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DOE OSTI · 1817193

Monolignol acyltransferase for lignin p-hydroxybenzoylation in Populus

Zhao, Yunjun·Yu, Xiaohong·Lam, Pui-Ying·Zhang, Kewei·Tobimatsu, Yuki·Liu, Chang-Jun
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Abstract

Plant lignification exhibits significant plasticity. Lignin in many species including Populus spp. has long been known decorated with p-hydroxybenzoates. However, the molecular basis for such structural modification remains undetermined. Here we report the identification and characterization of a Populus BAHD family acyltransferase that catalyzes monolignol p-hydroxybenzoylation, thus controlling the formation of p-hydroxybenzoylated lignin structures. We reveal that Populus acyltransferase PHBMT1 kinetically preferentially utilizes p-hydroxybenzoyl-CoA to acylate syringyl lignin monomer sinapyl alcohol in vitro. Consistently, disrupting PHBMT1 in Populus via CRISPR/Cas9 gene editing nearly completely depletes p-hydroxybenzoates of stem lignin; conversely, overexpression of PHBMT1 enhances stem lignin p-hydroxybenzoylation, suggesting PHBMT1 functions as a prime monolignol p-hydroxybenzoyltransferase in planta. Altering lignin p-hydroxybenzoylation significantly changes lignin solvent dissolution rate, indictive of its structural significance on lignin physiochemical properties. Identification of monolignol p-hydroxybenzoyltransferase offers a valuable tool for tailoring lignin structure and physiochemical properties and for engineering the industrially important platform chemical in woody biomass.

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Zhao, Yunjun, Yu, Xiaohong, Lam, Pui-Ying, Zhang, Kewei, Tobimatsu, Yuki, Liu, Chang-Jun. 2021-08-05. Monolignol acyltransferase for lignin p-hydroxybenzoylation in Populus. https://doi.org/10.1038/s41477-021-00975-1

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