中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
首页 机构 成果 学者
  
  1. CAS IR Grid
  2. 植物研究所
  3. 中国科学院植物研究所
  4. 中科院北方资源植物重点实验室
热门
Characterization of UGT716A1 as a Multi-substrate UDP: Flavonoid Glucosyltransferase Gene in Ginkgo biloba

文献类型：期刊论文

作者Su, Xiaojia4,5,6; Shen, Guoan4; Di, Shaokang4; Dixon, Richard A.; Pang, Yongzhen4,5
刊名FRONTIERS IN PLANT SCIENCE
出版日期2017
卷号8
关键词Ginkgo biloba flavonoids UGT716A1 multi-substrate UGT EGCG flavanol gallate glycosides
ISSN号1664-462X
DOI10.1038/nature23897
文献子类Article
英文摘要Ginkgo biloba L., a living fossil and medicinal plant, is a well-known rich source of bioactive flavonoids. The molecular mechanism underlying the biosynthesis of flavonoid glucosides, the predominant flavonoids in G. biloba, remains unclear. To better understand flavonoid glucosylation in G. biloba, we generated a transcriptomic dataset of G. biloba leaf tissue by high-throughput RNA sequencing. We identified 25 putative UDP-glycosyltransferase (UGT) unigenes that are potentially involved in the flavonoid glycosylation. Among them, we successfully isolated and expressed eight UGT genes in Escherichia coli, and found that recombinant UGT716A1 protein was active toward broad range of flavonoid/phenylpropanoid substrates. In particular, we discovered the first recombinant UGT protein, UGT716A1 from G. biloba, possessing unique activity toward flavanol gallates that have been extensively documented to have significant bioactivity relating to human health. UGT716A1 expression level paralleled the flavonoid distribution pattern in G. biloba. Ectopic over-expression of UGT716A1 in Arabidopsis thaliana led to increased accumulation of several flavonol glucosides. Identification and comparison of the in vitro enzymatic activity of UGT716A1 homologs revealed a UGT from the primitive land species Physcomitrella patens also showed broader substrate spectrum than those from higher plants A. thaliana, Vitis vinifera, and Medicago truncatula. The characterization of UGT716A1 from G. biloba bridges a gap in the evolutionary history of UGTs in gymnosperms. We also discuss the implication of UGT716A1 for biosynthesis, evolution, and bioengineering of diverse glucosylated flavonoids.
学科主题Science & Technology - Other Topics
出版地LAUSANNE
WOS关键词SECONDARY METABOLISM GLYCOSYLTRANSFERASES ; CHEMICAL-ANALYSIS ; QUALITY-CONTROL ; PLANT ; ARABIDOPSIS ; BIOSYNTHESIS ; TEA ; GENOME ; FAMILY ; IDENTIFICATION
语种英语
WOS记录号WOS:000411381300034
出版者FRONTIERS MEDIA SA
资助机构Major State Basic Research and Development ProgramNational Basic Research Program of China [2013CB127002] ; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31670305] ; Hundred Talents Program of the Chinese Academy of SciencesChinese Academy of Sciences [39391503-7]
源URL[http://ir.ibcas.ac.cn/handle/2S10CLM1/22345]  
专题中科院北方资源植物重点实验室
作者单位1.Dixon, Richard A.] Beijing Forestry Univ, Beijing Adv Innovat Ctr Tree Breeding Mol Design, Beijing, Peoples R China
2.Dixon, Richard A.] Univ North Texas, BioDiscovery Inst, Denton, TX 76203 USA
3.Dixon, Richard A.] Univ North Texas, Dept Biol Sci, Denton, TX 76203 USA
4.Chinese Acad Sci, Key Lab Plant Resources, Inst Bot, Beijing, Peoples R China
5.Chinese Acad Sci, Beijing Bot Garden, Inst Bot, Beijing, Peoples R China
6.Chinese Acad Agr Sci, Inst Anim Sci, Beijing, Peoples R China
7.Univ Chinese Acad Sci, Beijing, Peoples R China
推荐引用方式
GB/T 7714		 Su, Xiaojia,Shen, Guoan,Di, Shaokang,et al. Characterization of UGT716A1 as a Multi-substrate UDP: Flavonoid Glucosyltransferase Gene in Ginkgo biloba[J]. FRONTIERS IN PLANT SCIENCE,2017,8.
APA Su, Xiaojia,Shen, Guoan,Di, Shaokang,Dixon, Richard A.,&Pang, Yongzhen.(2017).Characterization of UGT716A1 as a Multi-substrate UDP: Flavonoid Glucosyltransferase Gene in Ginkgo biloba.FRONTIERS IN PLANT SCIENCE,8.
MLA Su, Xiaojia,et al."Characterization of UGT716A1 as a Multi-substrate UDP: Flavonoid Glucosyltransferase Gene in Ginkgo biloba".FRONTIERS IN PLANT SCIENCE 8(2017).

入库方式： OAI收割

来源：植物研究所

浏览0
下载0
收藏0
其他版本

除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。