ArticlePlant cell reports2015
Functional characterization of a chalcone synthase from the liverwort Plagiochasma appendiculatum.
Article in Plant cell reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 50 citations in OpenAlex.
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- Characterization of the Key Bibenzyl Synthase inInternational journal of molecular sciences · 2022Article
- A Moss 2-Oxoglutarate/Fe(II)-Dependent Dioxygenases (2-ODD) Gene of Flavonoids Biosynthesis Positively Regulates Plants Abiotic Stress Tolerance.Frontiers in plant science · 2022Article
- Two putative parallel pathways for naringenin biosynthesis inRSC advances · 2021Article
- Functional and Structural Investigation of Chalcone Synthases Based on Integrated Metabolomics and Transcriptome Analysis on Flavonoids and Anthocyanins Biosynthesis of the FernFrontiers in plant science · 2021Article
- An Overview of the Medicinally Important Plant Type III PKS Derived Polyketides.Frontiers in plant science · 2021Review
- Identification of chalcone synthase genes and their expression patterns reveal pollen abortion in cotton.Saudi journal of biological sciences · 2020Article
- Manipulation of β-carotene levels in tomato fruits results in increased ABA content and extended shelf life.Plant biotechnology journal · 2020Article
- Functional characterization of a liverworts bHLH transcription factor involved in the regulation of bisbibenzyls and flavonoids biosynthesis.BMC plant biology · 2019Article
- Transcriptomic and functional analyses unveil the role of long non-coding RNAs in anthocyanin biosynthesis during sea buckthorn fruit ripening.DNA research : an international journal for rapid publication of reports on genes and genomes · 2018Article
- Molecular Diversity of Alkenal Double Bond Reductases in the LiverwortMolecules (Basel, Switzerland) · 2018Article
- Functional Promiscuity of Two Divergent Paralogs of Type III Plant Polyketide Synthases.Plant physiology · 2016Article
- Transcriptome-enabled discovery and functional characterization of enzymes related to (2S)-pinocembrin biosynthesis from Ornithogalum caudatum and their application for metabolic engineering.Microbial cell factories · 2016Article
- Genome-Wide Identification, Characterization and Expression Analysis of the Chalcone Synthase Family in Maize.International journal of molecular sciences · 2016Article
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6 authors at 1 institution in 1 country.
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Abstract
key messageA chalcone synthase gene ( PaCHS ) was isolated and functionally characterized from liverwort. The ectopic expression of PaCHS in Marchantia paleacea callus raised the flavonoids content. Chalcone synthase (CHS; EC 2.3.1.74) is pivotal for the biosynthesis of flavonoid and anthocyanin pigments in plants. It produces naringenin chalcone by condensing one p-coumaroyl- and three malonyl-coenzyme A thioesters through a polyketide intermediate that is cyclized by intramolecular Claisen condensation. Although CHSs of higher plants have been extensively studied, enzyme properties of the CHSs in liverworts have been scarcely characterized. In this study, we report the cloning and characterization of CHS (designated as PaCHS) from the liverwort Plagiochasma appendiculatum. The gene product was 60-70 % identical with chalcone synthases from other species, and contained the characteristic conserved Cys-His-Asn catalytic triad. The recombinant PaCHS was able to catalyze p-coumaroyl-CoA and malonyl-CoA to generate naringenin in vitro. Heterologously expressed PaCHS protein showed similar kinetic properties to those of higher plant CHS. The ectopic expression of PaCHS in Marchantia paleacea callus raised the content of the total flavonoids. These results suggested that PaCHS played a key role in the flavonoids biosynthesis in liverworts. Furthermore, when the thallus of P. appendiculatum was treated with abiotic stress inducers methyl jasmonate, salicylic acid and abscisic acid, PaCHS expression was enhanced. This is the first time that a CHS in liverworts has been functionally characterized.
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