Terpenoid-based defenses in conifers: cDNA cloning, characterization, and functional expression of wound-inducible (
            <i>E</i>
            )-α-bisabolene synthase from grand fir (
            <i>Abies grandis</i>
            )

Bohlmann, Jörg; Crock, John; Jetter, Reinhard; Croteau, Rodney

doi:10.1073/pnas.95.12.6756

Cited by 163 publications

(117 citation statements)

References 40 publications

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“…Of these three putative sesqui-TPS, the amino acid sequence of PaTPS-Far has highest similarity with the loblolly pine a-farnesene synthase (81% I, 90% S; Phillips et al, 2003), but surprisingly also has very high sequence similarity with the spruce mono-TPS described above (Table II). PaTPS-Bis is most similar to grand fir E-a-bisabolene synthase (86% I, 91% S; Bohlmann et al, 1998a). The third putative sesqui-TPS, PaTPS-Lon, is most similar with d-selinene synthase from grand fir (62% I, 82% S; Steele et al, 1998a).…”

Section: Results Cdna Cloning Of a Family Of Nine Tps Genes From Norwmentioning

confidence: 94%

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Functional Characterization of Nine Norway Spruce TPS Genes and Evolution of Gymnosperm Terpene Synthases of the TPS-d Subfamily

2004

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Constitutive and induced terpenoids are important defense compounds for many plants against potential herbivores and pathogens. In Norway spruce (Picea abies L. Karst), treatment with methyl jasmonate induces complex chemical and biochemical terpenoid defense responses associated with traumatic resin duct development in stems and volatile terpenoid emissions in needles. The cloning of (1)-3-carene synthase was the first step in characterizing this system at the molecular genetic level. Here we report the isolation and functional characterization of nine additional terpene synthase (TPS) cDNAs from Norway spruce. These cDNAs encode four monoterpene synthases, myrcene synthase, (2)-limonene synthase, (2)-a/bpinene synthase, and (2)-linalool synthase; three sesquiterpene synthases, longifolene synthase, E,E-a-farnesene synthase, and E-a-bisabolene synthase; and two diterpene synthases, isopimara-7,15-diene synthase and levopimaradiene/abietadiene synthase, each with a unique product profile. To our knowledge, genes encoding isopimara-7,15-diene synthase and longifolene synthase have not been previously described, and this linalool synthase is the first described from a gymnosperm. These functionally diverse TPS account for much of the structural diversity of constitutive and methyl jasmonate-induced terpenoids in foliage, xylem, bark, and volatile emissions from needles of Norway spruce. Phylogenetic analyses based on the inclusion of these TPS into the TPS-d subfamily revealed that functional specialization of conifer TPS occurred before speciation of Pinaceae. Furthermore, based on TPS enclaves created by distinct branching patterns, the TPS-d subfamily is divided into three groups according to sequence similarities and functional assessment. Similarities of TPS evolution in angiosperms and modeling of TPS protein structures are discussed.

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Section: Results Cdna Cloning Of a Family Of Nine Tps Genes From Norwmentioning

confidence: 94%

“…These studies showed that a family of TPS genes is central to structural diversity of terpenoid defenses (Stofer Vogel et al, 1996;Bohlmann et al, 1997Bohlmann et al, , 1998aSteele et al, 1998a). Recent work in loblolly pine (Pinus taeda) provided information about stereospecificity of cloned pinene synthases in this species (Phillips et al, 2003).…”

mentioning

confidence: 99%

Functional Characterization of Nine Norway Spruce TPS Genes and Evolution of Gymnosperm Terpene Synthases of the TPS-d Subfamily

2004

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“…(Oxido)squalene cyclases (C 30 ) from both eukaryotes and prokaryotes are representatives [21ϳ24]. Other than triterpene (C 30 ) cyclases, Croteau and co-workers extensively studied reaction mechanisms of enzymes, such as (Ϫ)-limonene synthase (C 10 ) [25], myrcene synthase (C 10 ) [25] (Ϫ)-pinene synthase (C 10 ) [25], (Ϫ)-camphene synthase (C 10 ) [26], (Ϫ)-beta-phellandrene synthase (C 10 ) [26], terpinolene synthase (C 10 ) [26], delta-selinene synthase (C 15 ) [27], gamma-humulene synthase (C 15 ) [27], bisabolene synthase (C 15 ) [28], and abietadiene synthase (C 20 ) [29], etc., from grand fir (Abies grandis). Croteau et al [30] cloned and characterized a gene encoding taxadiene synthase (C 20 ) that catalyzes the committed step of biosynthesis of taxol, an anticancer drug isolated from yew.…”

