Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractDrosophila melanogaster sex peptide stimulates juvenile hormone synthesis and depresses sex pheromone production in Helicoverpa armigera    Next AbstractLipophorin-facilitated hydrocarbon uptake by oocytes in the German cockroach Blattella germanica (L.) »

Insect Biochem Mol Biol


Title:Common functional elements of Drosophila melanogaster seminal peptides involved in reproduction of Drosophila melanogaster and Helicoverpa armigera females
Author(s):Fan Y; Rafaeli A; Moshitzky P; Kubli E; Choffat Y; Applebaum SW;
Address:"Department of Entomology, The Hebrew University, P.O. Box 12, 76100, Rehovot, Israel"
Journal Title:Insect Biochem Mol Biol
Year:2000
Volume:30
Issue:8-Sep
Page Number:805 - 812
DOI: 10.1016/s0965-1748(00)00052-7
ISSN/ISBN:0965-1748 (Print) 0965-1748 (Linking)
Abstract:"Sex peptide (SP) and Ductus ejaculatorius peptide (Dup) 99B are synthesized in the retrogonadal complex of adult male Drosophila melanogaster, and are transferred in the male seminal fluid to the female genital tract during mating. They have been sequenced and shown to exhibit a high degree of homology in the C-terminal region. Both affect subsequent mating and oviposition by female D. melanogaster. SP also increases in vitro juvenile hormone (JH) biosynthesis in excised corpora allata (CA) of D. melanogaster and Helicoverpa armigera. We herein report that the partial C-terminal peptides SP(8-36) and SP(21-36) of D. melanogaster, and the truncated N-terminal SP(6-20) do not stimulate JH biosynthesis in vitro in CA of both species. Both of these C-terminal peptides reduce JH-III biosynthesis significantly. Dup99B, with no appreciable homology to SP in the N-terminal region, similarly lacks an effect on JH production by H. armigera CA. In contrast, the N-terminal peptides - SP(1-11) and SP(1-22) - do significantly activate JH biosynthesis of both species in vitro. We conclude that the first five N-terminal amino acid residues at the least, are essential for allatal stimulation in these disparate insect species. We have previously shown that the full-length SP(1-36) depresses pheromone biosynthesis in H. armigera in vivo and in vitro. We now show that full-length Dup99B and the C-terminal partial sequence SP(8-36) at low concentrations strongly depress (in the range of 90% inhibition) PBAN-stimulated pheromone biosynthesis of H. armigera. In addition, the N-terminal peptide SP(1-22), the shorter N-terminal peptide SP(1-11) and the truncated N-terminal SP(6-20) strongly inhibit pheromone biosynthesis at higher concentrations"
Keywords:Amino Acid Sequence Animals Drosophila melanogaster/*physiology Female Gonadal Steroid Hormones/biosynthesis/chemistry/*physiology Juvenile Hormones/biosynthesis Male Molecular Sequence Data Moths/*physiology Peptides/chemistry/*physiology Reproduction/ph;
Notes:"MedlineFan, Y Rafaeli, A Moshitzky, P Kubli, E Choffat, Y Applebaum, S W eng Research Support, Non-U.S. Gov't England 2000/07/06 Insect Biochem Mol Biol. 2000 Aug-Sep; 30(8-9):805-12. doi: 10.1016/s0965-1748(00)00052-7"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 19-12-2024