ArticleNature communications2015
Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- The carbohydrate-binding module of TrCel7A aids in navigating hemicellulose barriers in plant cell walls.The Journal of biological chemistry · 2026Article
- Reporter Group-Labeled Synthetic Cellulose: Structural Characterization and Utilization in Mapping the Cellulose Chain-Cleavage Modes of Cellulases.Biomacromolecules · 2026Article
- There is an "I" in team: individual improvements in supercharged cellulase cocktail facilitates cooperative cellulose degradation.Biotechnology for biofuels and bioproducts · 2026Article
- Stochastic model highlights the impact of crystallinity on saccharification dynamics depending on plant chemotype and pre-treatment.PloS one · 2025Article
- Thermobifida fusca Cel6B moves bidirectionally while processively degrading cellulose.Biotechnology for biofuels and bioproducts · 2024Article
- Single-molecule tracking reveals dual front door/back door inhibition of Cel7A cellulase by its product cellobiose.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Motility of an autonomous protein-based artificial motor that operates via a burnt-bridge principle.Nature communications · 2024Article
- Mechanochemical Coupling of Catalysis and Motion in a Cellulose-Degrading Multienzyme Nanomachine.ACS catalysis · 2024Article
- Constitutive overexpression of cellobiohydrolase 2 inEngineering microbiology · 2023Article
- Characterizing Biophysical Parameters of Single TCR-pMHC Interactions Using Optical Tweezers.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Acoustic force spectroscopy reveals subtle differences in cellulose unbinding behavior of carbohydrate-binding modules.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Single-molecule investigations of single-chain cellulose biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Myosin II Adjusts Motility Properties and Regulates Force Production Based on Motor Environment.Cellular and molecular bioengineering · 2022Article
- X-Ray Scattering Reveals Two Mechanisms of Cellulose Microfibril Degradation by Filamentous Fungi.Applied and environmental microbiology · 2022Article
- Enzyme Synergy in Transient Clusters of Endo- and Exocellulase Enables a Multilayer Mode of Processive Depolymerization of Cellulose.ACS catalysis · 2022Article
- Processive Enzymes Kept on a Leash: How Cellulase Activity in Multienzyme Complexes Directs Nanoscale Deconstruction of Cellulose.ACS catalysis · 2021Article
- Stochastic model of lignocellulosic material saccharification.PLoS computational biology · 2021Article
- Disruption of alpha-tubulin releases carbon catabolite repression and enhances enzyme production in Trichoderma reesei even in the presence of glucose.Biotechnology for biofuels · 2021Article
- A microalgal-based preparation with synergistic cellulolytic and detoxifying action towards chemical-treated lignocellulose.Plant biotechnology journal · 2021Article
- A Comparative Transcriptome Analysis ofGenes · 2020Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cellobiohydrolase 1 from Trichoderma reesei (TrCel7A) processively hydrolyses cellulose into cellobiose. Although enzymatic techniques have been established as promising tools in biofuel production, a clear understanding of the motor's mechanistic action has yet to be revealed. Here, we develop an optical tweezers-based single-molecule (SM) motility assay for precision tracking of TrCel7A. Direct observation of motility during degradation reveals processive runs and distinct steps on the scale of 1 nm. Our studies suggest TrCel7A is not mechanically limited, can work against 20 pN loads and speeds up when assisted. Temperature-dependent kinetic studies establish the energy requirements for the fundamental stepping cycle, which likely includes energy from glycosidic bonds and other sources. Through SM measurements of isolated TrCel7A domains, we determine that the catalytic domain alone is sufficient for processive motion, providing insight into TrCel7A's molecular motility mechanism.
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