title: Four terpene synthases produce major compounds of the gypsy moth feeding-induced volatile blend of Populus trichocarpa.
abstract: After herbivore damage, many plants increase their emission of volatile compounds, with terpenes usually comprising the major group of induced volatiles. Populus trichocarpa is the first woody species with a fully sequenced genome, enabling rapid molecular approaches towards characterization of volatile terpene biosynthesis in this and other poplar species. We identified and characterized four terpene synthases (PtTPS1-4) from P. trichocarpa which form major terpene compounds of the volatile blend induced by gypsy moth (Lymantria dispar) feeding. The enzymes were heterologously expressed and assayed with potential prenyl diphosphate substrates. PtTPS1 and PtTPS2 accepted only farnesyl diphosphate and produced (-)-germacrene D and (E,E)-α-farnesene as their major products, respectively. In contrast, PtTPS3 and PtTPS4 showed both mono- and sesquiterpene synthase activity. They produce the acyclic terpene alcohols linalool and nerolidol but exhibited opposite stereospecificity. qRT-PCR analysis revealed that the expression of the respective terpene synthase genes was induced after feeding of gypsy moth caterpillars. The TPS enzyme products may play important roles in indirect defense of poplar to herbivores and in mediating intra- and inter-plant signaling.
authors.affiliation: Max Planck Institute for Chemical Ecology, Department of Biochemistry, Hans-Knöll Straße 8, 07745 Jena, Germany.
authors.forename: Holger
authors.initials: H
authors.lastname: Danner
authors.affiliation: Max Planck Institute for Chemical Ecology, Department of Biochemistry, Hans-Knöll Straße 8, 07745 Jena, Germany.
authors.forename: G Andreas
authors.initials: GA
authors.lastname: Boeckler
authors.affiliation: Max Planck Institute for Chemical Ecology, Department of Biochemistry, Hans-Knöll Straße 8, 07745 Jena, Germany.
authors.forename: Sandra
authors.initials: S
authors.lastname: Irmisch
authors.affiliation: Department of Plant Sciences, University of Tennessee, Knoxville, TN 37996, USA.
authors.forename: Joshua S
authors.initials: JS
authors.lastname: Yuan
authors.affiliation: Department of Plant Sciences, University of Tennessee, Knoxville, TN 37996, USA.
authors.forename: Feng
authors.initials: F
authors.lastname: Chen
authors.affiliation: Max Planck Institute for Chemical Ecology, Department of Biochemistry, Hans-Knöll Straße 8, 07745 Jena, Germany.
authors.forename: Jonathan
authors.initials: J
authors.lastname: Gershenzon
authors.affiliation: Max Planck Institute for Chemical Ecology, Department of Biochemistry, Hans-Knöll Straße 8, 07745 Jena, Germany.
authors.forename: Sybille B
authors.initials: SB
authors.lastname: Unsicker
authors.affiliation: Max Planck Institute for Chemical Ecology, Department of Biochemistry, Hans-Knöll Straße 8, 07745 Jena, Germany.
authors.forename: Tobias G
authors.initials: TG
authors.lastname: Köllner
mesh_terms: D019883:Alkyl and Aryl Transferases / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D018506:Gene Expression Regulation, Plant; D060434:Herbivory; D008969:Molecular Sequence Data; D009036:Moths; D018515:Plant Leaves / Q000737:chemistry; D010940:Plant Proteins / Q000378:metabolism; D032107:Populus / Q000737:chemistry / Q000201:enzymology*; D013729:Terpenes / Q000737:chemistry*; D055549:Volatile Organic Compounds / Q000737:chemistry*
chemical_list: D010940:Plant Proteins; D013729:Terpenes; D055549:Volatile Organic Compounds; D019883:Alkyl and Aryl Transferases; C108877:terpene synthase