globalchange  > 气候变化与战略
DOI: 10.1073/pnas.1800008115
论文题名:
De novo formation of an aggregation pheromone precursor by an isoprenyl diphosphate synthase-related terpene synthase in the harlequin bug
作者: Lancaster J.; Khrimian A.; Young S.; Lehner B.; Luck K.; Wallingford A.; Ghosh S.K.B.; Zerbe P.; Muchlinski A.; Marek P.E.; Sparks M.E.; Tokuhisa J.G.; Tittiger C.; Köllner T.G.; Weber D.C.; Gundersen-Rindal D.E.; Kuhar T.P.; Tholl D.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2018
卷: 115, 期:37
起始页码: E8634
结束页码: E8641
语种: 英语
英文关键词: Aggregation pheromone ; Harlequin bug ; Hemiptera ; Pentatomidae ; Terpene synthase
Scopus关键词: 1,10 bisaboladien 1 ol (sesquipiperitol) ; 10,11 epoxy 1 bisabolen 3 ol ; geranyltransferase ; hormone precursor ; isoprenyl diphosphate synthase ; messenger RNA ; murgantiol ; sesquiterpene ; sex pheromone ; synthetase ; terpene synthase ; unclassified drug ; 4-(3-(3,3-dimethyloxiran-2-yl)-1-methylpropyl)-1-methylcyclohex-2-en-1ol ; farnesyl diphosphate ; insect protein ; isoprenoid phosphate ; pheromone ; sesquiterpene ; terpene synthase ; transferase ; animal tissue ; Article ; Brassicaceae ; chemical structure ; controlled study ; cuticle ; enzyme activity ; gene knockdown ; harlequin bug ; Hemiptera ; hormone synthesis ; male ; Murgantia histrionica ; mutagenesis ; nonhuman ; nucleotide sequence ; phylogeny ; priority journal ; protein aggregation ; protein function ; RNA interference ; animal ; biosynthesis ; chemistry ; classification ; enzymology ; genetics ; Heteroptera ; metabolism ; molecular model ; protein domain ; stereoisomerism ; Alkyl and Aryl Transferases ; Animals ; Biosynthetic Pathways ; Heteroptera ; Insect Proteins ; Male ; Models, Molecular ; Molecular Structure ; Pheromones ; Phylogeny ; Polyisoprenyl Phosphates ; Protein Domains ; Sesquiterpenes ; Stereoisomerism
英文摘要: Insects use a diverse array of specialized terpene metabolites as pheromones in intraspecific interactions. In contrast to plants and microbes, which employ enzymes called terpene synthases (TPSs) to synthesize terpene metabolites, limited information from few species is available about the enzymatic mechanisms underlying terpene pheromone biosynthesis in insects. Several stink bugs (Hemiptera: Pentatomidae), among them severe agricultural pests, release 15-carbon sesquiterpenes with a bisabolene skeleton as sex or aggregation pheromones. The harlequin bug, Murgantia histrionica, a specialist pest of crucifers, uses two stereoisomers of 10,11-epoxy-1-bisabolen-3-ol as a male-released aggregation pheromone called murgantiol. We show that MhTPS (MhIDS-1), an enzyme unrelated to plant and microbial TPSs but with similarity to trans-isoprenyl diphosphate synthases (IDS) of the core terpene biosynthetic pathway, catalyzes the formation of (1S,6S,7R)-1,10-bisaboladien-1-ol (sesquipiperitol) as a terpene intermediate in murgantiol biosynthesis. Sesquipiperitol, a so-far-unknown compound in animals, also occurs in plants, indicating convergent evolution in the biosynthesis of this sesquiterpene. RNAi-mediated knockdown of MhTPS mRNA confirmed the role of MhTPS in murgantiol biosynthesis. MhTPS expression is highly specific to tissues lining the cuticle of the abdominal sternites of mature males. Phylogenetic analysis suggests that MhTPS is derived from a trans-IDS progenitor and diverged from bona fide trans-IDS proteins including MhIDS-2, which functions as an (E,E)-farnesyl diphosphate (FPP) synthase. Structure-guided mutagenesis revealed several residues critical to MhTPS and MhFPPS activity. The emergence of an IDS-like protein with TPS activity in M. histrionica demonstrates that de novo terpene biosynthesis evolved in the Hemiptera in an adaptation for intraspecific communication. © 2018 National Academy of Sciences. All Rights Reserved.
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资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163663
Appears in Collections:气候变化与战略

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作者单位: Lancaster, J., Department of Biological Sciences, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, United States; Khrimian, A., Invasive Insect Biocontrol and Behavior Laboratory, Agricultural Research Service, US Department of Agriculture, Beltsville, MD 20705, United States; Young, S., Department of Biochemistry and Molecular Biology, University of Nevada, Reno, NV 89557, United States; Lehner, B., Department of Biological Sciences, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, United States; Luck, K., Department of Biochemistry, Max Planck Institute for Chemical Ecology, Jena, D-07745, Germany; Wallingford, A., Department of Entomology, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, United States; Ghosh, S.K.B., Invasive Insect Biocontrol and Behavior Laboratory, Agricultural Research Service, US Department of Agriculture, Beltsville, MD 20705, United States; Zerbe, P., Department of Plant Biology, University of California, Davis, CA 95616, United States; Muchlinski, A., Department of Biological Sciences, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, United States; Marek, P.E., Department of Entomology, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, United States; Sparks, M.E., Invasive Insect Biocontrol and Behavior Laboratory, Agricultural Research Service, US Department of Agriculture, Beltsville, MD 20705, United States; Tokuhisa, J.G., Department of Biological Sciences, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, United States, Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, United States; Tittiger, C., Department of Biochemistry and Molecular Biology, University of Nevada, Reno, NV 89557, United States; Köllner, T.G., Department of Biochemistry, Max Planck Institute for Chemical Ecology, Jena, D-07745, Germany; Weber, D.C., Invasive Insect Biocontrol and Behavior Laboratory, Agricultural Research Service, US Department of Agriculture, Beltsville, MD 20705, United States; Gundersen-Rindal, D.E., Invasive Insect Biocontrol and Behavior Laboratory, Agricultural Research Service, US Department of Agriculture, Beltsville, MD 20705, United States; Kuhar, T.P., Department of Entomology, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, United States; Tholl, D., Department of Biological Sciences, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, United States

Recommended Citation:
Lancaster J.,Khrimian A.,Young S.,et al. De novo formation of an aggregation pheromone precursor by an isoprenyl diphosphate synthase-related terpene synthase in the harlequin bug[J]. Proceedings of the National Academy of Sciences of the United States of America,2018-01-01,115(37)
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