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The Drosophila melanogaster Seminal Fluid Protein Acp62F Is a Protease Inhibitor That Is Toxic Upon Ectopic Expression
Oliver Lunga, Uyen Trama, Casey M. Finnertya, Marcie A. Eipper-Mainsa, John M. Kalba, and Mariana F. Wolfneraa Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853
Corresponding author: Mariana F. Wolfner, 423 Biotechnology Bldg., Cornell University, Ithaca, NY 14853., mfw5{at}cornell.edu (E-mail)
Communicating editor: C.-I WU
10% enters the circulatory system while
90% remains in the reproductive tract. We show that in the reproductive tract, Acp62F localizes to the lumen of the uterus and the female's sperm storage organs. Analysis of Acp62F's sequence, and biochemical assays, reveals that it encodes a trypsin inhibitor with sequence and structural similarities to extracellular serine protease inhibitors from the nematode Ascaris. In light of previous results demonstrating entry of Acp62F into the mated female's hemolymph, we propose that Acp62F is a candidate for a molecule to contribute to the Acp-dependent decrease in female life span. We propose that Acp62F's protease inhibitor activity exerts positive protective functions in the mated female's reproductive tract but that entry of a small amount of this protein into the female's hemolymph could contribute to the cost of mating.
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