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

Abstract

Lignin biosynthesis is evolutionarily conserved among higher plants and features a critical 3-hydroxylation reaction involving phenolic esters. Yet, increasing evidence questions the involvement of a single pathway to lignin formation in vascular plants. In this work 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.

Authors:
ORCiD logo [1];  [1];  [2];  [1];  [2]; ORCiD logo [2]; ORCiD logo [3];  [2]; ORCiD logo [3];  [2];  [2]; ORCiD logo [1]
  1. Univ. of North Texas, Denton, TX (United States); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
  2. Univ. of North Texas, Denton, TX (United States)
  3. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Publication Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
OSTI Identifier:
1545188
Grant/Contract Number:  
AC05-00OR22725
Resource Type:
Accepted Manuscript
Journal Name:
Nature Communications
Additional Journal Information:
Journal Volume: 10; Journal Issue: 1; Journal ID: ISSN 2041-1723
Publisher:
Nature Publishing Group
Country of Publication:
United States
Language:
English

Citation Formats

Barros, Jaime, Escamilla-Trevino, Luis, Song, Luhua, Rao, Xiaolan, Serrani-Yarce, Juan Carlos, Palacios, Maite Docampo, Engle, Nancy, Choudhury, Feroza K., Tschaplinski, Timothy J., Venables, Barney J., Mittler, Ron, and Dixon, Richard A. 4-Coumarate 3-hydroxylase in the lignin biosynthesis pathway is a cytosolic ascorbate peroxidase. United States: N. p., 2019. Web. doi:10.1038/s41467-019-10082-7.
Barros, Jaime, Escamilla-Trevino, Luis, Song, Luhua, Rao, Xiaolan, Serrani-Yarce, Juan Carlos, Palacios, Maite Docampo, Engle, Nancy, Choudhury, Feroza K., Tschaplinski, Timothy J., Venables, Barney J., Mittler, Ron, & Dixon, Richard A. 4-Coumarate 3-hydroxylase in the lignin biosynthesis pathway is a cytosolic ascorbate peroxidase. United States. doi:10.1038/s41467-019-10082-7.
Barros, Jaime, Escamilla-Trevino, Luis, Song, Luhua, Rao, Xiaolan, Serrani-Yarce, Juan Carlos, Palacios, Maite Docampo, Engle, Nancy, Choudhury, Feroza K., Tschaplinski, Timothy J., Venables, Barney J., Mittler, Ron, and Dixon, Richard A. Tue . "4-Coumarate 3-hydroxylase in the lignin biosynthesis pathway is a cytosolic ascorbate peroxidase". United States. doi:10.1038/s41467-019-10082-7. https://www.osti.gov/servlets/purl/1545188.
@article{osti_1545188,
title = {4-Coumarate 3-hydroxylase in the lignin biosynthesis pathway is a cytosolic ascorbate peroxidase},
author = {Barros, Jaime and Escamilla-Trevino, Luis and Song, Luhua and Rao, Xiaolan and Serrani-Yarce, Juan Carlos and Palacios, Maite Docampo and Engle, Nancy and Choudhury, Feroza K. and Tschaplinski, Timothy J. and Venables, Barney J. and Mittler, Ron and Dixon, Richard A.},
abstractNote = {Lignin biosynthesis is evolutionarily conserved among higher plants and features a critical 3-hydroxylation reaction involving phenolic esters. Yet, increasing evidence questions the involvement of a single pathway to lignin formation in vascular plants. In this work 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.},
doi = {10.1038/s41467-019-10082-7},
journal = {Nature Communications},
number = 1,
volume = 10,
place = {United States},
year = {2019},
month = {4}
}

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Works referenced in this record:

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