Functional Characterization of Sesquiterpene Synthase from Polygonum minus
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 g...
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| Language: | English |
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Wiley
2014-01-01
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| Series: | The Scientific World Journal |
| Online Access: | http://dx.doi.org/10.1155/2014/840592 |
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| author | Su-Fang Ee Zeti-Azura Mohamed-Hussein Roohaida Othman Noor Azmi Shaharuddin Ismanizan Ismail Zamri Zainal |
| author_facet | Su-Fang Ee Zeti-Azura Mohamed-Hussein Roohaida Othman Noor Azmi Shaharuddin Ismanizan Ismail Zamri Zainal |
| author_sort | Su-Fang Ee |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-23cd7b318e3548138626f7394a2241fc |
| institution | Kabale University |
| issn | 2356-6140 1537-744X |
| language | English |
| publishDate | 2014-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | The Scientific World Journal |
| spelling | doaj-art-23cd7b318e3548138626f7394a2241fc2025-02-03T01:09:27ZengWileyThe Scientific World Journal2356-61401537-744X2014-01-01201410.1155/2014/840592840592Functional Characterization of Sesquiterpene Synthase from Polygonum minusSu-Fang Ee0Zeti-Azura Mohamed-Hussein1Roohaida Othman2Noor Azmi Shaharuddin3Ismanizan Ismail4Zamri Zainal5School of Biosciences and Biotechnology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600 Bangi, Selangor, MalaysiaSchool of Biosciences and Biotechnology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600 Bangi, Selangor, MalaysiaSchool of Biosciences and Biotechnology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600 Bangi, Selangor, MalaysiaFaculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 Serdang, Selangor, MalaysiaSchool of Biosciences and Biotechnology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600 Bangi, Selangor, MalaysiaSchool of Biosciences and Biotechnology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600 Bangi, Selangor, MalaysiaPolygonum 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.http://dx.doi.org/10.1155/2014/840592 |
| spellingShingle | Su-Fang Ee Zeti-Azura Mohamed-Hussein Roohaida Othman Noor Azmi Shaharuddin Ismanizan Ismail Zamri Zainal Functional Characterization of Sesquiterpene Synthase from Polygonum minus The Scientific World Journal |
| title | Functional Characterization of Sesquiterpene Synthase from Polygonum minus |
| title_full | Functional Characterization of Sesquiterpene Synthase from Polygonum minus |
| title_fullStr | Functional Characterization of Sesquiterpene Synthase from Polygonum minus |
| title_full_unstemmed | Functional Characterization of Sesquiterpene Synthase from Polygonum minus |
| title_short | Functional Characterization of Sesquiterpene Synthase from Polygonum minus |
| title_sort | functional characterization of sesquiterpene synthase from polygonum minus |
| url | http://dx.doi.org/10.1155/2014/840592 |
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