Identification and evolutionary analysis of chalcone isomerase-fold proteins in ferns

Ni, Rong; Zhu, Tingting; Zhang, Xiaoshuang; Wang, Piao-Yi; Sun, Chun‐Jing; Qiao, Ya-Nan; Lou, Hongxiang; Cheng, Ai‐Xia

doi:10.1093/jxb/erz425

Cited by 42 publications

(52 citation statements)

References 44 publications

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“…Thus, in essence, CHIL is considered to be a rectifier-rather than an activator-of promiscuous CHS catalysis. Of note, during the review of this paper, a research group independently reported the ability of a fern CHIL to alter product specificity of CHS 23 , consistent with our results. The CHIL genes are ubiquitous in the genomes of land plants 17 and expressed along with CHS genes in diverse plant species 16,24 , and the physical interactions between CHIL and CHS are strictly conserved among the examined land plants (Figs.…”

Section: Discussionsupporting

confidence: 88%

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

et al. 2020

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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.

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Section: Discussionsupporting

confidence: 88%

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

et al. 2020

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“…Studies have found that type I CHIs are the bona fide CHIs with enzymatic activity converting naringenin chalcone to naringenin (Ni et al, 2020); overexpression of type I CHI genes increases the content of total flavonoid in various plants (Muir et al, 2001;Li et al, 2006;Park et al, 2011;Chung et al, 2019;Liu et al, 2019;Sun W. et al, 2019;Dare et al, 2020;Ni et al, 2020). In this study, three CHI Type I members were found in D. cambodiana; DcCHI1 may be the key isoform involved in flavonoid biosynthesis.…”

Section: Discussionmentioning

confidence: 48%

Identification and Characterization of Chalcone Isomerase Genes Involved in Flavonoid Production in Dracaena cambodiana

Zhu

Zhao

et al. 2021

Front. Plant Sci.

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Dragon’s blood is a traditional medicine in which flavonoids are the main bioactive compounds; however, the underlying formation mechanism of dragon’s blood remains largely poorly understood. Chalcone isomerase (CHI) is the key enzyme in the flavonoid biosynthesis pathway. However, CHI family genes are not well understood in Dracaena cambodiana Pierre ex Gagnep, an important source plant of dragon’s blood. In this study, 11 CHI family genes were identified from D. cambodiana, and they were classified into three types. Evolutionary and transcriptional profiling analysis revealed that DcCHI1 and DcCHI4 might be involved in flavonoid production. Both DcCHI1 and DcCHI4 displayed low expression levels in stem under normal growth conditions and were induced by methyl jasmonate (MeJA), 6-benzyl aminopurine (6-BA, synthetic cytokinin), ultraviolet-B (UV-B), and wounding. The recombinant proteins DcCHI1 and DcCHI4 were expressed in Escherichia coli and purified by His-Bind resin chromatography. Enzyme activity assay indicated that DcCHI1 catalyzed the formation of naringenin from naringenin chalcone, while DcCHI4 lacked this catalytic activity. Overexpression of DcCHI1 or DcCHI4 enhanced the flavonoid production in D. cambodiana and tobacco. These findings implied that DcCHI1 and DcCHI4 play important roles in flavonoid production. Thus, our study will not only contribute to better understand the function and expression regulation of CHI family genes involved in flavonoid production in D. cambodiana but also lay the foundation for developing the effective inducer of dragon’s blood.

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“…Since the flavonoid biosynthesis is mainly regulated at the transcriptional level [ 63 ] and previously reported blocks in the pathway are expected to be due to transcriptional down-regulation [ 93 , 94 ], we expect most branches of the flavonoid biosynthesis in C. tiglium to be functional. No CHI II candidate was detected, and thus C. tiglium probably lacks a 6′-deoxychalcone to 5-deoxyflavanone catalytic activity like most non-leguminous plants [ 30 , 95 ].…”

Section: Discussionmentioning

confidence: 99%

Automatic Identification of Players in the Flavonoid Biosynthesis with Application on the Biomedicinal Plant Croton tiglium

Pucker

Reiher

Schilbert

2020

Plants

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The flavonoid biosynthesis is a well-characterised model system for specialised metabolism and transcriptional regulation in plants. Flavonoids have numerous biological functions such as UV protection and pollinator attraction, but also biotechnological potential. Here, we present Knowledge-based Identification of Pathway Enzymes (KIPEs) as an automatic approach for the identification of players in the flavonoid biosynthesis. KIPEs combines comprehensive sequence similarity analyses with the inspection of functionally relevant amino acid residues and domains in subjected peptide sequences. Comprehensive sequence sets of flavonoid biosynthesis enzymes and knowledge about functionally relevant amino acids were collected. As a proof of concept, KIPEs was applied to investigate the flavonoid biosynthesis of the medicinal plant Croton tiglium on the basis of a transcriptome assembly. Enzyme candidates for all steps in the biosynthesis network were identified and matched to previous reports of corresponding metabolites in Croton species.

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Identification and evolutionary analysis of chalcone isomerase-fold proteins in ferns

Abstract: The emergence of type I CHIs may have occurred at the time of the divergence of the pteridophytes, with CHIL interacting with both CHS and CHI to promote flavonoid synthesis.

Cited by 42 publications

References 44 publications

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

Identification and Characterization of Chalcone Isomerase Genes Involved in Flavonoid Production in Dracaena cambodiana

Automatic Identification of Players in the Flavonoid Biosynthesis with Application on the Biomedicinal Plant Croton tiglium

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