ArticleThe Plant cell2011
Independent recruitment of an O-methyltransferase for syringyl lignin biosynthesis in Selaginella moellendorffii.
Article in The Plant cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Conservation of IAMT Preference for Indole Acetic Acid Methylation Across 250 Million Years of Seed Plant Divergence, With Only One Recent Evolutionary Switch in Ocimum.Genome biology and evolution · 2026Article
- Computational model of flower pattern evolution predicts spontaneous emergence of boundary cell types across the petal epidermis.Development (Cambridge, England) · 2026Article
- Convergence and parallelism in the evolution of plant metabolism.Journal of integrative plant biology · 2026Review
- Melatonin promotes stomatal immunity by mediating phytohormone crosstalk inFrontiers in plant science · 2026Article
- An ancient role for CYP73 monooxygenases in phenylpropanoid biosynthesis and embryophyte development.The EMBO journal · 2024Article
- Review
- DiverseHorticulture research · 2023Article
- Regioselective stilbene O-methylations in Saccharinae grasses.Nature communications · 2023Article
- Creation of a Plant Metabolite Spectral Library for Untargeted and Targeted Metabolomics.International journal of molecular sciences · 2023Article
- H-lignin can be deposited independently of CINNAMYL ALCOHOL DEHYDROGENASE C and D in Arabidopsis.Plant physiology · 2022Article
- The flying spider-monkey tree fern genome provides insights into fern evolution and arborescence.Nature plants · 2022Article
- Function of the HYDROXYCINNAMOYL-CoA:SHIKIMATE HYDROXYCINNAMOYL TRANSFERASE is evolutionarily conserved in embryophytes.The Plant cell · 2021Article
- Kingdom-wide analysis of the evolution of the plant type III polyketide synthase superfamily.Plant physiology · 2021Article
- Genome-wide identification and characterization of COMT gene family during the development of blueberry fruit.BMC plant biology · 2021Article
- Phylogenetic Occurrence of the Phenylpropanoid Pathway and Lignin Biosynthesis in Plants.Frontiers in plant science · 2021Review
- New Insights on Structures Forming the Lignin-Like Fractions of Ancestral Plants.Frontiers in plant science · 2021Article
- Expression Atlas ofThe Plant cell · 2020Article
- Peroxidase evolution in white-rot fungi follows wood lignin evolution in plants.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Cloning and Functional Characterization of Two 4-Coumarate: CoA Ligase Genes from Selaginella moellendorffii.Molecules (Basel, Switzerland) · 2018Article
- Identification of critical genes associated with lignin biosynthesis in radish (Raphanus sativus L.) by de novo transcriptome sequencing.Molecular genetics and genomics : MGG · 2017Article
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4 authors.
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Abstract
Syringyl lignin, an important component of the secondary cell wall, has traditionally been considered to be a hallmark of angiosperms because ferns and gymnosperms in general lack lignin of this type. Interestingly, syringyl lignin was also detected in Selaginella, a genus that represents an extant lineage of the most basal of the vascular plants, the lycophytes. In angiosperms, syringyl lignin biosynthesis requires the activity of ferulate 5-hydroxylase (F5H), a cytochrome P450-dependent monooxygenase, and caffeic acid/5-hydroxyferulic acid O-methyltransferase (COMT). Together, these two enzymes divert metabolic flux from the biosynthesis of guaiacyl lignin, a lignin type common to all vascular plants, toward syringyl lignin. Selaginella has independently evolved an alternative lignin biosynthetic pathway in which syringyl subunits are directly derived from the precursors of p-hydroxyphenyl lignin, through the action of a dual specificity phenylpropanoid meta-hydroxylase, Sm F5H. Here, we report the characterization of an O-methyltransferase from Selaginella moellendorffii, COMT, the coding sequence of which is clustered together with F5H at the adjacent genomic locus. COMT is a bifunctional phenylpropanoid O-methyltransferase that can methylate phenylpropanoid meta-hydroxyls at both the 3- and 5-position and function in concert with F5H in syringyl lignin biosynthesis in S. moellendorffii. Phylogenetic analysis reveals that Sm COMT, like F5H, evolved independently from its angiosperm counterparts.
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