4-Coumarate 3-hydroxylase in the lignin biosynthesis pathway is a cytosolic ascorbate peroxidase

Jaime Barros, Luis Escamilla-Trevino, Luhua Song, Xiaolan Rao, Juan Carlos Serrani-Yarce, Maite Docampo Palacios, Nancy Engle, Feroza K. Choudhury, Timothy J. Tschaplinski, Barney J. Venables, Ron Mittler and Richard A. Dixon ()
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Jaime Barros: University of North Texas
Luis Escamilla-Trevino: University of North Texas
Luhua Song: University of North Texas
Xiaolan Rao: University of North Texas
Juan Carlos Serrani-Yarce: University of North Texas
Maite Docampo Palacios: University of North Texas
Nancy Engle: Oak Ridge National Laboratory
Feroza K. Choudhury: University of North Texas
Timothy J. Tschaplinski: Oak Ridge National Laboratory
Barney J. Venables: University of North Texas
Ron Mittler: University of North Texas
Richard A. Dixon: University of North Texas

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: Abstract 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.

Date: 2019
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DOI: 10.1038/s41467-019-10082-7

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