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doi:10.1534/genetics.105.051011
A more recent version of this article appeared on July 1, 2006.
REGULAR RESEARCH PAPERS |
Deleterious Epistatic Interactions Between Electron Transport System Protein-Coding Loci in the Copepod Tigriopus californicus
Christopher Scott Willett 1*
1 UNC Chapel Hill
* To whom correspondence should be addressed. E-mail: willett4{at}email.unc.edu.
Submitted on September 12, 2005
Revised on November 10, 2005
Accepted on 12 April 2006
The nature of epistatic interactions between genes encoding interacting proteins in hybrid organisms can have important implications for the evolution of postzygotic reproductive isolation and speciation. At this point very little is known about the fitness differences caused by specific closely interacting but evolutionarily divergent proteins in hybrids between populations or species. The intertidal copepod Tigriopus californicus provides an excellent model in which to study such interactions because the species range includes numerous genetically divergent populations that are still capable of being crossed in the laboratory. Here, the effect on fitness due to the interactions of three complex III proteins of the electron transport system in F2 hybrid copepods resulting from crosses of a pair of divergent populations is examined. Significant deviations from Mendelian inheritance are observed for each of the three genes in F2 hybrid adults but not nauplii (larvae). The two-way interactions between these genes also have a significant impact upon the viability of these hybrid copepods. Dominance appears to play an important role in mediating the interactions between these loci as deviations are caused by heterozygote/homozygote deleterious interactions. These results suggest that the fitness consequences of the interactions of these three complex III-associated genes could influence reproductive isolation in this system.
Key Words: Dobzhansky-Muller incompatibilities, Postzygotic reproductive isolation, cytochrome c1, rieske iron-sulfur protein, ubiquinol/cytochrome c oxioreductase
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