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

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 Denessiouk, Yosuke Kawai, Satoko Sugawara, Kazuki Saito, Keiko Yonekura-Sakakibara, Yasumasa Morita, Atsushi Hoshino, Seiji Takahashi and Toru Nakayama ()
Additional contact information
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

Nature Communications, 2020, vol. 11, issue 1, 1-14

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-14558-9

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