Journal
FRONTIERS IN PLANT SCIENCE
Volume 13, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fpls.2022.852377
Keywords
gypenosides; oxidosqualene cyclase; cytochrome P450 monooxygenase; dammarenediol II synthase; Gynostemma longipes
Categories
Funding
- National Key RD Plan [2017YFC1702500]
- Major Science and Technique Programs in Yunnan Province [2019ZF011-1]
- Science and Technology Innovation team of Yunnan [202105AE160011]
- Yunnan Provincial Key Programs of Eco-friendly Food International Cooperation Research Center Project [2019ZG00901]
- Natural Science Foundation of Yunnan Province [202001AT070125]
- National Natural Science Foundation of China [31701854]
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This study conducted an integrative analysis of the metabolome and transcriptome in Gynostemma longipes, uncovering the biosynthetic pathway of ginsenosides and gypenosides. Additionally, a new dammarane-II synthase was identified, which may contribute to increasing the yield of these valuable compounds.
Gynostemma longipes contains an abundance of dammarane-type ginsenosides and gypenosides that exhibit extensive pharmacological activities. Increasing attention has been paid to the elucidation of cytochrome P450 monooxygenases (CYPs) and UDP-dependent glycosyltransferases (UGTs) that participate downstream of ginsenoside biosynthesis in the Panax genus. However, information on oxidosqualene cyclases (OSCs), the upstream genes responsible for the biosynthesis of different skeletons of ginsenoside and gypenosides, is rarely reported. Here, an integrative study of the metabolome and the transcriptome in the leaf, stolon, and rattan was conducted and the function of GlOSC1 was demonstrated. In total, 46 triterpenes were detected and found to be highly abundant in the stolon, whereas gene expression analysis indicated that the upstream OSC genes responsible for saponin skeleton biosynthesis were highly expressed in the leaf. These findings indicated that the saponin skeletons were mainly biosynthesized in the leaf by OSCs, and subsequently transferred to the stolon via CYPs and UGTs biosynthesis to form various ginsenoside and gypenosides. Additionally, a new dammarane-II synthase (DDS), GlOSC1, was identified by bioinformatics analysis, yeast expression assay, and enzyme assays. The results of the liquid chromatography-mass spectrometry (LC-MS) analysis proved that GlOSC1 could catalyze 2,3-oxidosqualene to form dammarenediol-II via cyclization. This work uncovered the biosynthetic mechanism of dammarenediol-II, an important starting substrate for ginsenoside and gypenosides biosynthesis, and may achieve the increased yield of valuable ginsenosides and gypenosides produced under excess substrate in a yeast cell factory through synthetic biology strategy.
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