| Autor: |
Waki, Toshiyuki, Mameda, Ryo, Nakano, Takuya, Yamada, Sayumi, Terashita, Miho, Ito, Keisuke, Tenma, Natsuki, Li, Yanbing, Fujino, Naoto, Uno, Kaichi, Yamashita, Satoshi, Aoki, Yuichi, Denessiouk, Konstantin, Kawai, Yosuke, Sugawara, Satoko, Saito, Kazuki, Yonekura-Sakakibara, Keiko, Morita, Yasumasa, Hoshino, Atsushi, Takahashi, Seiji |
| Předmět: |
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| Zdroj: |
Nature Communications; 2/13/2020, Vol. 11 Issue 1, p1-14, 14p |
| Abstrakt: |
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. Chalcone synthase is the first committed enzyme in the plant flavonoid biosynthesis pathway, yet shows low product specificity in vitro. Here Waki et al. show that chalcone isomerase-like proteins bind to and reduce the catalytic promiscuity of chalcone synthase, ensuring efficient flavonoid production in planta. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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