ArticleJournal of bacteriology2008
Mutations in the scaffoldin gene, cipA, of Clostridium thermocellum with impaired cellulosome formation and cellulose hydrolysis: insertions of a new transposable element, IS1447, and implications for cellulase synergism on crystalline cellulose.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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36 citing papers in PubMed, 68 citations in OpenAlex.
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- Lignocellulose degradation in bacteria and fungi: cellulosomes and industrial relevance.Frontiers in microbiology · 2025Review
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- Research progress of multi-enzyme complexes based on the design of scaffold protein.Bioresources and bioprocessing · 2023Review
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- A Single Nucleotide Change in theApplied and environmental microbiology · 2022Article
- Genetically Encodable Scaffolds for Optimizing Enzyme Function.Molecules (Basel, Switzerland) · 2021Review
- Inducing effects of cellulosic hydrolysate components of lignocellulose on cellulosome synthesis in Clostridium thermocellum.Microbial biotechnology · 2018Article
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- Firmicutes-enriched ISBiotechnology for biofuels · 2018Article
- Optimizing the composition of a synthetic cellulosome complex for the hydrolysis of softwood pulp: identification of the enzymatic core functions and biochemical complex characterization.Biotechnology for biofuels · 2018Article
- Revisiting the Regulation of the Primary Scaffoldin Gene in Clostridium thermocellum.Applied and environmental microbiology · 2017Article
- Cellulosomes: bacterial nanomachines for dismantling plant polysaccharides.Nature reviews. Microbiology · 2017Review
- Comparative characterization of all cellulosomal cellulases fromBiotechnology for biofuels · 2017Article
- How does cellulosome composition influence deconstruction of lignocellulosic substrates inBiotechnology for biofuels · 2017Article
- Enzymatic diversity of the Clostridium thermocellum cellulosome is crucial for the degradation of crystalline cellulose and plant biomass.Scientific reports · 2016Article
- Dramatic performance of Clostridium thermocellum explained by its wide range of cellulase modalities.Science advances · 2016Article
- Stoichiometric Assembly of the Cellulosome Generates Maximum Synergy for the Degradation of Crystalline Cellulose, as Revealed by In Vitro Reconstitution of the Clostridium thermocellum Cellulosome.Applied and environmental microbiology · 2015Article
- Article
- Clostridium thermocellum DSM 1313 transcriptional responses to redox perturbation.Biotechnology for biofuels · 2015Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mutants of Clostridium thermocellum that had lost the ability to adhere to microcrystalline cellulose were isolated. Six of them that showed diminished ability to depolymerize crystalline cellulose were selected. Size exclusion chromatography of the proteins from the culture supernatant revealed the loss of the supramolecular enzyme complex, the cellulosome. However, denaturing sodium dodecyl sulfate-polyacrylamide gel electrophoresis resulted in extracellular protein patterns comparable to those of isolated cellulosomes, except for a missing CipA band. Sequencing of the six mutant cipA genes revealed a new insertion (IS) element, IS1447, belonging to the IS3 family. It was inserted into the cipA reading frame in four different locations: cohesin module 1, two different positions in the carbohydrate binding module, and cohesin module 3. The IS sequences were identical and consisted of a transposase gene and the inverted repeats IRR and IRS. The insertion resulted in an obviously nonspecific duplication of 3 base pairs within the target sequence. This lack of specificity allows transposition without the need of a defined target DNA sequence. Eighteen copies of IS1447 were identified in the genomic sequence of C. thermocellum ATCC 27405. At least one of them can be activated for transposition. Compared to the wild type, the mutant culture supernatant, with a completely defective CipA protein, showed equal specific hydrolytic activity against soluble beta-glucan but a 15-fold reduction in specific activity with crystalline cellulose. These results identify a genetic basis for the synergistic effect of complex formation on crystalline-cellulose degradation.
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