4-Coumarate 3-hydroxylase in the lignin biosynthesis pathway is a cytosolic ascorbate peroxidase
| Autor: | Timothy J. Tschaplinski, Juan Carlos Serrani-Yarce, Feroza K. Choudhury, Luis Escamilla-Trevino, Barney J. Venables, Xiaolan Rao, Jaime Barros, Richard A. Dixon, Maite Docampo Palacios, Nancy L. Engle, Luhua Song, Ron Mittler |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Coumaric Acids Science Arabidopsis General Physics and Astronomy macromolecular substances 02 engineering and technology Lignin complex mixtures Article General Biochemistry Genetics and Molecular Biology Mixed Function Oxygenases 03 medical and health sciences chemistry.chemical_compound Ascorbate Peroxidases Caffeic Acids Cytosol Arabidopsis thaliana lcsh:Science Plant Proteins chemistry.chemical_classification Multidisciplinary biology Cell wall fungi technology industry and agriculture food and beverages General Chemistry 021001 nanoscience & nanotechnology biology.organism_classification Enzymes 030104 developmental biology Enzyme Biochemistry chemistry biology.protein lcsh:Q Lignin biosynthesis Brachypodium distachyon Secondary metabolism 0210 nano-technology Brachypodium Peroxidase |
| Zdroj: | Nature Communications, Vol 10, Iss 1, Pp 1-11 (2019) Nature Communications |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-019-10082-7 |
| Popis: | Lignin biosynthesis is evolutionarily conserved among higher plants and features a critical 3-hydroxylation reaction involving phenolic esters. However, increasing evidence questions the involvement of a single pathway to lignin formation in vascular plants. Here we describe an enzyme catalyzing the direct 3-hydroxylation of 4-coumarate to caffeate in lignin biosynthesis as a bifunctional peroxidase that oxidizes both ascorbate and 4-coumarate at comparable rates. A combination of biochemical and genetic evidence in the model plants Brachypodium distachyon and Arabidopsis thaliana supports a role for this coumarate 3-hydroxylase (C3H) in the early steps of lignin biosynthesis. The subsequent efficient O-methylation of caffeate to ferulate in grasses is substantiated by in vivo biochemical assays. Our results identify C3H as the only non-membrane bound hydroxylase in the lignin pathway and revise the currently accepted models of lignin biosynthesis, suggesting new gene targets to improve forage and bioenergy crops. Lignin biosynthesis in higher plants relies upon a 3-hydroxylation reaction that can occur via shikimate esters of 4-coumarate. Here, Barros et al. define an alternative biosynthetic pathway via cytosolic ascorbate peroxidase that can catalyze direct 3-hydroxylation of 4-coumarate. |
| Databáze: | OpenAIRE |
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