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 TakahashiToru Nakayama

Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review

12 Citeringar (Scopus)

Sammanfattning

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.
OriginalspråkEngelska
Artikelnummer870 (2020)
TidskriftNature Communications
Volym11
Utgåva1
DOI
StatusPublicerad - 2020
MoE-publikationstypA1 Tidskriftsartikel-refererad

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