ArticleProceedings of the National Academy of Sciences of the United States of America2012
Cellulose microfibril crystallinity is reduced by mutating C-terminal transmembrane region residues CESA1A903V and CESA3T942I of cellulose synthase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.
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85 citing papers in PubMed, 171 citations in OpenAlex.
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- Plasma Membrane and Endomembrane Lipids Are Involved in a Complex Adaptation ofInternational journal of molecular sciences · 2026Article
- A fungal natural product that inhibits plant cellulose biosynthesis by disrupting cellulose synthase complexes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Native Architecture of Wheat Straw Cell Walls: A Unified Model from X-ray Scattering and Solid-State NMR.Journal of the American Chemical Society · 2026Article
- Exploiting evolutionary diversity of cellulose synthase catalytic subunits to generate novel cellulose microfibril structure in Arabidopsis.Journal of experimental botany · 2026Article
- Cell wall-derived mechanical signals control cell growth and division during root development.Science advances · 2025Article
- Empirical evidence that glucan-interacting amino acid side chains within the transmembrane channel collectively facilitate cellulose synthase function.Plant molecular biology · 2025Article
- COBRA-LIKE4 modulates cellulose synthase velocity and facilitates cellulose deposition in the secondary cell wall.Plant physiology · 2024Article
- A cellulose synthesis inhibitor affects cellulose synthase complex secretion and cortical microtubule dynamics.Plant physiology · 2024Article
- Discovery and Characterization of Fluopipamine, a Putative Cellulose Synthase 1 Antagonist withinJournal of agricultural and food chemistry · 2024Article
- Cellulose biosynthesis inhibitor isoxaben causes nutrient-dependent and tissue-specific Arabidopsis phenotypes.Plant physiology · 2024Article
- On the Mechanism of the Ionizing Radiation-Induced Degradation and Recycling of Cellulose.Polymers · 2023Review
- Wood cellulose microfibrils have a 24-chain core-shell nanostructure in seed plants.Nature plants · 2023Article
- Point mutations in the catalytic domain disrupt cellulose synthase (CESA6) vesicle trafficking and protein dynamics.The Plant cell · 2023Article
- Essential amino acids in the Plant-Conserved and Class-Specific Regions of cellulose synthases.Plant physiology · 2023Article
- A large-scale forward genetic screen for maize mutants with altered lignocellulosic properties.Frontiers in plant science · 2023Article
- Tip growth defective1 interacts with cellulose synthase A3 to regulate cellulose biosynthesis in Arabidopsis.Plant molecular biology · 2022Article
- Solid-State NMR Investigations of Extracellular Matrixes and Cell Walls of Algae, Bacteria, Fungi, and Plants.Chemical reviews · 2022Review
25 more citing papers are in PubMed but not listed here.
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15 authors at 8 institutions in 3 countries.
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Abstract
The mechanisms underlying the biosynthesis of cellulose in plants are complex and still poorly understood. A central question concerns the mechanism of microfibril structure and how this is linked to the catalytic polymerization action of cellulose synthase (CESA). Furthermore, it remains unclear whether modification of cellulose microfibril structure can be achieved genetically, which could be transformative in a bio-based economy. To explore these processes in planta, we developed a chemical genetic toolbox of pharmacological inhibitors and corresponding resistance-conferring point mutations in the C-terminal transmembrane domain region of CESA1(A903V) and CESA3(T942I) in Arabidopsis thaliana. Using (13)C solid-state nuclear magnetic resonance spectroscopy and X-ray diffraction, we show that the cellulose microfibrils displayed reduced width and an additional cellulose C4 peak indicative of a degree of crystallinity that is intermediate between the surface and interior glucans of wild type, suggesting a difference in glucan chain association during microfibril formation. Consistent with measurements of lower microfibril crystallinity, cellulose extracts from mutated CESA1(A903V) and CESA3(T942I) displayed greater saccharification efficiency than wild type. Using live-cell imaging to track fluorescently labeled CESA, we found that these mutants show increased CESA velocities in the plasma membrane, an indication of increased polymerization rate. Collectively, these data suggest that CESA1(A903V) and CESA3(T942I) have modified microfibril structure in terms of crystallinity and suggest that in plants, as in bacteria, crystallization biophysically limits polymerization.
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