A conserved strategy of chalcone isomerase-like protein to rectify promiscuous chalcone synthase specificity
A conserved strategy of chalcone isomerase-like protein to rectify promiscuous chalcone synthase specificity
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DOI：
10.1038/s41467-020-14558-9
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发表时间：
2020-02-13
影响因子：
16.6
通讯作者：
Nakayama, Toru
中科院分区：
文献类型：
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作者：
Waki, Toshiyuki;Mameda, Ryo;Nakayama, Toru
陆地植物为生长、生存和繁殖产生各种各样的黄酮类物质。查尔酮合酶是类黄酮生物合成途径中的第一个关键酶，催化合成2，4，4‘，6’-四羟基查尔酮(THC)。然而，由于查尔酮产生途径的脱轨，它也产生其他聚酮，包括p-香豆酰三乙酸内酯(CTAL)。这种杂乱的CHS催化对类黄酮生物合成的效率产生了不利的影响，尽管它也被认为导致了二苯乙烯合成酶和p-香豆酰三乙酸合成酶的进化。在这项研究中，我们建立了查尔酮异构酶样蛋白(CHILs)，它是由陆地植物基因组中普遍存在的基因编码的，它与CHS结合，以增加THC的产生，减少CTAL的形成，从而纠正CHS的混杂催化。这种CHIL功能已经在不同的陆地植物物种中得到证实，并代表了一种保守的策略，促进了底物从苯丙烷途径到类黄酮途径的有效流入。
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.