scholarly journals Biochemical Characterization and Function of Eight Microbial Type Terpene Synthases from Lycophyte Selaginella moellendorffii

2021 ◽  
Vol 22 (2) ◽  
pp. 605
Author(s):  
Yapei Zhao ◽  
Tian Hu ◽  
Ruiqi Liu ◽  
Zhiqiang Hao ◽  
Guoyan Liang ◽  
...  
Keyword(s):  
Pseudomonas Syringae ◽  
Biochemical Characterization ◽  
Vascular Plant ◽  
Terpene Synthase ◽  
Tomato Dc3000 ◽  
Terpene Synthases ◽  
Geranyl Diphosphate ◽  
And Function ◽  
Selaginella Moellendorffii ◽  
And Staphylococcus Aureus

Selaginella moellendorffii is a lycophyte, a member of an ancient vascular plant lineage. Two distinct types of terpene synthase (TPS) genes were identified from this species, including S. moellendorffii TPS genes (SmTPSs) and S. moellendorffii microbial TPS-like genes (SmMTPSLs). The goal of this study was to investigate the biochemical functions of SmMTPSLs. Here, eight full-length SmMTPSL genes (SmMTPSL5, -15, -19, -23, -33, -37, -46, and -47) were functionally characterized from S. moellendorffii. Escherichia coli-expressed recombinant SmMTPSLs were tested for monoterpenes synthase and sesquiterpenes synthase activities. These enzymatic products were typical monoterpenes and sesquiterpenes that have been previous shown to be generated by typical plant TPSs when provided with geranyl diphosphate (GPP) and farnesyl diphosphate (FPP) as the substrates. Meanwhile, SmMTPSL23, -33, and -37 were up-regulated when induced by alamethicin (ALA) and methyl jasmonate (MeJA), suggesting a role for these genes in plants response to abiotic stresses. Furthermore, this study pointed out that the terpenoids products of SmMTPSL23, -33, and -37 have an antibacterial effect on Pseudomonas syringae pv. tomato DC3000 and Staphylococcus aureus. Taken together, these results provide more information about the catalytic and biochemical function of SmMTPSLs in S. moellendorffii plants.

scholarly journals Microbial-type terpene synthase genes occur widely in nonseed land plants, but not in seed plants

2016 ◽  
Vol 113 (43) ◽  
pp. 12328-12333 ◽  
Author(s):  
Qidong Jia ◽  
Guanglin Li ◽  
Tobias G. Köllner ◽  
Jianyu Fu ◽  
Xinlu Chen ◽  
...  
Keyword(s):  
Flowering Plants ◽  
Terpene Synthase ◽  
Seed Plants ◽  
Terpene Synthases ◽  
The Third ◽  
Wide Range ◽  
Prenyl Diphosphate ◽  
Bacteria And Fungi ◽  
Selaginella Moellendorffii ◽  
Catalytic Functions

The vast abundance of terpene natural products in nature is due to enzymes known as terpene synthases (TPSs) that convert acyclic prenyl diphosphate precursors into a multitude of cyclic and acyclic carbon skeletons. Yet the evolution of TPSs is not well understood at higher levels of classification. Microbial TPSs from bacteria and fungi are only distantly related to typical plant TPSs, whereas genes similar to microbial TPS genes have been recently identified in the lycophyte Selaginella moellendorffii. The goal of this study was to investigate the distribution, evolution, and biochemical functions of microbial terpene synthase-like (MTPSL) genes in other plants. By analyzing the transcriptomes of 1,103 plant species ranging from green algae to flowering plants, putative MTPSL genes were identified predominantly from nonseed plants, including liverworts, mosses, hornworts, lycophytes, and monilophytes. Directed searching for MTPSL genes in the sequenced genomes of a wide range of seed plants confirmed their general absence in this group. Among themselves, MTPSL proteins from nonseed plants form four major groups, with two of these more closely related to bacterial TPSs and the other two to fungal TPSs. Two of the four groups contain a canonical aspartate-rich “DDxxD” motif. The third group has a “DDxxxD” motif, and the fourth group has only the first two “DD” conserved in this motif. Upon heterologous expression, representative members from each of the four groups displayed diverse catalytic functions as monoterpene and sesquiterpene synthases, suggesting these are important for terpene formation in nonseed plants.

