Multi-omics reveal key enzymes involved in the formation of phenylpropanoid glucosides in Artemisia annua

Yin, Qinggang; Wu, Tianze; Gao, Ranran; Wu, Lan; Shi, Yuhua; Wang, Xinwen; Wang, Mengyue; Xu, Zhichao; Zhao, Yueliang; Su, Xiaojia; Su, Yanyan; Han, Xiaoyan; Yuan, Ling; Li, Xiang; Chen, Shilin

doi:10.1016/j.plaphy.2023.107795

Cited by 2 publications

(1 citation statement)

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“…The process of methylation is catalyzed using a methyltransferase that transfers a methyl group from S-adenosyl-L-methionine to an appropriate substrate. O-methylation occurs as one vital step in many plants' secondary metabolic biosynthesis, which involves flavonoids [9,10], terpenoids [11,12], and alkaloids [13,14]. O-methyltransferase is responsible for the formation of the structural diversity of flavonoids through methylation in plants.…”

Section: Introductionmentioning

confidence: 99%

Identification of One O-Methyltransferase Gene Involved in Methylated Flavonoid Biosynthesis Related to the UV-B Irradiation Response in Euphorbia lathyris

Zhao,

Huang,

et al. 2024

IJMS

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Flavonoids are ubiquitous polyphenolic compounds that play a vital role in plants’ defense response and medicinal efficacy. UV-B radiation is a vital environmental regulator governing flavonoid biosynthesis in plants. Many plants rapidly biosynthesize flavonoids as a response to UV-B stress conditions. Here, we investigated the effects of flavonoid biosynthesis via UV-B irradiation in Euphorbia lathyris. We found that exposure of the E. lathyris callus to UV-B radiation sharply increased the level of one O-methyltransferase (ElOMT1) transcript and led to the biosynthesis of several methylated flavonoids. The methyltransferase ElOMT1 was expressed heterologously in E. coli, and we tested the catalytic activity of recombinant ElOMT1 with possible substrates, including caffeic acid, baicalin, and luteolin, in vitro. ElOMT1 could efficiently methylate when the hydroxyl groups were contained in the core nucleus of the flavonoid. This molecular characterization identifies a methyltransferase responsible for the chemical modification of the core flavonoid structure through methylation and helps reveal the mechanism of methylated flavonoid biosynthesis in Euphorbiaceae. This study identifies the O-methyltransferase that responds to UV-B irradiation and helps shed light on the mechanism of flavonoid biosynthesis in Euphorbia lathyris.

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