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Functional Coadaptation Between Cytochrome C and Cytochrome C Oxidase Within Allopatric Populations of a Marine Copepod

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Specialty Science
Date 2002 Sep 25
PMID 12271133
Citations 62
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Abstract

Geographically isolated populations may accumulate alleles that function well on their own genetic backgrounds but poorly on the genetic backgrounds of other populations. Consequently, interpopulation hybridization may produce offspring of low fitness as a result of incompatibilities arising in allopatry. Genes participating in these epistatic incompatibility systems remain largely unknown. In fact, despite the widely recognized importance of epistatic interactions among gene products, few data directly address the functional consequences of such interactions among natural genetic variants. In the marine copepod, Tigriopus californicus, we found that the cytochrome c variants isolated from two different populations each had significantly higher activity with the cytochrome c oxidase derived from their respective source population. Three amino acid substitutions in the cytochrome c protein appear to be sufficient to confer population specificity. These results suggest that electron transport system (ETS) proteins form coadapted sets of alleles within populations and that disruption of the coadapted ETS gene complex leads to functional incompatibilities that may lower hybrid fitness.

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References
1.
Roberts V, Pique M . Definition of the interaction domain for cytochrome c on cytochrome c oxidase. III. Prediction of the docked complex by a complete, systematic search. J Biol Chem. 1999; 274(53):38051-60. DOI: 10.1074/jbc.274.53.38051. View

2.
Turelli M, Orr H . Dominance, epistasis and the genetics of postzygotic isolation. Genetics. 2000; 154(4):1663-79. PMC: 1461023. DOI: 10.1093/genetics/154.4.1663. View

3.
Rawson P, Brazeau D, Burton R . Isolation and characterization of cytochrome c from the marine copepod Tigriopus californicus. Gene. 2000; 248(1-2):15-22. DOI: 10.1016/s0378-1119(00)00145-1. View

4.
Barrientos A, Muller S, Dey R, Wienberg J, Moraes C . Cytochrome c oxidase assembly in primates is sensitive to small evolutionary variations in amino acid sequence. Mol Biol Evol. 2000; 17(10):1508-19. DOI: 10.1093/oxfordjournals.molbev.a026250. View

5.
Wu W, Schmidt T, Goodman M, Grossman L . Molecular evolution of cytochrome c oxidase subunit I in primates: is there coevolution between mitochondrial and nuclear genomes?. Mol Phylogenet Evol. 2000; 17(2):294-304. DOI: 10.1006/mpev.2000.0833. View