scholarly journals Genomic Organization of Plant Terpene Synthases and Molecular Evolutionary Implications

Genetics ◽  
2001 ◽  
Vol 158 (2) ◽  
pp. 811-832
Author(s):  
Susan C Trapp ◽  
Rodney B Croteau
Keyword(s):  
Natural Products ◽  
Secondary Metabolism ◽  
Intron Loss ◽  
Terpene Synthase ◽  
Primary Metabolism ◽  
Taxus Brevifolia ◽  
Terpene Synthases ◽  
Sequence Element ◽  
Geranyl Diphosphate ◽  
Terpenoid Synthase

Abstract Terpenoids are the largest, most diverse class of plant natural products and they play numerous functional roles in primary metabolism and in ecological interactions. The first committed step in the formation of the various terpenoid classes is the transformation of the prenyl diphosphate precursors, geranyl diphosphate, farnesyl diphosphate, and geranylgeranyl diphosphate, to the parent structures of each type catalyzed by the respective monoterpene (C10), sesquiterpene (C15), and diterpene synthases (C20). Over 30 cDNAs encoding plant terpenoid synthases involved in primary and secondary metabolism have been cloned and characterized. Here we describe the isolation and analysis of six genomic clones encoding terpene synthases of conifers, [(-)-pinene (C10), (-)-limonene (C10), (E)-α-bisabolene (C15), δ-selinene (C15), and abietadiene synthase (C20) from Abies grandis and taxadiene synthase (C20) from Taxus brevifolia], all of which are involved in natural products biosynthesis. Genome organization (intron number, size, placement and phase, and exon size) of these gymnosperm terpene synthases was compared to eight previously characterized angiosperm terpene synthase genes and to six putative terpene synthase genomic sequences from Arabidopsis thaliana. Three distinct classes of terpene synthase genes were discerned, from which assumed patterns of sequential intron loss and the loss of an unusual internal sequence element suggest that the ancestral terpenoid synthase gene resembled a contemporary conifer diterpene synthase gene in containing at least 12 introns and 13 exons of conserved size. A model presented for the evolutionary history of plant terpene synthases suggests that this superfamily of genes responsible for natural products biosynthesis derived from terpene synthase genes involved in primary metabolism by duplication and divergence in structural and functional specialization. This novel molecular evolutionary approach focused on genes of secondary metabolism may have broad implications for the origins of natural products and for plant phylogenetics in general.

scholarly journals Diversity and function of terpene synthases in the production of carrot aroma and flavor compounds

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Andrew Muchlinski ◽  
Mwafaq Ibdah ◽  
Shelby Ellison ◽  
Mossab Yahyaa ◽  
Bhagwat Nawade ◽  
...  
Keyword(s):  
Expression Profiles ◽  
Terpene Synthase ◽  
Terpene Synthases ◽  
Specific Expression ◽  
Metabolite Profiles ◽  
Germacrene D ◽  
Volatile Terpenes ◽  
And Function ◽  
Volatile Terpene

Abstract Carrot (Daucus carota L.) is an important root vegetable crop with high nutritional value, characteristic flavor, and benefits to human health. D. carota tissues produce an essential oil that is rich in volatile terpenes and plays a major role in carrot aroma and flavor. Although terpene composition represents a critical quality attribute of carrots, little is known about the biosynthesis of terpenes in this crop. Here, we functionally characterized 19 terpene synthase (TPS) genes in an orange carrot (genotype DH1) and compared tissue-specific expression profiles and in vitro products of their recombinant proteins with volatile terpene profiles from DH1 and four other colored carrot genotypes. In addition to the previously reported (E)-β-caryophyllene synthase (DcTPS01), we biochemically characterized several TPS proteins with direct correlations to major compounds of carrot flavor and aroma including germacrene D (DcTPS7/11), γ-terpinene (DcTPS30) and α-terpinolene (DcTPS03). Random forest analysis of volatiles from colored carrot cultivars identified nine terpenes that were clearly distinct among the cultivars and likely contribute to differences in sensory quality. Correlation of TPS gene expression and terpene metabolite profiles supported the function of DcTPS01 and DcTPS03 in these cultivars. Our findings provide a roadmap for future breeding efforts to enhance carrot flavor and aroma.

