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; Toru Nakayama

doi:10.1038/s41467-020-14558-9

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

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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.

Original language	English
Article number	870 (2020)
Journal	Nature Communications
Volume	11
Issue number	1
DOIs	https://doi.org/10.1038/s41467-020-14558-9
Publication status	Published - 2020
MoE publication type	A1 Journal article-refereed

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s41467-020-14558-9Final published version, 2.16 MBLicence: CC BY

https://urn.fi/URN:NBN:fi-fe202201148176

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Waki, T., Mameda, R., Nakano, T., Yamada, S., Terashita, M., Ito, K., Tenma, N., Li, Y., Fujino, N., Uno, K., Yamashita, S., Aoki, Y., Denessiouk, K., Kawai, Y., Sugawara, S., Saito, K., Yonekura-Sakakibara, K., Morita, Y., Hoshino, A., ... Nakayama, T. (2020). A conserved strategy of chalcone isomerase-like protein to rectify promiscuous chalcone synthase specificity. Nature Communications, 11(1), Article 870 (2020). https://doi.org/10.1038/s41467-020-14558-9

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title = "A conserved strategy of chalcone isomerase-like protein to rectify promiscuous chalcone synthase specificity",

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.",

author = "Toshiyuki Waki and Ryo Mameda and Takuya Nakano and Sayumi Yamada and Miho Terashita and Keisuke Ito and Natsuki Tenma and Yanbing Li and Naoto Fujino and Kaichi Uno and Satoshi Yamashita and Yuichi Aoki and Konstantin Denessiouk and Yosuke Kawai and Satoko Sugawara and Kazuki Saito and Keiko Yonekura-Sakakibara and Yasumasa Morita and Atsushi Hoshino and Seiji Takahashi and Toru Nakayama",

year = "2020",

doi = "10.1038/s41467-020-14558-9",

language = "English",

volume = "11",

journal = "Nature Communications",

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Waki, T, Mameda, R, Nakano, T, Yamada, S, Terashita, M, Ito, K, Tenma, N, Li, Y, Fujino, N, Uno, K, Yamashita, S, Aoki, Y, Denessiouk, K, Kawai, Y, Sugawara, S, Saito, K, Yonekura-Sakakibara, K, Morita, Y, Hoshino, A, Takahashi, S & Nakayama, T 2020, 'A conserved strategy of chalcone isomerase-like protein to rectify promiscuous chalcone synthase specificity', Nature Communications, vol. 11, no. 1, 870 (2020). https://doi.org/10.1038/s41467-020-14558-9

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

PY - 2020

Y1 - 2020

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.

U2 - 10.1038/s41467-020-14558-9

DO - 10.1038/s41467-020-14558-9

M3 - Article

SN - 2041-1723

VL - 11

JO - Nature Communications

JF - Nature Communications

IS - 1

M1 - 870 (2020)

ER -

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

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