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A conserved strategy of chalcone isomerase-like protein to rectify promiscuous chalcone synthase specificity.
Nature Communications ( IF 14.7 ) Pub Date : 2020-02-13 , DOI: 10.1038/s41467-020-14558-9 Toshiyuki Waki 1 , Ryo Mameda 1 , Takuya Nakano 1 , Sayumi Yamada 1 , Miho Terashita 1 , Keisuke Ito 1 , Natsuki Tenma 1 , Yanbing Li 1 , Naoto Fujino 1 , Kaichi Uno 1 , Satoshi Yamashita 2 , Yuichi Aoki 3 , Konstantin Denessiouk 4 , Yosuke Kawai 5 , Satoko Sugawara 6 , Kazuki Saito 6 , Keiko Yonekura-Sakakibara 6 , Yasumasa Morita 7 , Atsushi Hoshino 8 , Seiji Takahashi 1 , Toru Nakayama 1
Nature Communications ( IF 14.7 ) Pub Date : 2020-02-13 , DOI: 10.1038/s41467-020-14558-9 Toshiyuki Waki 1 , Ryo Mameda 1 , Takuya Nakano 1 , Sayumi Yamada 1 , Miho Terashita 1 , Keisuke Ito 1 , Natsuki Tenma 1 , Yanbing Li 1 , Naoto Fujino 1 , Kaichi Uno 1 , Satoshi Yamashita 2 , Yuichi Aoki 3 , Konstantin Denessiouk 4 , Yosuke Kawai 5 , Satoko Sugawara 6 , Kazuki Saito 6 , Keiko Yonekura-Sakakibara 6 , Yasumasa Morita 7 , Atsushi Hoshino 8 , Seiji Takahashi 1 , Toru Nakayama 1
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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.
中文翻译：
查尔酮异构酶样蛋白的保守策略，以纠正混杂查尔酮合酶的特异性。
陆地植物产生各种黄酮类化合物以促进生长，存活和繁殖。查尔酮合酶是类黄酮生物合成途径中第一个固定的酶，并催化2'，4,4'，6'-四羟基查尔酮（THC）的产生。但是，由于查尔酮生成途径的脱轨，它还会生成其他聚酮化合物，包括对香豆酰基三乙酸内酯（CTAL）。CHS催化的这种混杂性不利地影响了类黄酮生物合成的效率，尽管也认为它导致了二苯乙烯合酶和对香豆酰三乙酸合酶的进化。在这项研究中，我们建立了查尔酮异构酶样蛋白（CHIL），该蛋白由陆地植物基因组中普遍存在的基因编码，可与CHS结合以增强THC生成并减少CTAL形成，从而纠正了混杂的CHS催化。这种CHIL功能已在多种陆地植物物种中得到证实，并且代表了一种保守的策略，可促进底物从苯丙烷类途径向类黄酮途径的有效流入。
更新日期：2020-02-13
中文翻译：
查尔酮异构酶样蛋白的保守策略，以纠正混杂查尔酮合酶的特异性。
陆地植物产生各种黄酮类化合物以促进生长，存活和繁殖。查尔酮合酶是类黄酮生物合成途径中第一个固定的酶，并催化2'，4,4'，6'-四羟基查尔酮（THC）的产生。但是，由于查尔酮生成途径的脱轨，它还会生成其他聚酮化合物，包括对香豆酰基三乙酸内酯（CTAL）。CHS催化的这种混杂性不利地影响了类黄酮生物合成的效率，尽管也认为它导致了二苯乙烯合酶和对香豆酰三乙酸合酶的进化。在这项研究中，我们建立了查尔酮异构酶样蛋白（CHIL），该蛋白由陆地植物基因组中普遍存在的基因编码，可与CHS结合以增强THC生成并减少CTAL形成，从而纠正了混杂的CHS催化。这种CHIL功能已在多种陆地植物物种中得到证实，并且代表了一种保守的策略，可促进底物从苯丙烷类途径向类黄酮途径的有效流入。
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