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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
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    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.

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