Title of article :
Molecular mechanisms underlying sex pheromone production in the silkmoth, Bombyx mori: Characterization of the molecular components involved in bombykol biosynthesis
Author/Authors :
Matsumoto، نويسنده , , Shogo and Joe Hull، نويسنده , , J. and Ohnishi، نويسنده , , Atsushi and Moto، نويسنده , , Ken’ichi and F?nagy، نويسنده , , Adrien، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2007
Abstract :
Many species of female moths produce sex pheromones to attract conspecific males. To date, sex pheromones from more than 570 moth species have been chemically identified. Most moth species utilize Type I pheromones that consist of straight-chain compounds 10–18 carbons in length with a functional group of a primary alcohol, aldehyde, or acetate ester and usually with several double bonds. In contrast, some moth species use unsaturated hydrocarbons or hydrocarbon epoxides, classified as Type II lepidopteran pheromones, as sex pheromones. Studies over the past three decades have demonstrated that female moths usually produce sex pheromones as multi-component blends where the ratio of the individual components is precisely controlled, thus making it possible to generate species-specific pheromone blends. As for the biosynthesis of Type I pheromones, it is well established that they are de novo synthesized in the pheromone gland (PG) through modifications of fatty acid biosynthetic pathways. However, as many of the molecular components within the PG cells (i.e., enzymes, proteins, and small regulatory molecules) have not been functionally characterized, the molecular mechanisms underlying sex pheromone production in PG cells remain poorly understood. To address this, we have recently characterized some of the molecules involved in the biosynthesis of the sex pheromone bombykol in the silkmoth, Bombyx mori. Characterization of these, and other, key molecules will facilitate our understanding of the precise mechanisms underlying lepidopteran sex pheromone production.
Keywords :
DESATURASE , Fatty acyl reductase , Lipid droplets , PBAN receptor , RNAi
Journal title :
Journal of Insect Physiology
Journal title :
Journal of Insect Physiology