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Characterization of two O-methyltransferases involved in the biosynthesis of O-methylated catechins in tea plant

Author

Listed:
  • Ji-Qiang Jin

    (Ministry of Agriculture and Rural Affairs; Tea Research Institute of the Chinese Academy of Agricultural Sciences)

  • Fu-Rong Qu

    (Ministry of Agriculture and Rural Affairs; Tea Research Institute of the Chinese Academy of Agricultural Sciences)

  • Huisi Huang

    (Jinan University)

  • Qing-Shuai Liu

    (Ministry of Agriculture and Rural Affairs; Tea Research Institute of the Chinese Academy of Agricultural Sciences)

  • Meng-Yuan Wei

    (Ministry of Agriculture and Rural Affairs; Tea Research Institute of the Chinese Academy of Agricultural Sciences)

  • Yuee Zhou

    (Jinan University)

  • Ke-Lin Huang

    (Anhui Agricultural University)

  • Zhibo Cui

    (Jinan University)

  • Jie-Dan Chen

    (Ministry of Agriculture and Rural Affairs; Tea Research Institute of the Chinese Academy of Agricultural Sciences)

  • Wei-Dong Dai

    (Ministry of Agriculture and Rural Affairs; Tea Research Institute of the Chinese Academy of Agricultural Sciences)

  • Li Zhu

    (Ministry of Agriculture and Rural Affairs; Tea Research Institute of the Chinese Academy of Agricultural Sciences)

  • Ming-Zhe Yao

    (Ministry of Agriculture and Rural Affairs; Tea Research Institute of the Chinese Academy of Agricultural Sciences)

  • Zhi-Min Zhang

    (Jinan University)

  • Liang Chen

    (Ministry of Agriculture and Rural Affairs; Tea Research Institute of the Chinese Academy of Agricultural Sciences)

Abstract

Tea is known for having a high catechin content, with the main component being (−)-epigallocatechin gallate (EGCG), which has significant bioactivities, including potential anti-cancer and anti-inflammatory activity. The poor intestinal stability and permeability of EGCG, however, undermine these health-improving benefits. O-methylated EGCG derivatives, found in a few tea cultivars in low levels, have attracted considerable interest due to their increased bioavailability. Here, we identify two O-methyltransferases from tea plant: CsFAOMT1 that has a specific O-methyltransferase activity on the 3ʹʹ-position of EGCG to generate EGCG3′′Me, and CsFAOMT2 that predominantly catalyzes the formation of EGCG4″Me. In different tea tissues and germplasms, the transcript levels of CsFAOMT1 and CsFAOMT2 are strongly correlated with the amounts of EGCG3ʹʹMe and EGCG4ʹʹMe, respectively. Furthermore, the crystal structures of CsFAOMT1 and CsFAOMT2 reveal the key residues necessary for 3ʹʹ- and 4ʹʹ-O-methylation. These findings may provide guidance for the future development of tea cultivars with high O-methylated catechin content.

Suggested Citation

  • Ji-Qiang Jin & Fu-Rong Qu & Huisi Huang & Qing-Shuai Liu & Meng-Yuan Wei & Yuee Zhou & Ke-Lin Huang & Zhibo Cui & Jie-Dan Chen & Wei-Dong Dai & Li Zhu & Ming-Zhe Yao & Zhi-Min Zhang & Liang Chen, 2023. "Characterization of two O-methyltransferases involved in the biosynthesis of O-methylated catechins in tea plant," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-40868-9
    DOI: 10.1038/s41467-023-40868-9
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    References listed on IDEAS

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    1. Weiyi Zhang & Youjun Zhang & Haiji Qiu & Yafei Guo & Haoliang Wan & Xiaoliang Zhang & Federico Scossa & Saleh Alseekh & Qinghua Zhang & Pu Wang & Li Xu & Maximilian H-W Schmidt & Xinxin Jia & Daili Li, 2020. "Genome assembly of wild tea tree DASZ reveals pedigree and selection history of tea varieties," Nature Communications, Nature, vol. 11(1), pages 1-12, December.
    2. Xinchao Wang & Hu Feng & Yuxiao Chang & Chunlei Ma & Liyuan Wang & Xinyuan Hao & A’lun Li & Hao Cheng & Lu Wang & Peng Cui & Jiqiang Jin & Xiaobo Wang & Kang Wei & Cheng Ai & Sheng Zhao & Zhichao Wu &, 2020. "Population sequencing enhances understanding of tea plant evolution," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
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    Cited by:

    1. Simon d’Oelsnitz & Daniel J. Diaz & Wantae Kim & Daniel J. Acosta & Tyler L. Dangerfield & Mason W. Schechter & Matthew B. Minus & James R. Howard & Hannah Do & James M. Loy & Hal S. Alper & Y. Jessie, 2024. "Biosensor and machine learning-aided engineering of an amaryllidaceae enzyme," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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