Section: Biosynthesis Of Isoprenoidsmentioning

confidence: 99%

Studies on Biosynthetic Genes and Enzymes of Isoprenoids Produced by Actinomycetes

Dairi

2005

J Antibiot

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Most Streptomyces strains are equipped with only the 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway for the formation of isopentenyl diphosphate, a common precursor of isoprenoids. In addition to this pathway, some Streptomyces strains possess the mevalonate (MV) pathway via which isoprenoid antibiotics are produced. We have recently cloned and analyzed the MV pathway gene clusters and their flanking regions from terpentecin, BE-40644, and furaquinocin A producers. All these clusters contained genes coding for mevalonate kinase, mevalonate diphosphate decarboxylase, phosphomevalonate kinase, type 2 IPP isomerase, HMGCoA reductase, and HMG-CoA synthase. The order of each of the open reading frames (ORFs) is also the same, and the respective homologous ORFs show more than 70% amino acid identity with each other. In contrast to these conservative gene organizations, the biosynthetic genes of terpentecin, BE-40644, and furaquinocin A were located just upstream and/or downstream of the MV pathway gene cluster. These facts suggested that all the actinomycete strains possessing both the MV and MEP pathways produce isoprenoid compounds and the biosynthetic genes of one of these isoprenoids usually exist adjacent to the MV pathway gene cluster. Therefore, when the presence of the MV cluster is detected by molecular genetic techniques, isoprenoids may be produced by the cultivation of these actinomycete strains. During the course of these studies, we identified diterpene cyclases possessing unique primary structures that differ from those of eukaryotes and catalyze unique reactions.Keywords isoprenoid, mevalonate pathway, biosynthesis, cyclase, Actinomycetes IntroductionActinomycete strains usually produce a number of secondary metabolites that often possess pharmaceutical activities. Therefore, for a long time, the strains have been used for many screenings to find novel, medically useful compounds. Consequently, more than 60 percent of the known antibiotics, including not only antibacterial antibiotics but also bioactive microbial compounds, have been reported to be produced by actinomycetes [1]. Presently, such pharmaceutically important, novel compounds can be found in the culture broth of actinomycete strains by screening rare actinomycetes, developing new screening strategies, employing sensitive assay methods for the detection of low concentrations of antibiotics, etc. However, sometimes, "semi-new antibiotics"-derivatives of known antibiotics-were isolated; discovering novel antibiotics every year became very difficult.In the past two decades, recombinant DNA technology has come into play in this field. Gene clusters encoding many natural products have been cloned and characterized. Moreover, whole-genome sequencing has uncovered hundreds of candidates for secondary metabolic pathways. Among them, the biosynthetic machinery of nonribosomal peptide and polyketide natural products has been extensively investigated [2ϳ7]. Recent progress in the application of combinatorial biosynthesis methods to these bi...

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“…Fig. 2B) demonstrated only weak similarity (,27% identity) to those not involved in labdanerelated diterpenoid biosynthesis (Dudareva et al, 1996;Wildung and Croteau, 1996;Bohlmann et al, 1998b). Slightly higher similarity (approximately 30% identity) was found with the identified gymnosperm bifunctional class II/I diterpene synthases, which are involved in labdane-related biosynthesis (Stofer Vogel et al, 1996;Schepmann et al, 2001;Martin et al, 2004).…”

