单甘醇
木质素
肉桂醇脱氢酶
化学
细胞壁
植物
生物化学
生物
基因
生物合成
作者
Yunjun Zhao,Xiaohong Yu,Pui Ying Lam,Kewei Zhang,Yuki Tobimatsu,Chang‐Jun Liu
出处
期刊:Nature plants
[Springer Nature]
日期:2021-08-05
卷期号:7 (9): 1288-1300
被引量:27
标识
DOI:10.1038/s41477-021-00975-1
摘要
Plant lignification exhibits notable plasticity. Lignin in many species, including Populus spp., has long been known to be 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 catalyses monolignol p-hydroxybenzoylation, thus controlling the formation of p-hydroxybenzoylated lignin structures. We reveal that Populus acyltransferase PHBMT1 kinetically preferentially uses 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 substantially changes the lignin solvent dissolution rate, indicative 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.
科研通智能强力驱动
Strongly Powered by AbleSci AI