL 33136, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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