A Geranylfarnesyl Diphosphate Synthase Provides the Precursor for Sesterterpenoid (C25) Formation in the Glandular Trichomes of the Mint Species Leucosceptrum canum. Issue 3 (3rd March 2016)
- Record Type:
- Journal Article
- Title:
- A Geranylfarnesyl Diphosphate Synthase Provides the Precursor for Sesterterpenoid (C25) Formation in the Glandular Trichomes of the Mint Species Leucosceptrum canum. Issue 3 (3rd March 2016)
- Main Title:
- A Geranylfarnesyl Diphosphate Synthase Provides the Precursor for Sesterterpenoid (C25) Formation in the Glandular Trichomes of the Mint Species Leucosceptrum canum
- Authors:
- Liu, Yan
Luo, Shi-Hong
Schmidt, Axel
Wang, Guo-Dong
Sun, Gui-Ling
Grant, Marcus
Kuang, Ce
Yang, Min-Jie
Jing, Shu-Xi
Li, Chun-Huan
Schneider, Bernd
Gershenzon, Jonathan
Li, Sheng-Hong - Abstract:
- Abstract : The biosynthesis pathway to the C25 linear precursor of defensive sesterterpenoids, which highly accumulate in glandular trichomes of Leucosceptrum canum, was revealed through transcriptomic analysis. Abstract: Plant sesterterpenoids, an important class of terpenoids, are widely distributed in various plants, including food crops. However, little is known about their biosynthesis. Here, we cloned and functionally characterized a plant geranylfarnesyl diphosphate synthase (Lc-GFDPS), the enzyme producing the C25 prenyl diphosphate precursor to all sesterterpenoids, from the glandular trichomes of the woody plant Leucosceptrum canum . GFDPS catalyzed the formation of GFDP after expression in Escherichia coli . Overexpressing GFDPS in Arabidopsis thaliana also gave an extract catalyzing GFDP formation. GFDPS was strongly expressed in glandular trichomes, and its transcript profile was completely in accordance with the sesterterpenoid accumulation pattern. GFDPS is localized to the plastids, and inhibitor studies indicated its use of isoprenyl diphosphate substrates supplied by the 2-C-methyl-d -erythritol 4-phosphate pathway. Application of a jasmonate defense hormone induced GFDPS transcript and sesterterpenoid accumulation, while reducing feeding and growth of the generalist insect Spodoptera exigua, suggesting that these C25 terpenoids play a defensive role. Phylogenetic analysis suggested that GFDPS probably evolved from plant geranylgeranyl diphosphate synthaseAbstract : The biosynthesis pathway to the C25 linear precursor of defensive sesterterpenoids, which highly accumulate in glandular trichomes of Leucosceptrum canum, was revealed through transcriptomic analysis. Abstract: Plant sesterterpenoids, an important class of terpenoids, are widely distributed in various plants, including food crops. However, little is known about their biosynthesis. Here, we cloned and functionally characterized a plant geranylfarnesyl diphosphate synthase (Lc-GFDPS), the enzyme producing the C25 prenyl diphosphate precursor to all sesterterpenoids, from the glandular trichomes of the woody plant Leucosceptrum canum . GFDPS catalyzed the formation of GFDP after expression in Escherichia coli . Overexpressing GFDPS in Arabidopsis thaliana also gave an extract catalyzing GFDP formation. GFDPS was strongly expressed in glandular trichomes, and its transcript profile was completely in accordance with the sesterterpenoid accumulation pattern. GFDPS is localized to the plastids, and inhibitor studies indicated its use of isoprenyl diphosphate substrates supplied by the 2-C-methyl-d -erythritol 4-phosphate pathway. Application of a jasmonate defense hormone induced GFDPS transcript and sesterterpenoid accumulation, while reducing feeding and growth of the generalist insect Spodoptera exigua, suggesting that these C25 terpenoids play a defensive role. Phylogenetic analysis suggested that GFDPS probably evolved from plant geranylgeranyl diphosphate synthase under the influence of positive selection. The isolation of GFDPS provides a model for investigating sesterterpenoid formation in other species and a tool for manipulating the formation of this group in plants and other organisms. … (more)
- Is Part Of:
- The Plant Cell. Volume 28:Issue 3(2016)
- Journal:
- The Plant Cell
- Issue:
- Volume 28:Issue 3(2016)
- Issue Display:
- Volume 28, Issue 3 (2016)
- Year:
- 2016
- Volume:
- 28
- Issue:
- 3
- Issue Sort Value:
- 2016-0028-0003-0000
- Page Start:
- 804
- Page End:
- 822
- Publication Date:
- 2016-03-03
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.15.00715 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16359.xml