Sex pheromone desaturase functioning in a primitive Ostrinia moth is cryptically conserved in congeners' genomes

Sex pheromone desaturase functioning in a primitive Ostrinia moth is cryptically conserved in congeners' genomes
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DOI:
10.1073/pnas.1019519108
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发表时间:
2011-04-26
影响因子:
11.1
通讯作者:
Ishikawa, Yukio
Ishikawa, Yukio
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Fujii, Takeshi;Ito, Katsuhiko;Ishikawa, Yukio

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(E)-11-和(Z)-11-十四烯基乙酸酯是玉米蛾最常见的雌虫性信息素成分。雌蛾信息素腺体中表达的Delta 11-去饱和酶是信息素分子中引入双键的关键酶。玉米螟的单一Delta 11-去饱和酶OnubZ/E11已被证明从底物十四酸中产生类似于7:3的(E)-11-和(Z)-11-十四烯酸混合物。而亚洲玉米蛾的性信息素为(E)-11-十四烯醇,为玉米螟的原始种。这种信息素是独一无二的,因为它不是乙酰化的,也不包括Z异构体。在本研究中,我们通过克隆和功能分析的PG专一性的Delta11-去饱和酶,我们发现在信息素中缺乏Z异构体是由于该物种Delta11-去饱和酶LATPG1具有严格的产物专一性。系统发育分析表明,LATPG1与OnubZ/E11的亲缘关系不密切。相反,它与在亚洲玉米象和亚洲玉米螟基因组中发现的与反转录病毒连锁的隐蔽Delta 11-脱饱和酶(ezi-Delta 11)密切相关。综上所述,结果表明,一种不寻常的Delta 11-去饱和酶在宽边野生稻中得到了功能表达,尽管编码这种酶的基因在同系物中似乎是隐蔽的。
(E)-11- and (Z)-11-tetradecenyl acetate are the most common female sex pheromone components in Ostrinia moths. The Delta 11-desaturase expressed in the pheromone gland (PG) of female moths is a key enzyme that introduces a double bond into pheromone molecules. A single Delta 11-desaturase of Ostrinia nubilalis, OnubZ/E11, has been shown to produce an similar to 7: 3 mixture of (E)-11- and (Z)-11-tetradecenoate from the substrate tetradecanoate. In contrast, the sex pheromone of Ostrinia latipennis, a primitive species of Ostrinia, is (E)-11-tetradecenol. This pheromone is unique in that it is not acetylated, and includes no Z isomer. In the present study, through the cloning and functional analysis of a PG-specific Delta 11-desaturase in O. latipennis, we showed that the absence of the Z isomer in the pheromone is attributable to the strict product specificity of the Delta 11-desaturase in this species, LATPG1. Phylogenetic analysis revealed that LATPG1 was not closely related to OnubZ/E11. Rather, it was closely related to retroposon-linked cryptic Delta 11-desaturases (ezi-Delta 11) found in the genomes of O. nubilalis and Ostrinia furnacalis. Taken together, the results showed that an unusual Delta 11-desaturase is functionally expressed in O. latipennis, although the genes encoding this enzyme appear to be cryptic in congeners.