ArticleTheScientificWorldJournal2014
Functional characterization of sesquiterpene synthase from Polygonum minus.
Article in TheScientificWorldJournal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 28 citations in OpenAlex.
- Molecular insights into Valencene synthase (SgTPS-V) and its role in sesquiterpenoid biosynthesis.BMC plant biology · 2026Article
- Cloning and functional identification of sesquiterpene synthase geneFrontiers in plant science · 2025Article
- Cloning, Expression and Functional Characterization of a Novel α-Humulene Synthase, Responsible for the Formation of Sesquiterpene in Agarwood Originating fromCurrent issues in molecular biology · 2023Article
- Cloning and Characterization of 1,8-Cineole Synthase (Frontiers in plant science · 2022Article
- Article
- MicroRNAs Roles in Plants Secondary Metabolism.Plant signaling & behavior · 2021Review
- Regulation of terpenoid biosynthesis by miRNA in Persicaria minor induced by Fusarium oxysporum.BMC genomics · 2019Article
- De novo transcriptome sequencing and metabolite profiling analyses reveal the complex metabolic genes involved in the terpenoid biosynthesis in Blue Anise Sage (Salvia guaranitica L.).DNA research : an international journal for rapid publication of reports on genes and genomes · 2018Article
- Article
- Identification and characterization of a novel sesquiterpene synthase, 4-amorphen-11-ol synthase, fromPlant biotechnology (Tokyo, Japan) · 2018Article
- Functional Characterisation of New Sesquiterpene Synthase from the Malaysian Herbal Plant,Molecules (Basel, Switzerland) · 2018Article
- Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Polygonum minus is an aromatic plant, which contains high abundance of terpenoids, especially the sesquiterpenes C15H24. Sesquiterpenes were believed to contribute to the many useful biological properties in plants. This study aimed to functionally characterize a full length sesquiterpene synthase gene from P. minus. P. minus sesquiterpene synthase (PmSTS) has a complete open reading frame (ORF) of 1689 base pairs encoding a 562 amino acid protein. Similar to other sesquiterpene synthases, PmSTS has two large domains: the N-terminal domain and the C-terminal metal-binding domain. It also consists of three conserved motifs: the DDXXD, NSE/DTE, and RXR. A three-dimensional protein model for PmSTS built clearly distinguished the two main domains, where conserved motifs were highlighted. We also constructed a phylogenetic tree, which showed that PmSTS belongs to the angiosperm sesquiterpene synthase subfamily Tps-a. To examine the function of PmSTS, we expressed this gene in Arabidopsis thaliana. Two transgenic lines, designated as OE3 and OE7, were further characterized, both molecularly and functionally. The transgenic plants demonstrated smaller basal rosette leaves, shorter and fewer flowering stems, and fewer seeds compared to wild type plants. Gas chromatography-mass spectrometry analysis of the transgenic plants showed that PmSTS was responsible for the production of β -sesquiphellandrene.
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