scholarly journals Computational-guided discovery and characterization of a sesquiterpene synthase from Streptomyces clavuligerus

2015 ◽  
Vol 112 (18) ◽  
pp. 5661-5666 ◽  
Author(s):  
Jeng-Yeong Chow ◽  
Bo-Xue Tian ◽  
Gurusankar Ramamoorthy ◽  
Brandan S. Hillerich ◽  
Ronald D. Seidel ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Homology Model ◽  
Streptomyces Clavuligerus ◽  
Major Product ◽  
Terpene Synthase ◽  
Terpene Synthases ◽  
Guided Discovery ◽  
Functional Assignment ◽  
Reaction Channels

Terpenoids are a large structurally diverse group of natural products with an array of functions in their hosts. The large amount of genomic information from recent sequencing efforts provides opportunities and challenges for the functional assignment of terpene synthases that construct the carbon skeletons of these compounds. Inferring function from the sequence and/or structure of these enzymes is not trivial because of the large number of possible reaction channels and products. We tackle this problem by developing an algorithm to enumerate possible carbocations derived from the farnesyl cation, the first reactive intermediate of the substrate, and evaluating their steric and electrostatic compatibility with the active site. The homology model of a putative pentalenene synthase (Uniprot: B5GLM7) from Streptomyces clavuligerus was used in an automated computational workflow for product prediction. Surprisingly, the workflow predicted a linear triquinane scaffold as the top product skeleton for B5GLM7. Biochemical characterization of B5GLM7 reveals the major product as (5S,7S,10R,11S)-cucumene, a sesquiterpene with a linear triquinane scaffold. To our knowledge, this is the first documentation of a terpene synthase involved in the synthesis of a linear triquinane. The success of our prediction for B5GLM7 suggests that this approach can be used to facilitate the functional assignment of novel terpene synthases.

scholarly journals Systematic mining of fungal chimeric terpene synthases using an efficient precursor-providing yeast chassis

2021 ◽  
Vol 118 (29) ◽  
pp. e2023247118
Author(s):  
Rong Chen ◽  
Qidong Jia ◽  
Xin Mu ◽  
Ben Hu ◽  
Xiang Sun ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Functional Divergence ◽  
Duplication Event ◽  
Early Gene ◽  
Terpene Synthase ◽  
Functional Evolution ◽  
Terpene Synthases ◽  
Potential Models ◽  
Origin And Evolution ◽  
Functional Conservation

Chimeric terpene synthases, which consist of C-terminal prenyltransferase (PT) and N-terminal class I terpene synthase (TS) domains (termed PTTSs here), is unique to fungi and produces structurally diverse di- and sesterterpenes. Prior to this study, 20 PTTSs had been functionally characterized. Our understanding of the origin and functional evolution of PTTS genes is limited. Our systematic search of sequenced fungal genomes among diverse taxa revealed that PTTS genes were restricted to Dikarya. Phylogenetic findings indicated different potential models of the origin and evolution of PTTS genes. One was that PTTS genes originated in the common Dikarya ancestor and then underwent frequent gene loss among various subsequent lineages. To understand their functional evolution, we selected 74 PTTS genes for biochemical characterization in an efficient precursor-providing yeast system employing chassis-based, robot-assisted, high-throughput automatic assembly. We found 34 PTTS genes that encoded active enzymes and collectively produced 24 di- and sesterterpenes. About half of these di- and sesterterpenes were also the products of the 20 known PTTSs, indicating functional conservation, whereas the PTTS products included the previously unknown sesterterpenes, sesterevisene (1), and sesterorbiculene (2), suggesting that a diversity of PTTS products awaits discovery. Separating functional PTTSs into two monophyletic groups implied that an early gene duplication event occurred during the evolution of the PTTS family followed by functional divergence with the characteristics of distinct cyclization mechanisms.

