Conserved molecular mechanism for the stage specificity of the mosquito vitellogenic response to ecdysone

被引:51
作者
Li, C
Kapitskaya, MZ
Zhu, J
Miura, K
Segraves, W
Raikhel, AS [1 ]
机构
[1] Michigan State Univ, Genet Program, E Lansing, MI 48824 USA
[2] Michigan State Univ, Dept Entomol, E Lansing, MI 48824 USA
[3] Yale Univ, Dept Mol Cellular & Dev Biol, New Haven, CT 06520 USA
关键词
20-hydroxyecdysone; ecdysone; developmental competence; nuclear receptor; early gene; FTZ-F1; vitellogenesis; mosquito;
D O I
10.1006/dbio.2000.9792
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
In the mosquito Aedes aegypti, the adult female becomes competent for a vitellogenic response to ecdysone after previtellogenic development. Here, we show that beta FTZ-F1, the nuclear receptor implicated as a competence factor for stage-specific responses to ecdysone during Drosophila metamorphosis, serves a similar function during mosquito vitellogenesis. AaFTZ-F1 is expressed highly in the mosquito fat body during pre- and postvitellogenic periods when ecdysteroid titers are low. The mosquito AaFTZ-F1 transcript nearly disappears in mid-vitellogenesis when ecdysteroid titers are high. An expression peak of HR3, a nuclear receptor implicated in the activation of beta FTZ-P1 in Drosophila, precedes each rise in mosquito FTZ-F1 expression. In in vitro fat body culture, AaFTZ-F1 expression is inhibited by 20-hydroxyecdysone (20E) and superactivated by its withdrawal. Following in vitro AaFTZ-F1 superactivation, a secondary 20E challenge results in superinduction of the early AaE75 gene and the late target VCP gene. Electrophoretic mobility-shift assays show that the onset of ecdysone-response competence in the mosquito fat body is correlated with the appearance of the functional AeFTZ-F1 protein at the end of the previtellogenic development. These findings suggest that a conserved molecular mechanism for controlling stage specificity is reiteratively used during metamorphic and reproductive responses to ecdysone. (C) 2000 Academic Press.
引用
收藏
页码:96 / 110
页数:15
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