4.6 Article

A novel terpene synthase controls differences in anti-aphrodisiac pheromone production between closely related Heliconius butterflies

Journal

PLOS BIOLOGY
Volume 19, Issue 1, Pages -

Publisher

PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pbio.3001022

Keywords

-

Funding

  1. Natural Research Council Doctoral Training Partnership [NE/L002507/1]
  2. Smithsonian Tropical Research Institute Short Term Fellowship
  3. European Research Council [339873]
  4. Deutsche Forschungsgemeinschaft Emmy Noether fellowship [GZ:ME4845/1-1]
  5. Jane and Aatos Erkko Foundation
  6. Natural Research Council studentship [PFZE/063]
  7. Herchel Smith Postdoctoral Research Fellowship
  8. Smithsonian Tropical Research Institute Fellowship
  9. Smithsonian Tropical Research Institute
  10. National Science Foundation [DEB 1257689]
  11. Deutsche Forschungsgemeinschaft [Schu984/12-1]

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This study investigated the recent divergence of two species, H. melpomene and Heliconius cydno, in terms of the presence of (E)-beta-ocimene. Through linkage mapping, gene expression, and functional analyses, two novel TPS enzymes were identified, demonstrating independent evolutionary origins of chemical convergence. The research showed that the loss of (E)-beta-ocimene in H. cydno was due to coding, not regulatory, differences.
Plants and insects often use the same compounds for chemical communication, but not much is known about the genetics of convergent evolution of chemical signals. The terpene (E)-beta-ocimene is a common component of floral scent and is also used by the butterfly Heliconius melpomene as an anti-aphrodisiac pheromone. While the biosynthesis of terpenes has been described in plants and microorganisms, few terpene synthases (TPSs) have been identified in insects. Here, we study the recent divergence of 2 species, H. melpomene and Heliconius cydno, which differ in the presence of (E)-beta-ocimene; combining linkage mapping, gene expression, and functional analyses, we identify 2 novel TPSs. Furthermore, we demonstrate that one, HmelOS, is able to synthesise (E)-beta-ocimene in vitro. We find no evidence for TPS activity in HcydOS (HmelOS ortholog of H. cydno), suggesting that the loss of (E)-beta-ocimene in this species is the result of coding, not regulatory, differences. The TPS enzymes we discovered are unrelated to previously described plant and insect TPSs, demonstrating that chemical convergence has independent evolutionary origins.

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