Abstract

BackgroundChrysanthemyl diphosphate synthase (CDS) is a key enzyme in biosynthetic pathways producing pyrethrins and irregular monoterpenes. These compounds are confined to plants of the tribe Anthemideae of the Asteraceae, and play an important role in defending the plants against herbivorous insects. It has been proposed that the CDS genes arose from duplication of the farnesyl diphosphate synthase (FDS) gene and have different function from FDSs. However, the duplication time toward the origin of CDS and the evolutionary force behind the functional divergence of the CDS gene are still unknown.ResultsTwo duplication events were detected in the evolutionary history of the FDS gene family in the Asteraceae, and the second duplication led to the origin of CDS. CDS occurred after the divergence of the tribe Mutisieae from other tribes of Asteraceae but before the birth of the Anthemideae tribe. After its origin, CDS accumulated four mutations in sites homologous to the substrate-binding and catalysis sites of FDS. Of these, two sites were involved in the binding of the nucleophilic substrate isopentenyl diphosphate in FDS. Maximum likelihood analyses showed that some sites in CDS were under positive selection and were scattered throughout primary sequences, whereas in the three-dimensional structure model they clustered in the large central cavity.ConclusionPositive selection associated with gene duplication played a major role in the evolution of CDS.

Highlights

  • Chrysanthemyl diphosphate synthase (CDS) is a key enzyme in biosynthetic pathways producing pyrethrins and irregular monoterpenes

  • Because CDS carries out the production of irregular monoterpenes that are important secondary metabolites for defense against herbivorous insects in Anthemideae, we investigated whether the functional divergence of CDS was driven by positive selection

  • With the exception of the A. ageratoides cCDS, which included a large indel in the N-terminal, the cCDS sequences varied in length from 1330 to 1430 bp, with the ORF having a length of 1182 to 1197 bp, encoding proteins of 394 to 399 amino-acids

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Summary

Introduction

Chrysanthemyl diphosphate synthase (CDS) is a key enzyme in biosynthetic pathways producing pyrethrins and irregular monoterpenes. These compounds are confined to plants of the tribe Anthemideae of the Asteraceae, and play an important role in defending the plants against herbivorous insects. Irregular monoterpenes are much less common than other isoprenoids and are confined to plants of the tribe Anthemideae in the family Asteraceae [1,2,5] These secondary metabolites play an important role in their defense against herbivorous insects [1,2,4,6,7,8]. Previous studies demonstrated that CDS has a T → G substitution in region IV and a D → N substitution in the first aspartate in region V [1,2]

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