TY - JOUR
T1 - A conserved strategy of chalcone isomerase-like protein to rectify promiscuous chalcone synthase specificity
AU - Waki, Toshiyuki
AU - Mameda, Ryo
AU - Nakano, Takuya
AU - Yamada, Sayumi
AU - Terashita, Miho
AU - Ito, Keisuke
AU - Tenma, Natsuki
AU - Li, Yanbing
AU - Fujino, Naoto
AU - Uno, Kaichi
AU - Yamashita, Satoshi
AU - Aoki, Yuichi
AU - Denessiouk, Konstantin
AU - Kawai, Yosuke
AU - Sugawara, Satoko
AU - Saito, Kazuki
AU - Yonekura-Sakakibara, Keiko
AU - Morita, Yasumasa
AU - Hoshino, Atsushi
AU - Takahashi, Seiji
AU - Nakayama, Toru
N1 - Funding Information:
We are grateful to Prof. Richard L. Smith, Graduate School of Environmental Studies, Tohoku University, for his invaluable advice. We thank Edanz Group (www.edanze-diting.com/ac) for editing a draft of this manuscript. This study was supported in part by a JSPS KAKENHI grant (18H03938) and the NIBB Collaborative Research Program (14-388, 15-352, 16-319, 17-332, and 18-337).
Publisher Copyright:
© 2020, The Author(s).
PY - 2020/12/1
Y1 - 2020/12/1
N2 - 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.
AB - 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.
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U2 - 10.1038/s41467-020-14558-9
DO - 10.1038/s41467-020-14558-9
M3 - Article
C2 - 32054839
AN - SCOPUS:85079339338
SN - 2041-1723
VL - 11
JO - Nature Communications
JF - Nature Communications
IS - 1
M1 - 870
ER -