Title Analysis of the role of geranylgeranyl diphosphate synthase 8 from Tripterygium wilfordii in diterpenoids biosynthesis
Authors Su, Ping
Gao, Linhui
Tong, Yuru
Guan, Hongyu
Liu, Shuang
Zhang, Yifeng
Zhao, Yujun
Wang, Jiadian
Hu, Tianyuan
Tu, Lichan
Zhou, Jiawei
Ma, Baowei
Huang, Luqi
Gao, Wei
Affiliation Chinese Acad Chinese Med Sci, Natl Resource Ctr Chinese Mat Med, State Key Lab Dao di Herbs, Beijing 100700, Peoples R China
Capital Med Univ, Sch Tradit Chinese Med, Beijing 100069, Peoples R China
Shenyang Pharmaceut Univ, Sch Tradit Chinese Mat Med, Shenyang 110016, Liaoning, Peoples R China
Beijing Univ Chinese Med, Affiliated Hosp 3, Beijing 100029, Peoples R China
Peking Univ, Sch Pharmaceut Sci, State Key Lab Nat & Biomimet Drugs, Beijing 100191, Peoples R China
Keywords Tripterygium wilfordii
Geranylgeranyl diphosphate synthase
Geranyl diphosphate synthase small subunit
Subunit interactions
Engineering bacteria
Issue Date 2019
Publisher PLANT SCIENCE
Abstract Tripterygium wilfordii is known to contain various types of bioactive diterpenoids that exhibit many remarkable activities. Many studies have recently been targeted toward the elucidation of the diterpenoids biosynthetic pathways in attempts to obtain these compounds with a view to solving the dilemma of low yield in plants. However, the short-chain prenyltransferases (SC-PTSs) responsible for the formation of geranylgeranyl diphosphate (GGPP), a crucial precursor for synthesizing the skeleton structures of diterpenoids, have not been characterized in depth. Here, T. wilfordii transcriptome data were used to identify eight putative GGPPSs, including two small subunits of geranyl diphosphate synthase (GPPS.SSU). Of them, GGPPS1, GGPPS7, GGPPS8, GPPS.SSU II and GPPS.SSU were translocated mainly into chloroplasts, and GGPPS8 exhibited the optimal catalytic efficiency with respect to catalyzing the formation of GGPP. In addition, the expression pattern of GGPPS8 was similar to that of downstream terpene synthase genes that are directly correlated with triptolide production in roots, indicating that GGPPS8 was most likely to participate in triptolide biosynthesis in roots among the studied enzymes. GPPS.SSU was inactive alone but interacted with GGPPS1, GGPPS7 and GGPPS8 to change the product from GGPP to GPP. These findings implicate that these candidate genes can be regulated to shift the metabolic flux toward diterpenoid formation, increasing the yields of bioactive diterpenoids in plants.
URI http://hdl.handle.net/20.500.11897/546394
ISSN 0168-9452
DOI 10.1016/j.plantsci.2019.05.013
Indexed SCI(E)
EI
Appears in Collections: 药学院
天然药物与仿生药物国家重点实验室

Files in This Work
There are no files associated with this item.

Web of Science®


0

Checked on Last Week

Scopus®



Checked on Current Time

百度学术™


0

Checked on Current Time

Google Scholar™





License: See PKU IR operational policies.