Functional characterization of(E)-β-caryophyllene synthase from lima bean and its up-regulation by spider mites and alamethicin

作     者：LI Feng-qi FU Ning-ning ZHOU Jing-jiang WANG Gui-rong 

作者机构：Institute of Plant and Environment ProtectionBeijing Academy of Agriculture and Forestry Sciences Institute of Plant ProtectionChinese Academy of Agricultural Sciences Department of Biological Chemistry and Crop ProtectRothamsted Research 

出 版 物：《Journal of Integrative Agriculture》 (农业科学学报（英文版）)

年 卷 期：2017年第16卷第10期

页      面：2231-2238页

核心收录：

学科分类：090403[农学-农药学(可授农学、理学学位）] 09[农学] 0904[农学-植物保护] 

基　　金：funded by the International Science and Technology Cooperation Program of China (2013DFG32230) the Major Project of Genetically Modified Organisms Breeding,China (2016ZX08010005) 

主　　题：plant defence terpene synthases (E)--caryophyllene lima bean 

摘      要：（E）-β-Caryophyllene is a sesquiterpene compound widely distributed in plants and functions in plant defence. However, little is known about the sequence and function of （E）-β-caryophyllene synthase in lima bean （Phaseolus lunatus）. Here, we report a new full-length cDNA （PICAHS） encoding （E）-β-caryophyllene synthase, a possible key enzyme of plant defence. The cDNA of PICAHS contains an open reading frame of 1 761 bp, encoding a protein of 586 amino acids with a predicted mass of 67.95 kDa. The deduced amino acid sequence shows 52% identity with sesquiterpene synthase MtCAHS of Med- icago truncatula. Based on phylogenetic analysis, PICAHS is classified as the terpene synthases （TPS）-a subfamily. The recombinant enzyme, expressed in Escherichia coil, catalysed the formation of a major product （E）-β-caryophyllene （82%） and a minor product a-humulene （18%） from farnesyl dJphosphate. Real-time quantitative PCR （qRT-PCR） analysis found that the PICAHS transcript was significantly up-regulated in leaves after treatment with spider mites and alamethicin （ALA）, suggesting its ecological function in plant defence.