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

Author

Listed:
  • Jaime Barros

    (University of North Texas
    University of North Texas
    Oak Ridge National Laboratory)

  • Luis Escamilla-Trevino

    (University of North Texas
    University of North Texas
    Oak Ridge National Laboratory)

  • Luhua Song

    (University of North Texas
    University of North Texas)

  • Xiaolan Rao

    (University of North Texas
    University of North Texas
    Oak Ridge National Laboratory)

  • Juan Carlos Serrani-Yarce

    (University of North Texas
    University of North Texas)

  • Maite Docampo Palacios

    (University of North Texas
    University of North Texas)

  • Nancy Engle

    (Oak Ridge National Laboratory
    Oak Ridge National Laboratory)

  • Feroza K. Choudhury

    (University of North Texas
    University of North Texas)

  • Timothy J. Tschaplinski

    (Oak Ridge National Laboratory
    Oak Ridge National Laboratory)

  • Barney J. Venables

    (University of North Texas)

  • Ron Mittler

    (University of North Texas
    University of North Texas)

  • Richard A. Dixon

    (University of North Texas
    University of North Texas
    Oak Ridge National Laboratory
    Oak Ridge National Laboratory)

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.

Suggested Citation

  • 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, 2019. "4-Coumarate 3-hydroxylase in the lignin biosynthesis pathway is a cytosolic ascorbate peroxidase," Nature Communications, Nature, vol. 10(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-10082-7
    DOI: 10.1038/s41467-019-10082-7
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    Cited by:

    1. Evgeny Chupakhin & Olga Babich & Stanislav Sukhikh & Svetlana Ivanova & Ekaterina Budenkova & Olga Kalashnikova & Alexander Prosekov & Olga Kriger & Vyacheslav Dolganyuk, 2022. "Bioengineering and Molecular Biology of Miscanthus," Energies, MDPI, vol. 15(14), pages 1-14, July.

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