ArticleProceedings of the National Academy of Sciences of the United States of America2015
Phosphorylation is an on/off switch for 5-hydroxyconiferaldehyde O-methyltransferase activity in poplar monolignol biosynthesis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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37 citing papers in PubMed.
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- Phenylpropanoids metabolism: recent insight into stress tolerance and plant development cues.Frontiers in plant science · 2025Review
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- Deciphering the intricate hierarchical gene regulatory network: unraveling multi-level regulation and modifications driving secondary cell wall formation.Horticulture research · 2024Article
- Prediction of Protein Ion-Ligand Binding Sites with ELECTRA.Molecules (Basel, Switzerland) · 2023Article
- Multiplex CRISPR editing of wood for sustainable fiber production.Science (New York, N.Y.) · 2023Article
- Lignin engineering in forest trees: From gene discovery to field trials.Plant communications · 2022Review
- Proteomic and metabolic disturbances in lignin-modified Brachypodium distachyon.The Plant cell · 2022Article
- Insights into the Molecular Regulation of Lignin Content in Triploid Poplar Leaves.International journal of molecular sciences · 2022Article
- Ubiquitylome analysis reveals the involvement of ubiquitination in the bast fiber growth of ramie.Planta · 2021Article
- Association of gene expression with syringyl to guaiacyl ratio in sugarcane lignin.Plant molecular biology · 2021Article
- Abscisic acid regulates secondary cell-wall formation and lignin deposition inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Sweet Basil Has Distinct Synthases for Eugenol Biosynthesis in Glandular Trichomes and Roots with Different Regulatory Mechanisms.International journal of molecular sciences · 2021Article
- Integrated Transcriptomic and Proteomic Analysis in the Roadmap of the Xylem Development Stage inFrontiers in plant science · 2021Article
- Phenylpropanoid Biosynthesis Gene Expression Precedes Lignin Accumulation During Shoot Development in Lowland and Upland Switchgrass Genotypes.Frontiers in plant science · 2021Article
- Modeling cross-regulatory influences on monolignol transcripts and proteins under single and combinatorial gene knockdowns in Populus trichocarpa.PLoS computational biology · 2020Article
- Multifeature analyses of vascular cambial cells reveal longevity mechanisms in oldProceedings of the National Academy of Sciences of the United States of America · 2020Article
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10 authors.
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Abstract
Although phosphorylation has long been known to be an important regulatory modification of proteins, no unequivocal evidence has been presented to show functional control by phosphorylation for the plant monolignol biosynthetic pathway. Here, we present the discovery of phosphorylation-mediated on/off regulation of enzyme activity for 5-hydroxyconiferaldehyde O-methyltransferase 2 (PtrAldOMT2), an enzyme central to monolignol biosynthesis for lignification in stem-differentiating xylem (SDX) of Populus trichocarpa. Phosphorylation turned off the PtrAldOMT2 activity, as demonstrated in vitro by using purified phosphorylated and unphosphorylated recombinant PtrAldOMT2. Protein extracts of P. trichocarpa SDX, which contains endogenous kinases, also phosphorylated recombinant PtrAldOMT2 and turned off the recombinant protein activity. Similarly, ATP/Mn(2+)-activated phosphorylation of SDX protein extracts reduced the endogenous SDX PtrAldOMT2 activity by ∼ 60%, and dephosphorylation fully restored the activity. Global shotgun proteomic analysis of phosphopeptide-enriched P. trichocarpa SDX protein fractions identified PtrAldOMT2 monophosphorylation at Ser(123) or Ser(125) in vivo. Phosphorylation-site mutagenesis verified the PtrAldOMT2 phosphorylation at Ser(123) or Ser(125) and confirmed the functional importance of these phosphorylation sites for O-methyltransferase activity. The PtrAldOMT2 Ser(123) phosphorylation site is conserved across 93% of AldOMTs from 46 diverse plant species, and 98% of the AldOMTs have either Ser(123) or Ser(125). PtrAldOMT2 is a homodimeric cytosolic enzyme expressed more abundantly in syringyl lignin-rich fiber cells than in guaiacyl lignin-rich vessel cells. The reversible phosphorylation of PtrAldOMT2 is likely to have an important role in regulating syringyl monolignol biosynthesis of P. trichocarpa.
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