IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v16y2025i1d10.1038_s41467-025-56864-0.html
   My bibliography  Save this article

Polymerization of proanthocyanidins under the catalysis of miR397a-regulated laccases in Salvia miltiorrhiza and Populus trichocarpa

Author

Listed:
  • Caili Li

    (Chinese Academy of Medical Sciences & Peking Union Medical College)

  • Xiaoxiao Qiu

    (Chinese Academy of Medical Sciences & Peking Union Medical College)

  • Xuemin Hou

    (Chinese Academy of Medical Sciences & Peking Union Medical College)

  • Dongqiao Li

    (Chinese Academy of Medical Sciences & Peking Union Medical College)

  • Maochang Jiang

    (Chinese Academy of Medical Sciences & Peking Union Medical College)

  • Xinyun Cui

    (Chinese Academy of Medical Sciences & Peking Union Medical College)

  • Xian Pan

    (Chinese Academy of Medical Sciences & Peking Union Medical College)

  • Fenjuan Shao

    (Chinese Academy of Forestry)

  • Quanzi Li

    (Zhejiang A & F University)

  • De-Yu Xie

    (North Carolina State University)

  • Vincent L. Chiang

    (North Carolina State University)

  • Shanfa Lu

    (Chinese Academy of Medical Sciences & Peking Union Medical College)

Abstract

Proanthocyanidins (PAs) play significant roles in plants and are bioactive compounds with health benefits. The polymerization mechanism has been debated for decades. Here we show that laccases (LACs) are involved in PA polymerization and miR397a is a negative regulator of PA biosynthesis in Salvia miltiorrhiza and Populus trichocarpa. Elevation of miR397a level causes significant downregulation of LACs, severe reduction of polymerized PAs, and significant increase of flavan-3-ol monomers in transgenic S. miltiorrhiza and P. trichocarpa plants. Enzyme activity analysis shows that miR397a-regulated SmLAC1 catalyzes the polymerization of flavan-3-ols and the conversion of B-type PAs to A-type. Both catechin and epicatechin can serve as the starter unit and the extension unit during PA polymerization. Overexpression of SmLAC1 results in significant increase of PA accumulation, accompanied by the decrease of catechin and epicatechin contents. Consistently, CRISPR/Cas9-mediated SmLAC1 knockout shows the opposite results. Based on these results, a scheme for LAC-catalyzed PA polymerization is proposed. The work provides insights into PA polymerization mechanism.

Suggested Citation

  • Caili Li & Xiaoxiao Qiu & Xuemin Hou & Dongqiao Li & Maochang Jiang & Xinyun Cui & Xian Pan & Fenjuan Shao & Quanzi Li & De-Yu Xie & Vincent L. Chiang & Shanfa Lu, 2025. "Polymerization of proanthocyanidins under the catalysis of miR397a-regulated laccases in Salvia miltiorrhiza and Populus trichocarpa," Nature Communications, Nature, vol. 16(1), pages 1-19, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-56864-0
    DOI: 10.1038/s41467-025-56864-0
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-025-56864-0
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-025-56864-0?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    1. Nan Lu & Ji Hyung Jun & Ying Li & Richard A. Dixon, 2023. "An unconventional proanthocyanidin pathway in maize," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    2. Keji Yu & Richard A. Dixon & Changqing Duan, 2022. "A role for ascorbate conjugates of (+)-catechin in proanthocyanidin polymerization," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    3. Javier F. Palatnik & Edwards Allen & Xuelin Wu & Carla Schommer & Rebecca Schwab & James C. Carrington & Detlef Weigel, 2003. "Control of leaf morphogenesis by microRNAs," Nature, Nature, vol. 425(6955), pages 257-263, September.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.

      More about this item

      Statistics

      Access and download statistics

      Corrections

      All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-56864-0. See general information about how to correct material in RePEc.

      If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

      If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

      If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

      For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

      Please note that corrections may take a couple of weeks to filter through the various RePEc services.

      IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.