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Versatility in acyltransferase activity completes chicoric acid biosynthesis in purple coneflower

Author

Listed:
  • Rao Fu

    (Sichuan University)

  • Pingyu Zhang

    (Sichuan University)

  • Ge Jin

    (Sichuan University)

  • Lianglei Wang

    (Sichuan University)

  • Shiqian Qi

    (Sichuan University, and Collaborative Innovation Center for Biotherapy)

  • Yang Cao

    (Sichuan University)

  • Cathie Martin

    (Department of Metabolic Biology and Biological Chemistry, John Innes Centre)

  • Yang Zhang

    (Sichuan University)

Abstract

Purple coneflower (Echinacea purpurea (L.) Moench) is a popular native North American herbal plant. Its major bioactive compound, chicoric acid, is reported to have various potential physiological functions, but little is known about its biosynthesis. Here, taking an activity-guided approach, we identify two cytosolic BAHD acyltransferases that form two intermediates, caftaric acid and chlorogenic acid. Surprisingly, a unique serine carboxypeptidase-like acyltransferase uses chlorogenic acid as its acyl donor and caftaric acid as its acyl acceptor to produce chicoric acid in vacuoles, which has evolved its acyl donor specificity from the better-known 1-O-β-D-glucose esters typical for this specific type of acyltransferase to chlorogenic acid. This unusual pathway seems unique to Echinacea species suggesting convergent evolution of chicoric acid biosynthesis. Using these identified acyltransferases, we have reconstituted chicoric acid biosynthesis in tobacco. Our results emphasize the flexibility of acyltransferases and their roles in the evolution of specialized metabolism in plants.

Suggested Citation

  • Rao Fu & Pingyu Zhang & Ge Jin & Lianglei Wang & Shiqian Qi & Yang Cao & Cathie Martin & Yang Zhang, 2021. "Versatility in acyltransferase activity completes chicoric acid biosynthesis in purple coneflower," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-21853-6
    DOI: 10.1038/s41467-021-21853-6
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    Cited by:

    1. Junlan Zeng & Xiaoqiang Liu & Zhaoyue Dong & Fangyuan Zhang & Fei Qiu & Mingyu Zhong & Tengfei Zhao & Chunxian Yang & Lingjiang Zeng & Xiaozhong Lan & Hongbo Zhang & Junhui Zhou & Min Chen & Kexuan Ta, 2024. "Discovering a mitochondrion-localized BAHD acyltransferase involved in calystegine biosynthesis and engineering the production of 3β-tigloyloxytropane," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    2. Zixin Zhang & Xin Zhang & Yuting Chen & Wenqian Jiang & Jing Zhang & Jiayu Wang & Yanjun Wu & Shouchuang Wang & Xiao Yang & Mingchun Liu & Yang Zhang, 2023. "Understanding the mechanism of red light-induced melatonin biosynthesis facilitates the engineering of melatonin-enriched tomatoes," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    3. Wenna Li & Zhao Zhou & Xianglai Li & Lin Ma & Qingyuan Guan & Guojun Zheng & Hao Liang & Yajun Yan & Xiaolin Shen & Jia Wang & Xinxiao Sun & Qipeng Yuan, 2022. "Biosynthesis of plant hemostatic dencichine in Escherichia coli," Nature Communications, Nature, vol. 13(1), pages 1-9, December.

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