A conserved strategy of chalcone isomerase-like protein to rectify promiscuous chalcone synthase specificity
| Autor: | Yasumasa Morita, Konstantin Denessiouk, Takuya Nakano, Miho Terashita, Kazuki Saito, Naoto Fujino, Satoshi Yamashita, Natsuki Tenma, Sayumi Yamada, Keisuke Ito, Toshiyuki Waki, Keiko Yonekura-Sakakibara, Satoko Sugawara, Yanbing Li, Atsushi Hoshino, Yosuke Kawai, Toru Nakayama, Seiji Takahashi, Ryo Mameda, Kaichi Uno, Yuichi Aoki |
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| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0106 biological sciences
0301 basic medicine Flavonoid Arabidopsis General Physics and Astronomy 01 natural sciences Biochemistry Substrate Specificity chemistry.chemical_compound Chalcones heterocyclic compounds lcsh:Science Intramolecular Lyases Plant Proteins chemistry.chemical_classification Multidisciplinary biology ATP synthase Phenylpropanoid food and beverages Plants Genetically Modified Chalcone synthase Chalcone isomerase Chalcone Evolution Science Genes Plant General Biochemistry Genetics and Molecular Biology Article Evolution Molecular 03 medical and health sciences Flavonoids fungi Genetic Complementation Test General Chemistry Biosynthetic Pathways Kinetics 030104 developmental biology Flavonoid biosynthesis Enzyme chemistry Polyketides biology.protein Biocatalysis Embryophyta lcsh:Q Plant sciences Acyltransferases 010606 plant biology & botany |
| Zdroj: | Nature Communications Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020) |
| ISSN: | 2041-1723 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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