ArticleThe Plant cell2014
Systems biology of lignin biosynthesis in Populus trichocarpa: heteromeric 4-coumaric acid:coenzyme A ligase protein complex formation, regulation, and numerical modeling.
Article in The Plant cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 83 citations in OpenAlex.
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- Epigenetic regulation of lignin biosynthesis in wood formation.The New phytologist · 2025Article
- Integrated Multi-Omics Analysis to Reveal the Molecular Mechanisms of Inflorescence Elongation inInternational journal of molecular sciences · 2024Article
- The metabolic fingerprint of Scots pine-root and needle metabolites show different patterns in dying trees.Tree physiology · 2024Article
- Multiplex CRISPR editing of wood for sustainable fiber production.Science (New York, N.Y.) · 2023Article
- Article
- A tracking work on how Sm4CL2 re-directed the biosynthesis of salvianolic acids and tanshinones in Salvia miltiorrhiza hairy roots.Plant cell reports · 2023Article
- Genome-edited rice deficient in two 4-COUMARATE:COENZYME A LIGASE genes displays diverse lignin alterations.Plant physiology · 2022Article
- Transcriptomic and Epigenomic Assessment Reveals Epigenetic Regulation of WRKY Genes in Response toCurrent genomics · 2022Article
- A PtrLBD39-mediated transcriptional network regulates tension wood formation inPlant communications · 2022Article
- Homo- and Hetero-Dimers of CAD Enzymes Regulate Lignification and Abiotic Stress Response in Moso Bamboo.International journal of molecular sciences · 2021Article
- Transcriptional landscape of highly lignified poplar stems at single-cell resolution.Genome biology · 2021Article
- The entry reaction of the plant shikimate pathway is subjected to highly complex metabolite-mediated regulation.The Plant cell · 2021Article
- Enzyme Complexes of Ptr4CL and PtrHCT Modulate Co-enzyme A Ligation of Hydroxycinnamic Acids for Monolignol Biosynthesis inFrontiers in plant science · 2021Article
- Hunting monolignol transporters: membrane proteomics and biochemical transport assays with membrane vesicles of Norway spruce.Journal of experimental botany · 2020Article
- Compensatory Guaiacyl Lignin Biosynthesis at the Expense of Syringyl Lignin inPlant physiology · 2020Article
- Regulation of Lignin Biosynthesis by Post-translational Protein Modifications.Frontiers in plant science · 2020Review
- Hierarchical Transcription Factor and Chromatin Binding Network for Wood Formation in Black Cottonwood (The Plant cell · 2019Article
- Xylan in the Middle: Understanding Xylan Biosynthesis and Its Metabolic Dependencies Toward Improving Wood Fiber for Industrial Processing.Frontiers in plant science · 2019Review
Corrections and comments
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Authors and funding
15 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
As a step toward predictive modeling of flux through the pathway of monolignol biosynthesis in stem differentiating xylem of Populus trichocarpa, we discovered that the two 4-coumaric acid:CoA ligase (4CL) isoforms, 4CL3 and 4CL5, interact in vivo and in vitro to form a heterotetrameric protein complex. This conclusion is based on laser microdissection, coimmunoprecipitation, chemical cross-linking, bimolecular fluorescence complementation, and mass spectrometry. The tetramer is composed of three subunits of 4CL3 and one of 4CL5. 4CL5 appears to have a regulatory role. This protein-protein interaction affects the direction and rate of metabolic flux for monolignol biosynthesis in P. trichocarpa. A mathematical model was developed for the behavior of 4CL3 and 4CL5 individually and in mixtures that form the enzyme complex. The model incorporates effects of mixtures of multiple hydroxycinnamic acid substrates, competitive inhibition, uncompetitive inhibition, and self-inhibition, along with characteristic of the substrates, the enzyme isoforms, and the tetrameric complex. Kinetic analysis of different ratios of the enzyme isoforms shows both inhibition and activation components, which are explained by the mathematical model and provide insight into the regulation of metabolic flux for monolignol biosynthesis by protein complex formation.
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