ArticleNature plants2021
Monolignol acyltransferase for lignin p-hydroxybenzoylation in Populus.
Article in Nature plants, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 43 citations in OpenAlex.
- Simultaneous Overexpression of FERULOYL-CoA 6'-HYDROXYLASE 1 and COUMARIN SYNTHASE Leads to Coumarin-Enriched Lignin and Improved Saccharification in Greenhouse- and Field-Grown Poplar.Plant biotechnology journal · 2026Article
- A Dual-gRNA CRISPR/Cas9 System for Efficient Generation of Large Fragment Deletions in Poplar.Bio-protocol · 2026Article
- Engineering 2-Pyrone-4,6-Dicarboxylic Acid Production Reveals Metabolic Plasticity of Poplar.Plant biotechnology journal · 2026Article
- Engineered Accumulation of Protocatechuate in Corn Biomass to Enhance Biomanufacturing.ACS sustainable chemistry & engineering · 2025Article
- Pd/C promotes C-H bond activation and oxidation of p-hydroxybenzoate during hydrogenolysis of poplar.Nature communications · 2025Article
- Article
- Applications of CRISPR Technologies in Forestry and Molecular Wood Biotechnology.International journal of molecular sciences · 2024Review
- Synthetic-biology approach for plant lignocellulose engineering.Plant biotechnology (Tokyo, Japan) · 2024Article
- Expression of dehydroshikimate dehydratase in poplar induces transcriptional and metabolic changes in the phenylpropanoid pathway.Journal of experimental botany · 2024Article
- Simultaneous suppression of lignin, tricin and wall-bound phenolic biosynthesis via the expression of monolignol 4-O-methyltransferases in rice.Plant biotechnology journal · 2024Article
- Mutating alfalfaFrontiers in plant science · 2024Article
- Lignin Hydrogenolysis: Phenolic Monomers from Lignin and Associated Phenolates across Plant Clades.ACS sustainable chemistry & engineering · 2023Article
- Novel candidate genes for lignin structure identified through genome-wide association study of naturally varyingFrontiers in plant science · 2023Article
- Metabolic engineering of p-hydroxybenzoate in poplar lignin.Plant biotechnology journal · 2023Article
- Family characteristics, phylogenetic reconstruction, and potential applications of the plant BAHD acyltransferase family.Frontiers in plant science · 2023Review
- Engineering sorghum for higher 4-hydroxybenzoic acid content.Metabolic engineering communications · 2022Article
- Lignin engineering in forest trees: From gene discovery to field trials.Plant communications · 2022Review
- Genome assembly and chemogenomic profiling of National Flower of Singapore Papilionanthe Miss Joaquim 'Agnes' reveals metabolic pathways regulating floral traits.Communications biology · 2022Article
- A new approach to zip-lignin: 3,4-dihydroxybenzoate is compatible with lignification.The New phytologist · 2022Article
- pHBMT1, a BAHD-family monolignol acyltransferase, mediates lignin acylation in poplar.Plant physiology · 2022Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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