Purification, properties and heteromeric association of type-1 and type-2 lepidopteran farnesyl diphosphate synthases

Sen, Stephanie E.; Cusson, Michel; Trobaugh, Corey; Béliveau, Catherine; Richard, Thenesha; Graham, Wendy; Mimms, Adrian; Roberts, Gregory

doi:10.1016/j.ibmb.2007.05.012

Cited by 37 publications

(30 citation statements)

References 21 publications

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“…S5, which suggests that these genes diversified before species diversification. Only one copy of each MPB gene was found in the draft genome, whereas more than one FPPS are found in some Lepidoptera (33). In MPB, the only juvenile hormone biosynthesized is juvenile hormone III, whereas some Lepidoptera also have juvenile hormone 0, juvenile hormone I, or juvenile hormone II (34).…”

Section: Discussionmentioning

confidence: 99%

Frontalin pheromone biosynthesis in the mountain pine beetle, Dendroctonus ponderosae , and the role of isoprenyl diphosphate synthases

Keeling

Chiu

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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The mountain pine beetle (Dendroctonus ponderosae Hopkins) is the most destructive pest of western North American pine forests. Adult males produce frontalin, an eight-carbon antiaggregation pheromone, via the mevalonate pathway, as part of several pheromones that initiate and modulate the mass attack of host trees. Frontalin acts as a pheromone, attractant, or kairomone in most Dendroctonus species, other insects, and even elephants. 6-Methylhept-6-en-2-one, a frontalin precursor, is hypothesized to originate from 10-carbon geranyl diphosphate (GPP), 15-carbon farnesyl diphosphate (FPP), or 20-carbon geranylgeranyl diphosphate (GGPP) via a dioxygenase-or cytochrome P450-mediated carboncarbon bond cleavage. To investigate the role of isoprenyl diphosphate synthases in pheromone biosynthesis, we characterized a bifunctional GPP/FPP synthase and a GGPP synthase in the mountain pine beetle. The ratio of GPP to FPP produced by the GPP/FPP synthase was highly dependent on the ratio of the substrates isopentenyl diphosphate and dimethylallyl diphosphate used in the assay. Transcript levels in various tissues and life stages suggested that GGPP rather than GPP or FPP is used as a precursor to frontalin. Reduction of transcript levels by RNA interference of the isoprenyl diphosphate synthases identified GGPP synthase as having the largest effect on frontalin production, suggesting that frontalin is derived from a 20-carbon isoprenoid precursor rather than from the 10-or 15-carbon precursors. (Fig. 1), is an antiaggregation pheromone known to be synthesized de novo via the mevalonate pathway in male midgut tissue (3, 4). Frontalin acts as a pheromone, attractant, or kairomone in most other Dendroctonus species, other insects (5), and even elephants (6, 7) and has been studied in bark beetles for more than 40 y (8). Its biosynthetic precursor, 6-methylhept-6-en-2-one (6MHO), found in both insects and elephants (6, 9), is hypothesized to originate from cleavage of geranyl diphosphate (GPP), farnesyl diphosphate (FPP), or geranylgeranyl diphosphate (GGPP) by a dioxygenase or cytochrome P450 (10). These isoprenyl diphosphates are biosynthesized from the five-carbon precursors isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) by the isoprenyl diphosphate synthases (IDSs) GPP synthase (GPPS), FPP synthase (FPPS), and GGPP synthase (GGPPS). However, it is not known which of these isoprenyl diphosphates is used as a precursor in frontalin biosynthesis.A few IDSs have been characterized in Coleoptera, including an FPPS from the cotton boll weevil (Anthonomus grandis) (11), a GPPS/FPPS from the horseradish leaf beetle (Phaedon cochleariae) (12), and a unique GPPS from the pine engraver beetle (Ips pini) that also produces myrcene (13,14). To assess their importance in pheromone biosynthesis, we identified and functionally characterized two IDSs in MPB. Based on three different lines of evidence, gene-expression patterns of the IDSs, enzyme activity of recombinant proteins, and the frontalin content of dsRNA-trea...

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Section: Discussionmentioning

confidence: 99%

Frontalin pheromone biosynthesis in the mountain pine beetle, Dendroctonus ponderosae , and the role of isoprenyl diphosphate synthases

Keeling

Chiu

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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“…However, none of the other P. striolata trans-IDS enzymes identified in this study produced significant amounts of (E)-GPP under our assay conditions. It was previously shown that product chain length or activity of plant and insect IDSs can be influenced by heterooligomerization, which may also play a role in (E)-GPP and (Z,E)-FPP synthesis in P. striolata (9,(39)(40)(41). Moreover, IDS product chain length may also be influenced by the IPP/DMAPP ratio (8), and different metal ion cofactors as recently demonstrated in the mustard leaf beetle, Phaedon cochleariae (5).…”

Section: P Striolata Possesses An Evolutionarily Novel Class Of Tps mentioning

confidence: 93%

“…No transcripts with similarity to plant or microbial terpene synthases were evident in a transcriptome of this species. However, a remarkably high number of genes were present that were predicted to encode enzymes similar to insect trans-IDSs, which produce geranyl diphosphate [(E)-GPP] and/ or farnesyl diphosphate [(E,E)-FPP] from the C 5 precursors isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) (5,9,10). Functional characterization of the recombinant IDS-like enzymes led to the discovery of four TPS enzymes which formed a separate clade in a phylogenetic analysis of coleopteran trans-IDS and trans-IDS-like enzymes.…”

