Pheromone-gland-specific fatty-acyl reductase in the adzuki bean borer, Ostrinia scapulalis (Lepidoptera: Crambidae)

Antony, Binu; Fujii, Takeshi; Moto, Ken'ichi; Matsumoto, Shogo; Fukuzawa, Mai; Nakano, Ryo; Tatsuki, Sadahiro; Ishikawa, Yukio

doi:10.1016/j.ibmb.2008.10.008

Cited by 72 publications

(75 citation statements)

References 20 publications

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“…We extracted total RNA using the RNeasy isolation kit (Qiagen) and synthesized first-strand cDNA using Stratascript reverse transcriptase (Stratagene). An ∼290-bp fragment was amplified using pgFAR_F and pgFAR_R primers as previously described (10,39). Gene-specific primers were designed and used in PCRs to amplify the 5′ and 3′ cDNA ends with the SMART RACE amplification kit (Clontech) following the manufacturer's instructions.…”

Section: Methodsmentioning

confidence: 99%

Functional consequences of sequence variation in the pheromone biosynthetic gene pgFAR for Ostrinia moths

Lassance

Liénard

Antony

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Pheromones are central to the mating systems of a wide range of organisms, and reproductive isolation between closely related species is often achieved by subtle differences in pheromone composition. In insects and moths in particular, the use of structurally similar components in different blend ratios is usually sufficient to impede gene flow between taxa. To date, the genetic changes associated with variation and divergence in pheromone signals remain largely unknown. Using the emerging model system Ostrinia, we show the functional consequences of mutations in the protein-coding region of the pheromone biosynthetic fatty-acyl reductase gene pgFAR. Heterologous expression confirmed that pgFAR orthologs encode enzymes exhibiting different substrate specificities that are the direct consequences of extensive nonsynonymous substitutions. When taking natural ratios of pheromone precursors into account, our data reveal that pgFAR substrate preference provides a good explanation of how species-specific ratios of pheromone components are obtained among Ostrinia species. Moreover, our data indicate that positive selection may have promoted the observed accumulation of nonsynonymous amino acid substitutions. Site-directed mutagenesis experiments substantiate the idea that amino acid polymorphisms underlie subtle or drastic changes in pgFAR substrate preference. Altogether, this study identifies the reduction step as a potential source of variation in pheromone signals in the moth genus Ostrinia and suggests that selection acting on particular mutations provides a mechanism allowing pheromone reductases to evolve new functional properties that may contribute to variation in the composition of pheromone signals.

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Section: Methodsmentioning

confidence: 99%

Functional consequences of sequence variation in the pheromone biosynthetic gene pgFAR for Ostrinia moths

Lassance

Liénard

Antony

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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“…A phylogeny of the lepidopteran FAR repertoire was constructed using moth and butterfly FAR genes collected from GenBank, genomic, and EST databases. Twenty-one gene paralogs of the functional B. mori pgFAR gene were found in the silkworm genome database, of which many had homologs in O. nubilalis (17) and its congener O. scapulalis (18) or in various butterfly EST datasets (Fig. 5).…”

Section: Tissue Distribution and Temporal And Diurnal Analysis Of Yevmentioning

confidence: 99%

“…In most species, pheromone production is also regulated by neurohormonal factors that in several cases have been shown to control activation of the reductase system (11,15,16). Despite the presumed central role of FARs in fatty-alcohol pheromone synthesis in moths, very few molecular and functional insights are available, except from the silkworm Bombyx mori (16) and the European corn borer O. nubilalis and its congener Ostrinia scapulalis (17,18). Whereas the pheromone blends of B. mori and Ostrinia spp.…”

mentioning

confidence: 99%

Evolution of multicomponent pheromone signals in small ermine moths involves a single fatty-acyl reductase gene

Liénard

Hagström²,

Lassance³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

112

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Fatty-acyl CoA reductases (FAR) convert fatty acids into fatty alcohols in pro- and eukaryotic organisms. In the Lepidoptera, members of the FAR gene family serve in the biosynthesis of sex pheromones involved in mate communication. We used a group of closely related species, the small ermine moths (Lepidoptera: Yponomeutidae) as a model to investigate the role of FARs in the biosynthesis of complex pheromone blends. Homology-based molecular cloning in three Yponomeuta species led to the identification of multiple putative FAR transcripts homologous to FAR genes from the Bombyx mori genome. The expression of one transcript was restricted to the female pheromone-gland tissue, suggesting a role in pheromone biosynthesis, and the encoded protein belonged to a recently identified Lepidoptera-specific pgFAR gene subfamily. The Yponomeuta evonymellus pgFAR mRNA was up-regulated in sexually mature females and exhibited a 24-h cyclic fluctuation pattern peaking in the pheromone production period. Heterologous expression confirmed that the Yponomeuta pgFAR orthologs in all three species investigated [ Y. evonymellus (L.), Yponomeuta padellus (L.), and Yponomeuta rorellus (Hübner)] encode a functional FAR with a broad substrate range that efficiently promoted accumulation of primary alcohols in recombinant yeast supplied with a series of biologically relevant C14- or C16-acyl precursors. Taken together, our data evidence that a single alcohol-producing pgFAR played a critical function in the production of the multicomponent pheromones of yponomeutids and support the hypothesis of moth pheromone-biosynthetic FARs belonging to a FAR gene subfamily unique to Lepidoptera.

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“…This was an especially surprising finding because reduction of pheromone precursor fatty acids to their corresponding alcohols had been found to be a common step in the biosynthesis of oxygenated sex-pheromone components regardless of the moth species. Although the published pgFAR genes currently in the literature are limited to those of B. mori and Ostrinia scapulalis, 30) our finding implies that pgFARs from different moth species constitute a family of pgFARs of varying substrate specificities. Following our publication, two mammalian FAR isozymes responsible for the synthesis of wax monoesters and ether lipids were identified.…”

Section: Bombykol Biosynthesis Enzymesmentioning

confidence: 74%

Molecular Mechanisms Underlying Sex Pheromone Production in Moths

Matsumoto

2010

Bioscience, Biotechnology, and Biochemistry

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Pheromone-gland-specific fatty-acyl reductase in the adzuki bean borer, Ostrinia scapulalis (Lepidoptera: Crambidae)

Cited by 72 publications

References 20 publications

Functional consequences of sequence variation in the pheromone biosynthetic gene pgFAR for Ostrinia moths

Functional consequences of sequence variation in the pheromone biosynthetic gene pgFAR for Ostrinia moths

Evolution of multicomponent pheromone signals in small ermine moths involves a single fatty-acyl reductase gene

Molecular Mechanisms Underlying Sex Pheromone Production in Moths

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