Disruption of p-coumaroyl-CoA:monolignol transferases in rice drastically alters lignin composition

Lam, Lydia Pui Ying; Tobimatsu, Yuki; Suzuki, Shiro; Tanaka, Takuto; Yamamoto, Senri; Takeda-Kimura, Yuri; Osakabe, Yuriko; Osakabe, Keishi; Ralph, John; Bartley, Laura E.; Umezawa, Toshiaki

doi:10.1093/plphys/kiad549

Title: Disruption of p-coumaroyl-CoA:monolignol transferases in rice drastically alters lignin composition

Journal Article · 12 October 2023 · Plant Physiology (Bethesda)

DOI: https://doi.org/10.1093/plphys/kiad549 · OSTI ID:2294081

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Kyoto University (Japan); Akita University (Japan); Kyoto University Research Institute for Sustainable Humanosphere
Kyoto University (Japan)
Kyoto University (Japan); Gifu University (Japan)
Kyoto University (Japan); Yamagata University (Japan)
Tokyo Institute of Technology, Kanagawa (Japan)
Tokushima University (Japan)
University of Wisconsin, Madison, WI (United States)
Kyoto University (Japan); Washington State University, Pullman, WA (United States)

Grasses are abundant feedstocks that can supply lignocellulosic biomass for production of cell-wall-derived chemicals. In grass cell walls, lignin is acylated with p-coumarate. These p-coumarate decorations arise from the incorporation of monolignol p-coumarate conjugates during lignification. A previous biochemical study identified a rice (Oryza sativa) BAHD acyltransferase (AT) with p-coumaroyl-CoA:monolignol transferase (PMT) activity in vitro. In this study, we determined that that enzyme, which we name OsPMT1 (also known as OsAT4), and the closely related OsPMT2 (OsAT3) harbor similar catalytic activity toward monolignols. We generated rice mutants deficient in either or both OsPMT1 and OsPMT2 by CRISPR/Cas9-mediated mutagenesis and subjected the mutants’ cell walls to analysis using chemical and nuclear magnetic resonance methods. Our results demonstrated that OsPMT1 and OsPMT2 both function in lignin p-coumaroylation in the major vegetative tissues of rice. Notably, lignin-bound p-coumarate units were undetectable in the ospmt1 ospmt2-2 double-knockout mutant. Further, in-depth structural analysis of purified lignins from the ospmt1 ospmt2-2 mutant compared with control lignins from wild-type rice revealed stark changes in polymer structures, including alterations in syringyl/guaiacyl aromatic unit ratios and inter-monomeric linkage patterns, and increased molecular weights. Furthermore, our results provide insights into lignin polymerization in grasses that will be useful for the optimization of bioengineering approaches for the effective use of biomass in biorefineries.

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Research Organization:: Great Lakes Bioenergy Research Center (GLBRC), Madison, WI (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: SC0018409

OSTI ID:: 2294081

Journal Information:: Plant Physiology (Bethesda), Journal Name: Plant Physiology (Bethesda) Journal Issue: 2 Vol. 194; ISSN 0032-0889

Publisher:: American Society of Plant BiologistsCopyright Statement

Country of Publication:: United States

Language:: English

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