Section: Significancementioning

confidence: 99%

“…Sesquiterpenes are biosynthesized from three C 5 isopentenoid units supplied by the mevalonate pathway, which are then joined sequentially via the action of enzymes known as trans-isoprenyl diphosphate synthases (trans-IDS) to produce the linear C 15 intermediate (E,E)-farnesyl diphosphate (FPP). Trans-IDS enzymes have been identified and characterized in a number of insect species (4)(5)(6)(7)(8)(9)(10). The huge diversity of sesquiterpene carbon skeletons are formed from FPP in the next step by the catalysis of terpene synthases (TPSs).…”

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Novel family of terpene synthases evolved from trans -isoprenyl diphosphate synthases in a flea beetle

Beran

Rahfeld

Luck

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Sesquiterpenes play important roles in insect communication, for example as pheromones. However, no sesquiterpene synthases, the enzymes involved in construction of the basic carbon skeleton, have been identified in insects to date. We investigated the biosynthesis of the sesquiterpene (6R,7S)-himachala-9,11-diene in the crucifer flea beetle Phyllotreta striolata, a compound previously identified as a male-produced aggregation pheromone in several Phyllotreta species. A (6R,7S)-himachala-9,11-diene–producing sesquiterpene synthase activity was detected in crude beetle protein extracts, but only when (Z,E)-farnesyl diphosphate [(Z,E)-FPP] was offered as a substrate. No sequences resembling sesquiterpene synthases from plants, fungi, or bacteria were found in the P. striolata transcriptome, but we identified nine divergent putative trans-isoprenyl diphosphate synthase (trans-IDS) transcripts. Four of these putative trans-IDSs exhibited terpene synthase (TPS) activity when heterologously expressed. Recombinant PsTPS1 converted (Z,E)-FPP to (6R,7S)-himachala-9,11-diene and other sesquiterpenes observed in beetle extracts. RNAi-mediated knockdown of PsTPS1 mRNA in P. striolata males led to reduced emission of aggregation pheromone, confirming a significant role of PsTPS1 in pheromone biosynthesis. Two expressed enzymes showed genuine IDS activity, with PsIDS1 synthesizing (E,E)-FPP, whereas PsIDS3 produced neryl diphosphate, (Z,Z)-FPP, and (Z,E)-FPP. In a phylogenetic analysis, the PsTPS enzymes and PsIDS3 were clearly separated from a clade of known coleopteran trans-IDS enzymes including PsIDS1 and PsIDS2. However, the exon–intron structures of IDS and TPS genes in P. striolata are conserved, suggesting that this TPS gene family evolved from trans-IDS ancestors.

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“…FPP serves as a precursor to non-sterol isoprenoid pathway products of insects including dolichols, ubiquinones, prenyl groups of certain proteins, and juvenile hormones in addition to being the putative precursor to female-produced pheromones (Hedin et al, 1979). Insect FPPSs characterized to date are mostly from lepidopterans and were studied in the context of juvenile hormone biosynthesis (Castillo-Garcia and Couillaud, 1999;Kikuchi et al, 2001;Cusson et al, 2006;Sen et al, 2007b). We isolated the first coleopteran FPPS from A. grandis.…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterization of farnesyl diphosphate synthase from the cotton boll weevil, Anthonomus grandis

Taban

Tittiger

Blomquist

et al. 2009

Arch Insect Biochem Physiol

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Farnesyl diphosphate synthase (FPPS) catalyzes the consecutive condensation of two molecules of isopentenyl diphosphate with dimethylallyl diphosphate to form farnesyl diphosphate (FPP). In insects, FPP is used for the synthesis of ubiquinones, dolicols, protein prenyl groups, and juvenile hormone. A full-length cDNA of FPPS was cloned from the cotton boll weevil, Anthonomus grandis (AgFPPS). AgFPPS cDNA consists of 1,835 nucleotides and encodes a protein of 438 amino acids. The deduced amino acid sequence has high similarity to previously isolated insect FPPSs and other known FPPSs. Recombinant AgFPPS expressed in E. coli converted labeled isopentenyl diphosphate in the presence of dimethylallyl diphosphate to FPP. Southern blot analysis indicated the presence of a single copy gene. Using molecular modeling, the three-dimensional structure of coleopteran FPPS was determined and compared to the X-ray crystal structure of avian FPPS. The alpha-helical fold is conserved in AgFPPS and the size of the active site cavity is consistent with the enzyme being a FPPS.

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Purification, properties and heteromeric association of type-1 and type-2 lepidopteran farnesyl diphosphate synthases

Cited by 37 publications

References 21 publications

Frontalin pheromone biosynthesis in the mountain pine beetle, Dendroctonus ponderosae , and the role of isoprenyl diphosphate synthases

Frontalin pheromone biosynthesis in the mountain pine beetle, Dendroctonus ponderosae , and the role of isoprenyl diphosphate synthases

Novel family of terpene synthases evolved from trans -isoprenyl diphosphate synthases in a flea beetle

Isolation and characterization of farnesyl diphosphate synthase from the cotton boll weevil, Anthonomus grandis

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