Gradual Release of Sperm Bound Sex-Peptide Controls Female Postmating Behavior in Drosophila

Autor: Jing Peng, Thomas Honegger, Shanjun Chen, Eric Kubli, Susann Büsser, Huanfa Liu
Přispěvatelé: University of Zurich, Kubli, E
Jazyk: angličtina
Předmět:
10127alt Institute of Zoology (former)
Male
musculoskeletal diseases
Proteases
endocrine system
Transgene
Blotting
Western
Molecular Sequence Data
education
Peptide
1100 General Agricultural and Biological Sciences
Cleavage (embryo)
General Biochemistry
Genetics and Molecular Biology
Sexual Behavior
Animal
1300 General Biochemistry
Genetics and Molecular Biology
Hemolymph
medicine
Animals
Drosophila Proteins
Amino Acid Sequence
Transgenes
reproductive and urinary physiology
DNA Primers
chemistry.chemical_classification
Genetics
biology
Agricultural and Biological Sciences(all)
Biochemistry
Genetics and Molecular Biology(all)
urogenital system
biology.organism_classification
Trypsin
beta-Galactosidase
Sperm
Spermatozoa
Cell biology
Drosophila melanogaster
chemistry
Microscopy
Fluorescence
Mutagenesis
Site-Directed
570 Life sciences
590 Animals (Zoology)
Intercellular Signaling Peptides and Proteins
Female
General Agricultural and Biological Sciences
Peptides
medicine.drug
Zdroj: Current Biology. (3):207-213
ISSN: 0960-9822
DOI: 10.1016/j.cub.2005.01.034
Popis: Background: In many female insects, peptides transferred in the seminal fluid induce postmating responses (PMR), such as a drastic increase of egg laying and reduction of receptivity (readiness to mate). In Drosophila melanogaster , sex-peptide (SP) elicits short- and long-term PMR, but only the latter in the presence of stored sperm (sperm effect). Results: Here, we elucidate the interaction between SP and sperm by immunofluorescence microscopy. Transgenic males were used to study the effects of SP modification on the PMR of females in vivo. We report that SP binds to sperm with its N-terminal end. In females, the C-terminal part of SP known to be essential to induce the PMR is gradually released from stored sperm by cleavage at a trypsin cleavage site, thus prolonging the PMR. These findings are confirmed by analyzing the PMR elicited by males containing transgenes encoding modified SPs. SP lacking the N-terminal end cannot bind, and SP without the trypsin cleavage site binds permanently to sperm. Conclusion: By binding to sperm tails, SP prolongs the PMR. Thus, besides a carrier for genetic information, sperm is also the carrier for SP. Binding to sperm may protect the peptide from degradation by proteases in the hemolymph and, thus, prolong its half-life. Longer sperm tails may transfer more SP and thus increase the reproductive fitness of the male. We suggest that this could explain the excessive length of sperm tails in some Drosophila species.
Databáze: OpenAIRE
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