Section: Sequence Comparison Suggested a Role In Labdane-related Ditementioning

confidence: 99%

“…OsDTS2 was the reference sequence in all cases. The class I terpene synthases not involved in labdane-related diterpenoid biosynthesis, yet containing 'insertional' elements, are linalool synthase from Clarkia breweri (Dudareva et al, 1996), taxadiene synthase from Taxus brevifolia , and bisabolene synthase from Abies grandis (Bohlmann et al, 1998b). Bifunctional class II/I terpene synthases producing labdane-related diterpenes of normal stereochemistry are those from the gymnosperms A. grandis (Stofer Vogel et al, 1996), Ginkgo biloba (Schepmann et al, 2001), and Picea abies (Martin et al, 2004).…”

Section: Sequence Analysis and Alignmentsmentioning

confidence: 99%

Identification of Syn-Pimara-7,15-Diene Synthase Reveals Functional Clustering of Terpene Synthases Involved in Rice Phytoalexin/Allelochemical Biosynthesis

et al. 2004

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Rice (Oryza sativa) produces momilactone diterpenoids as both phytoalexins and allelochemicals. Accordingly, the committed step in biosynthesis of these natural products is catalyzed by the class I terpene synthase that converts syn-copalyl diphosphate to the corresponding polycyclic hydrocarbon intermediate syn-pimara-7,15-diene. Here, a functional genomics approach was utilized to identify a syn-copalyl diphosphate specific 9b-pimara-7,15-diene synthase (OsDTS2). To our knowledge, this is the first identified terpene synthase with this particular substrate stereoselectivity and, by comparison with the previously described and closely related ent-copalyl diphosphate specific cassa-12,15-diene synthase (OsDTC1), provides a model system for investigating the enzymatic determinants underlying the observed difference in substrate specificity. Further, OsDTS2 mRNA in leaves is up-regulated by conditions that stimulate phytoalexin biosynthesis but is constitutively expressed in roots, where momilactones are constantly synthesized as allelochemicals. Therefore, transcription of OsDTS2 seems to be an important regulatory point for controlling production of these defensive compounds. Finally, the gene identified here as OsDTS2 has previously been mapped at 14.3 cM on chromosome 4. The class II terpene synthase producing syn-copalyl diphosphate from the universal diterpenoid precursor geranylgeranyl diphosphate was also mapped to this same region. These genes catalyze sequential cyclization steps in momilactone biosynthesis and seem to have been evolutionarily coupled by physical linkage and resulting cosegregation. Further, the observed correlation between physical proximity and common metabolic function indicates that other such class I and class II terpene synthase gene clusters may similarly catalyze consecutive reactions in shared biosynthetic pathways.Plants produce a vast and diverse array of low-molecular weight organic compounds, the overwhelming majority of which are secondary metabolites with nonessential, yet important, functions such as defense . For example, phytoalexins are produced in response to microbial infections and exhibit antimicrobial activity (VanEtten et al., 1994), while allelochemicals are secreted to the rhizosphere and suppress the growth of neighboring plants (Bais et al., 2004). Often found serving in such roles are terpenoids, which are particularly abundant in plant metabolism and form the largest class of natural products, exhibiting wide diversity in chemical structure and biological function . Much of the structural variation within this class arises from the diverse carbon backbones formed by terpene synthases (cyclases). These divalent metal dependent enzymes carry out complex electrophilic cyclizations/ rearrangements to create these diverse skeletal structures from relatively simple acyclic precursors (Davis and Croteau, 2000). Notably, production of a specific backbone structure either dictates, or at least severely restricts, the metabolic fate of that particular molecule. Thus,...

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Terpenoid-based defenses in conifers: cDNA cloning, characterization, and functional expression of wound-inducible ( E )-α-bisabolene synthase from grand fir ( Abies grandis )

Cited by 163 publications

References 40 publications

Functional Characterization of Nine Norway Spruce TPS Genes and Evolution of Gymnosperm Terpene Synthases of the TPS-d Subfamily

Functional Characterization of Nine Norway Spruce TPS Genes and Evolution of Gymnosperm Terpene Synthases of the TPS-d Subfamily

Studies on Biosynthetic Genes and Enzymes of Isoprenoids Produced by Actinomycetes

Identification of Syn-Pimara-7,15-Diene Synthase Reveals Functional Clustering of Terpene Synthases Involved in Rice Phytoalexin/Allelochemical Biosynthesis

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