气候变化领域集成服务门户(CCPortal): De novo formation of an aggregation pheromone precursor by an isoprenyl diphosphate synthase-related terpene synthase in the harlequin bug

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DOI	10.1073/pnas.1800008115
	De novo formation of an aggregation pheromone precursor by an isoprenyl diphosphate synthase-related terpene synthase in the harlequin bug
	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.
发表日期	2018
ISSN	0027-8424
起始页码	E8634
结束页码	E8641
卷号	115 期号:37
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.
英文关键词	Aggregation pheromone; Harlequin bug; Hemiptera; Pentatomidae; Terpene synthase
语种	英语
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
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/160467
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 Ca...
推荐引用方式 GB/T 7714	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],2018,115(37).
APA	Lancaster J..,Khrimian A..,Young S..,Lehner B..,Luck K..,...&Tholl D..(2018).De novo formation of an aggregation pheromone precursor by an isoprenyl diphosphate synthase-related terpene synthase in the harlequin bug.Proceedings of the National Academy of Sciences of the United States of America,115(37).
MLA	Lancaster J.,et al."De novo formation of an aggregation pheromone precursor by an isoprenyl diphosphate synthase-related terpene synthase in the harlequin bug".Proceedings of the National Academy of Sciences of the United States of America 115.37(2018).