ArticlePlant molecular biology2011
Functional characterization of two new members of the caffeoyl CoA O-methyltransferase-like gene family from Vanilla planifolia reveals a new class of plastid-localized O-methyltransferases.
Article in Plant molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 78 citations in OpenAlex.
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- Genome-Wide Characterization ofGenes · 2024Article
- Genetic Engineering Approaches for the Microbial Production of Vanillin.Biomolecules · 2024Review
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- Genome-Wide Identification and Expression Analysis ofInternational journal of molecular sciences · 2023Article
- Evolution and expression analysis of the caffeoyl-CoA 3-O-methyltransferase (CCoAOMT) gene family in jute (Corchorus L.).BMC genomics · 2023Article
- Functional Diversification and Structural Origins of Plant Natural Product Methyltransferases.Molecules (Basel, Switzerland) · 2022Review
- RNA-Seq and Iso-Seq Reveal the Important Role ofGenes · 2022Article
- Two types of O-methyltransferase are involved in biosynthesis of anticancer methoxylated 4'-deoxyflavones in Scutellaria baicalensis Georgi.Plant biotechnology journal · 2022Article
- Gene-Metabolite Network Analysis Revealed Tissue-Specific Accumulation of Therapeutic Metabolites inInternational journal of molecular sciences · 2021Article
- Integrated Metabolome and Transcriptome Analysis Unveils Novel Pathway Involved in the Formation of Yellow Peel in Cucumber.International journal of molecular sciences · 2021Article
- Identification and expression analysis of caffeoyl-coenzyme A O-methyltransferase family genes related to lignin biosynthesis in tea plant (Camellia sinensis).Protoplasma · 2021Article
- A phased Vanilla planifolia genome enables genetic improvement of flavour and production.Nature food · 2020Article
- Characterization of a caffeoyl-CoA O-methyltransferase-like enzyme involved in biosynthesis of polymethoxylated flavones in Citrus reticulata.Journal of experimental botany · 2020Article
- Identification of genes from the general phenylpropanoid and monolignol-specific metabolism in two sugarcane lignin-contrasting genotypes.Molecular genetics and genomics : MGG · 2020Article
- Sorghum CCoAOMT and CCoAOMT-like gene evolution, structure, expression and the role of conserved amino acids in protein activity.Molecular genetics and genomics : MGG · 2018Article
- Molecular Cloning and Characterization of aInternational journal of molecular sciences · 2018Article
- Article
- A deep transcriptomic analysis of pod development in the vanilla orchid (Vanilla planifolia).BMC genomics · 2014Article
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7 authors at 2 institutions in 2 countries.
Funding
Abstract
Caffeoyl CoA O-methyltransferases (OMTs) have been characterized from numerous plant species and have been demonstrated to be involved in lignin biosynthesis. Higher plant species are known to have additional caffeoyl CoA OMT-like genes, which have not been well characterized. Here, we identified two new caffeoyl CoA OMT-like genes by screening a cDNA library from specialized hair cells of pods of the orchid Vanilla planifolia. Characterization of the corresponding two enzymes, designated Vp-OMT4 and Vp-OMT5, revealed that in vitro both enzymes preferred as a substrate the flavone tricetin, yet their sequences and phylogenetic relationships to other enzymes are distinct from each other. Quantitative analysis of gene expression indicated a dramatic tissue-specific expression pattern for Vp-OMT4, which was highly expressed in the hair cells of the developing pod, the likely location of vanillin biosynthesis. Although Vp-OMT4 had a lower activity with the proposed vanillin precursor, 3,4-dihydroxybenzaldehyde, than with tricetin, the tissue specificity of expression suggests it may be a candidate for an enzyme involved in vanillin biosynthesis. In contrast, the Vp-OMT5 gene was mainly expressed in leaf tissue and only marginally expressed in pod hair cells. Phylogenetic analysis suggests Vp-OMT5 evolved from a cyanobacterial enzyme and it clustered within a clade in which the sequences from eukaryotic species had predicted chloroplast transit peptides. Transient expression of a GFP-fusion in tobacco demonstrated that Vp-OMT5 was localized in the plastids. This is the first flavonoid OMT demonstrated to be targeted to the plastids.
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