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Proc Natl Acad Sci U S A

Title:		Novel family of terpene synthases evolved from trans-isoprenyl diphosphate synthases in a flea beetle
Author(s):		Beran F; Rahfeld P; Luck K; Nagel R; Vogel H; Wielsch N; Irmisch S; Ramasamy S; Gershenzon J; Heckel DG; Kollner TG;
Address:		"Research Group Sequestration and Detoxification in Insects, Max Planck Institute for Chemical Ecology, 07745 Jena, Germany; fberan@ice.mpg.de. Department of Bioorganic Chemistry, Max Planck Institute for Chemical Ecology, 07745 Jena, Germany; Department of Biochemistry, Max Planck Institute for Chemical Ecology, 07745 Jena, Germany; Department of Entomology, Max Planck Institute for Chemical Ecology, 07745 Jena, Germany; Department of Mass Spectrometry, Max Planck Institute for Chemical Ecology, 07745 Jena, Germany; Entomology, AVRDC-The World Vegetable Center, Shanhua, Tainan 74151, Taiwan"
Journal Title:		Proc Natl Acad Sci U S A
Year:		2016
Volume:		20160302
Issue:		11
Page Number:		2922 - 2927
DOI:		10.1073/pnas.1523468113
ISSN/ISBN:		1091-6490 (Electronic) 0027-8424 (Print) 0027-8424 (Linking)
Abstract:		"Sesquiterpenes play important roles in insect communication, for example as pheromones. However, no sesquiterpene synthases, the enzymes involved in construction of the basic carbon skeleton, have been identified in insects to date. We investigated the biosynthesis of the sesquiterpene (6R,7S)-himachala-9,11-diene in the crucifer flea beetle Phyllotreta striolata, a compound previously identified as a male-produced aggregation pheromone in several Phyllotreta species. A (6R,7S)-himachala-9,11-diene-producing sesquiterpene synthase activity was detected in crude beetle protein extracts, but only when (Z,E)-farnesyl diphosphate [(Z,E)-FPP] was offered as a substrate. No sequences resembling sesquiterpene synthases from plants, fungi, or bacteria were found in the P. striolata transcriptome, but we identified nine divergent putative trans-isoprenyl diphosphate synthase (trans-IDS) transcripts. Four of these putative trans-IDSs exhibited terpene synthase (TPS) activity when heterologously expressed. Recombinant PsTPS1 converted (Z,E)-FPP to (6R,7S)-himachala-9,11-diene and other sesquiterpenes observed in beetle extracts. RNAi-mediated knockdown of PsTPS1 mRNA in P. striolata males led to reduced emission of aggregation pheromone, confirming a significant role of PsTPS1 in pheromone biosynthesis. Two expressed enzymes showed genuine IDS activity, with PsIDS1 synthesizing (E,E)-FPP, whereas PsIDS3 produced neryl diphosphate, (Z,Z)-FPP, and (Z,E)-FPP. In a phylogenetic analysis, the PsTPS enzymes and PsIDS3 were clearly separated from a clade of known coleopteran trans-IDS enzymes including PsIDS1 and PsIDS2. However, the exon-intron structures of IDS and TPS genes in P. striolata are conserved, suggesting that this TPS gene family evolved from trans-IDS ancestors"
Keywords:		"Alkyl and Aryl Transferases/*classification/genetics/isolation & purification Amino Acid Sequence Animals Cloning, Molecular Coleoptera/classification/*enzymology/genetics Evolution, Molecular Female Gene Components *Genes, Insect Genetic Speciation Insec;"
Notes:		"MedlineBeran, Franziska Rahfeld, Peter Luck, Katrin Nagel, Raimund Vogel, Heiko Wielsch, Natalie Irmisch, Sandra Ramasamy, Srinivasan Gershenzon, Jonathan Heckel, David G Kollner, Tobias G eng Comparative Study Research Support, Non-U.S. Gov't 2016/03/05 Proc Natl Acad Sci U S A. 2016 Mar 15; 113(11):2922-7. doi: 10.1073/pnas.1523468113. Epub 2016 Mar 2"