IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v11y2020i1d10.1038_s41467-020-14558-9.html
   My bibliography  Save this article

A conserved strategy of chalcone isomerase-like protein to rectify promiscuous chalcone synthase specificity

Author

Listed:
  • Toshiyuki Waki

    (Tohoku University)

  • Ryo Mameda

    (Tohoku University)

  • Takuya Nakano

    (Tohoku University)

  • Sayumi Yamada

    (Tohoku University)

  • Miho Terashita

    (Tohoku University)

  • Keisuke Ito

    (Tohoku University)

  • Natsuki Tenma

    (Tohoku University)

  • Yanbing Li

    (Tohoku University)

  • Naoto Fujino

    (Tohoku University)

  • Kaichi Uno

    (Tohoku University)

  • Satoshi Yamashita

    (Kanazawa University)

  • Yuichi Aoki

    (Tohoku Medical Megabank Organization)

  • Konstantin Denessiouk

    (Åbo Akademi University)

  • Yosuke Kawai

    (National Center for Global Health and Medicine)

  • Satoko Sugawara

    (The RIKEN Center for Sustainable Resource Science)

  • Kazuki Saito

    (The RIKEN Center for Sustainable Resource Science)

  • Keiko Yonekura-Sakakibara

    (The RIKEN Center for Sustainable Resource Science)

  • Yasumasa Morita

    (Meijo University)

  • Atsushi Hoshino

    (National Institute for Basic Biology)

  • Seiji Takahashi

    (Tohoku University)

  • Toru Nakayama

    (Tohoku University)

Abstract

Land plants produce diverse flavonoids for growth, survival, and reproduction. Chalcone synthase is the first committed enzyme of the flavonoid biosynthetic pathway and catalyzes the production of 2′,4,4′,6′-tetrahydroxychalcone (THC). However, it also produces other polyketides, including p-coumaroyltriacetic acid lactone (CTAL), because of the derailment of the chalcone-producing pathway. This promiscuity of CHS catalysis adversely affects the efficiency of flavonoid biosynthesis, although it is also believed to have led to the evolution of stilbene synthase and p-coumaroyltriacetic acid synthase. In this study, we establish that chalcone isomerase-like proteins (CHILs), which are encoded by genes that are ubiquitous in land plant genomes, bind to CHS to enhance THC production and decrease CTAL formation, thereby rectifying the promiscuous CHS catalysis. This CHIL function has been confirmed in diverse land plant species, and represents a conserved strategy facilitating the efficient influx of substrates from the phenylpropanoid pathway to the flavonoid pathway.

Suggested Citation

  • Toshiyuki Waki & Ryo Mameda & Takuya Nakano & Sayumi Yamada & Miho Terashita & Keisuke Ito & Natsuki Tenma & Yanbing Li & Naoto Fujino & Kaichi Uno & Satoshi Yamashita & Yuichi Aoki & Konstantin Denes, 2020. "A conserved strategy of chalcone isomerase-like protein to rectify promiscuous chalcone synthase specificity," Nature Communications, Nature, vol. 11(1), pages 1-14, December.
  • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14558-9
    DOI: 10.1038/s41467-020-14558-9
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-020-14558-9
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-020-14558-9?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
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Colin Y. Kim & Andrew J. Mitchell & David W. Kastner & Claire E. Albright & Michael A. Gutierrez & Christopher M. Glinkerman & Heather J. Kulik & Jing-Ke Weng, 2023. "Emergence of a proton exchange-based isomerization and lactonization mechanism in the plant coumarin synthase COSY," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

    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:11:y:2020:i:1:d:10.1038_s41467-020-14558-9. 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.

    We have no bibliographic references for this item. You can help adding them by using 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.