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Proc Natl Acad Sci U S A


Title:Functional consequences of sequence variation in the pheromone biosynthetic gene pgFAR for Ostrinia moths
Author(s):Lassance JM; Lienard MA; Antony B; Qian S; Fujii T; Tabata J; Ishikawa Y; Lofstedt C;
Address:"Department of Biology, Lund University, SE-22362 Lund, Sweden. lassance@fas.harvard.edu"
Journal Title:Proc Natl Acad Sci U S A
Year:2013
Volume:20130213
Issue:10
Page Number:3967 - 3972
DOI: 10.1073/pnas.1208706110
ISSN/ISBN:1091-6490 (Electronic) 0027-8424 (Print) 0027-8424 (Linking)
Abstract:"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"
Keywords:"Amino Acid Sequence Animals Female *Genes, Insect Genetic Variation Insect Proteins/genetics/metabolism Male Metabolic Networks and Pathways Molecular Sequence Data Moths/*genetics/*metabolism Mutagenesis, Site-Directed Mutation Oxidoreductases/genetics/m;"
Notes:"MedlineLassance, Jean-Marc Lienard, Marjorie A Antony, Binu Qian, Shuguang Fujii, Takeshi Tabata, Jun Ishikawa, Yukio Lofstedt, Christer eng Research Support, Non-U.S. Gov't 2013/02/15 Proc Natl Acad Sci U S A. 2013 Mar 5; 110(10):3967-72. doi: 10.1073/pnas.1208706110. Epub 2013 Feb 13"

 
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Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
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