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MBE Advance Access published online on June 22, 2009
Molecular Biology and Evolution, doi:10.1093/molbev/msp121
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© The Author 2009. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Research Article

Protease Gene Duplication and Proteolytic Activity in Drosophila Female Reproductive Tracts

Erin S. Kelleher1,2,* and James E. Pennington3

1 Department of Ecology and Evolutionary Biology, University of Arizona, Tucson, AZ 85721
2 Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853
3 Department of Biochemistry and Molecular Biophysics, Center for Insect Science, University of Arizona, Tucson, AZ 85721

* to whom correspondence should be addressed: esk72{at}cornell.edu, Phone: (607) 254-4569, Fax: (607) 255-6249

Received for publication March 18, 2009. Revision received May 20, 2009. Accepted for publication June 12, 2009.

Secreted proteases play integral roles in sexual reproduction in a broad range of taxa. In the genetic model Drosophila melanogaster, these molecules are thought to process peptides and activate enzymes inside female reproductive tracts, mediating critical post-mating responses. A recent study of female reproductive tract proteins in the cactophilic fruit-fly D. arizonae, identified pervasive, lineage-specific gene duplication amongst secreted proteases. Here we compare the evolutionary dynamics, biochemical nature, and physiological significance of secreted female reproductive serine endoproteases (SFRSEs) between D. arizonae and its congener D. melanogaster. We show that D. arizonae lower female reproductive tract (LFRT) proteins are significantly enriched for recently-duplicated secreted proteases, particularly serine endoproteases, relative to D. melanogaster. Isolated lumen from D. arizonae LFRTs, furthermore, exhibits significant tryspin-like and elastase-like serine endoprotease acitivity, while no such activity is seen in D. melanogaster. Finally, trypsin and elastase-like activity in D. arizonae female reproductive tracts is negatively regulated by mating. We propose that the intense proteolytic environment of the D. arizonae female reproductive tract relates to the extraordinary reproductive physiology of this species, and that ongoing gene duplication amongst these proteases is an evolutionary consequence of sexual conflict.

Key Words: Gene Duplication • Protease • Reproductive Protein • Female Reproductive Tract • Sexual Conflict


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