The hrp pathogenicity island of Pseudomonas syringae pv. tomato DC3000 is induced by plant phenolic acids

2015 ◽  
Vol 53 (10) ◽  
pp. 725-731 ◽  
Author(s):  
Jun Seung Lee ◽  
Hye Ryun Ryu ◽  
Ji Young Cha ◽  
Hyung Suk Baik
Keyword(s):  
Pseudomonas Syringae ◽  
Phenolic Acids ◽  
Pathogenicity Island ◽  
Tomato Dc3000

scholarly journals A Draft Genome Sequence of Pseudomonas syringae pv. tomato T1 Reveals a Type III Effector Repertoire Significantly Divergent from That of Pseudomonas syringae pv. tomato DC3000

2009 ◽  
Vol 22 (1) ◽  
pp. 52-62 ◽  
Author(s):  
Nalvo F. Almeida ◽  
Shuangchun Yan ◽  
Magdalen Lindeberg ◽  
David J. Studholme ◽  
David J. Schneider ◽  
...  
Keyword(s):  
Host Range ◽  
Host Specificity ◽  
Pseudomonas Syringae ◽  
Genome Sequence ◽  
Draft Genome ◽  
Draft Genome Sequence ◽  
Tomato Dc3000 ◽  
Type Iii ◽  
Host Range Determination ◽  
Range Determination

Diverse gene products including phytotoxins, pathogen-associated molecular patterns, and type III secreted effectors influence interactions between Pseudomonas syringae strains and plants, with additional yet uncharacterized factors likely contributing as well. Of particular interest are those interactions governing pathogen-host specificity. Comparative genomics of closely related pathogens with different host specificity represents an excellent approach for identification of genes contributing to host-range determination. A draft genome sequence of Pseudomonas syringae pv. tomato T1, which is pathogenic on tomato but nonpathogenic on Arabidopsis thaliana, was obtained for this purpose and compared with the genome of the closely related A. thaliana and tomato model pathogen P. syringae pv. tomato DC3000. Although the overall genetic content of each of the two genomes appears to be highly similar, the repertoire of effectors was found to diverge significantly. Several P. syringae pv. tomato T1 effectors absent from strain DC3000 were confirmed to be translocated into plants, with the well-studied effector AvrRpt2 representing a likely candidate for host-range determination. However, the presence of avrRpt2 was not found sufficient to explain A. thaliana resistance to P. syringae pv. tomato T1, suggesting that other effectors and possibly type III secretion system–independent factors also play a role in this interaction.

scholarly journals Cloning and characterization of α-pinene synthase from Chamaecyparis formosensis Matsum

Holzforschung ◽  
2009 ◽  
Vol 63 (1) ◽  
Author(s):  
Fang-Hua Chu ◽  
Pei-Min Kuo ◽  
Yu-Rong Chen ◽  
Sheng-Yang Wang
Keyword(s):  
Major Product ◽  
Open Reading Frame ◽  
Terpene Synthase ◽  
Geranyl Diphosphate ◽  
Reading Frame ◽  
E Coli ◽  
Phylogenetic Taxonomy ◽  
Chamaecyparis Formosensis ◽  
Pcr Method

AbstractAnalyzing the gene sequences of terpene synthase (TPS) may contribute to a better understanding of terpenes biosynthesis and evolution of phylogenetic taxonomy.Chamaecyparis formosensisis an endemic and precious conifer of Taiwan. To understand the biosynthesis mechanism of terpenes in this tree, a full length of putative mono-TPS, named asCf-Pin(GeneBank accession no. EU099434), was obtained by PCR method and RACE extension. TheCf-Pinhas an 1887-bp open reading frame and encodes 628 amino acids. To identify the function ofCf-Pin,the recombinant protein fromEscherichia coliwas incubated with geranyl diphosphate, produced one major product, the structure of which was elucidated. GC/MS analysis and matching of retention time and mass spectrum with authentic standards revealed that this product isα-pinene. This is the first report of cloning of a mono-TPS and functionally expressed inE. coliand which could be identified asα-pinene synthase from a Cupressaceae conifer.

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