Identification of chalcone isomerase in the basal land plants reveals an ancient evolution of enzymatic cyclization activity for synthesis of flavonoids

© 2017 Brookhaven National Laboratory and Shandong University. New Phytologist © 2017 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 217(2018), 2 vom: 08. Jan., Seite 909-924
1. Verfasser: Cheng, Ai-Xia (VerfasserIn)
Weitere Verfasser: Zhang, Xuebin, Han, Xiao-Juan, Zhang, Yu-Ying, Gao, Shuai, Liu, Chang-Jun, Lou, Hong-Xiang
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2018
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Selaginella moellendorffii (Spikemoss) chalcone isomerase evolution flavonoids liverwort Fatty Acids Flavonoids mehr... Plant Proteins Intramolecular Lyases EC 5.5.- EC 5.5.1.6
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245 1 0 |a Identification of chalcone isomerase in the basal land plants reveals an ancient evolution of enzymatic cyclization activity for synthesis of flavonoids 
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520 |a © 2017 Brookhaven National Laboratory and Shandong University. New Phytologist © 2017 New Phytologist Trust. 
520 |a Flavonoids ubiquitously distribute to the terrestrial plants and chalcone isomerase (CHI)-catalyzed intramolecular and stereospecific cyclization of chalcones is a committed step in the production of flavonoids. However, so far the bona fide CHIs are found only in vascular plants, and their origin and evolution remains elusive. We conducted transcriptomic and/or genomic sequence search, subsequent phylogenetic analysis, and detailed biochemical and genetic characterization to explore the potential existence of CHI proteins in the basal bryophyte liverwort species and the lycophyte Selaginella moellendorffii. We found that both liverwort and Selaginella species possess canonical CHI-fold proteins that cluster with their corresponding higher plant counterparts. Among them, some members exhibited bona fide CHI activity, which catalyze stereospecific cyclization of both 6'-hydroxychalcone and 6'-deoxychalcone, yielding corresponding 5-hydroxy and 5-deoxyflavanones, resembling the typical type II CHIs currently known to be 'specific' for legume plants. Expressing those primitive bona fide CHIs in the Arabidopsis chi mutant restores the seed coat transparent testa phenotype and the accumulation of flavonoids. These findings, in contrast to our current understanding of the evolution of enzymatic CHIs, suggest that emergence of the bona fide type II CHIs is an ancient evolution event that occurred before the divergence of liverwort lineages 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Research Support, U.S. Gov't, Non-P.H.S. 
650 4 |a Selaginella moellendorffii (Spikemoss) 
650 4 |a chalcone isomerase 
650 4 |a evolution 
650 4 |a flavonoids 
650 4 |a liverwort 
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650 7 |a Flavonoids  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Intramolecular Lyases  |2 NLM 
650 7 |a EC 5.5.-  |2 NLM 
650 7 |a chalcone isomerase  |2 NLM 
650 7 |a EC 5.5.1.6  |2 NLM 
700 1 |a Zhang, Xuebin  |e verfasserin  |4 aut 
700 1 |a Han, Xiao-Juan  |e verfasserin  |4 aut 
700 1 |a Zhang, Yu-Ying  |e verfasserin  |4 aut 
700 1 |a Gao, Shuai  |e verfasserin  |4 aut 
700 1 |a Liu, Chang-Jun  |e verfasserin  |4 aut 
700 1 |a Lou, Hong-Xiang  |e verfasserin  |4 aut 
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