Monolignol acyltransferase for lignin p-hydroxybenzoylation in Populus
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 functionsmore »