Common functional elements of Drosophila melanogaster seminal peptides involved in reproduction of Drosophila melanogaster and Helicoverpa armigera females

Common functional elements of Drosophila melanogaster seminal peptides involved in reproduction of Drosophila melanogaster and Helicoverpa armigera females
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DOI:
10.1016/s0965-1748(00)00052-7
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发表时间:
2000-08-01
影响因子:
3.8
通讯作者:
Applebaum, SW
Applebaum, SW
中科院分区:
农林科学2区
文献类型:
--
作者:
Fan, YL;Rafaeli, A;Applebaum, SW

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雄性黑腹果蝇在性腺后复合体中合成性多肽(SP)和射精管多肽(DUP)99b,并在交配过程中通过雄性精液转移到雌性生殖道。对它们进行了测序,并证明它们在C-末端区域具有高度的同源性。两者都会影响雌性黑腹潜蝇随后的交配和产卵。SP还能促进黑腹夜蛾和棉铃虫的体外保幼激素(JH)生物合成。在此,我们报道了黑腹隐翅虫的部分C端肽SP8-36和SP21-36以及截短的N端SP6-20在体外不能刺激两种动物CA的JH生物合成。这两个C端肽都显著减少了JH-III的生物合成。Dup99B在N-末端与SP没有明显的同源性,同样对棉铃虫JH的产生也没有影响。相反,N端肽-SP1-11和SP1-22在体外确实显著激活了两个物种的JH生物合成。我们得出结论,在这些不同的昆虫物种中,前五个N末端氨基酸残基至少是所有刺激所必需的。我们先前已经证明,全长SP1-36在体内和体外都能抑制棉铃虫信息素的生物合成。我们现在发现,全长Dup99B和C端部分序列SP8-36在低浓度下强烈抑制PBAN刺激的棉铃虫信息素生物合成,抑制率为90%。此外,N-端肽SP1-22、较短的N-三端肽SP1-11和截短的N-末端SP6-20在较高浓度下强烈抑制信息素的生物合成。(C)2000爱思唯尔科学有限公司。保留所有权利。
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 SP8-36 and SP21-36 of D. melanogaster, and the truncated N-terminal SP6-20 do nor, 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 - SP1-11 and SP1-22 - 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 SP1-36 depresses pheromone biosynthesis in H. armigera In vivo and in vitro. We now show that full-length Dup99B and the C-terminal partial sequence SP8-36 at low concentrations strongly depress tin the range of 90% inhibition) PBAN-stimulated pheromone biosynthesis of H. armigera. In addition, the N-terminal peptide SP1-22, the shorter N-terninal peptide SP1-11 and the truncated N-terminal SP6-20 strongly inhibit pheromone biosynthesis at higher concentrations. (C) 2000 Elsevier Science Ltd. All rights reserved.