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Updated: Jan 23, 2026

Author Spotlight: Integrating Biochemical Functions of β-Glucanases and Peroxidase Enzymes in Wheat-RWA Interaction
Published on: July 26, 2024
A Wheat β-Patchoulene Synthase Confers Resistance Against Herbivory in Transgenic Arabidopsis
Qingyu Pu1, Jin Liang2, Qinqin Shen3
1Institute of Ecological Agriculture, College of Agronomy, Sichuan Agricultural University, Chengdu 611130, China. cnpuqingyu@sina.com.
Abstract:
Terpenoids play important roles in plant defense. Although some terpene synthases have been characterized, terpenoids and their biosynthesis in wheat (Triticumaestivum L.) still remain largely unknown. Here, we describe the identification of a terpene synthase gene in wheat. It encodes a sesquiterpene synthase that catalyzes β-patchoulene formation with E,E-farnesyl diphosphate (FPP) as the substrate, thus named as TaPS. TaPS exhibits inducible expression in wheat in response to various elicitations. Particularly, alamethicin treatment strongly induces TaPS gene expression and β-patchoulene accumulation in wheat. Overexpression of TaPS in Arabidopsis successfully produces β-patchoulene, verifying the biochemical function of TaPS in planta. Furthermore, these transgenic Arabidopsis plants exhibit resistance against herbivory by repelling beet armyworm larvae feeding, thereby indicating anti-herbivory activity of β-patchoulene. The catalytic mechanism of TaPS is also explored by homology modeling and site-directed mutagenesis. Two key amino acids are identified to act in protonation and stability of intermediates and product formation. Taken together, one wheat sesquiterpene synthase is identified as β-patchoulene synthase. TaPS exhibits inducible gene expression and the sesquiterpene β-patchoulene is involved in repelling insect infestation.
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