ArticleApplied and environmental microbiology2011
Use of label-free quantitative proteomics to distinguish the secreted cellulolytic systems of Caldicellulosiruptor bescii and Caldicellulosiruptor obsidiansis.
Article in Applied and environmental microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 78 citations in OpenAlex.
- Teredinibacter turnerae secretome highlights key enzymes for plant cell wall degradation.Bioresources and bioprocessing · 2025Article
- Role of cell-substrate association during plant biomass solubilization by the extreme thermophile Caldicellulosiruptor bescii.Extremophiles : life under extreme conditions · 2023Article
- Characterization of the Biomass Degrading Enzyme GuxA fromInternational journal of molecular sciences · 2022Article
- Proteomic perspectives on thermotolerant microbes: an updated review.Molecular biology reports · 2022Review
- Bioconversion of Lignocellulosic Biomass into Value Added Products under Anaerobic Conditions: Insight into Proteomic Studies.International journal of molecular sciences · 2021Review
- Perturbation of the peptidoglycan network and utilization of the signal recognition particle-dependent pathway enhances the extracellular production of a truncational mutant of CelA in Escherichia coli.Journal of industrial microbiology & biotechnology · 2021Article
- Coexpression of a β-d-Xylosidase from Thermotoga maritima and a Family 10 Xylanase from Acidothermus cellulolyticus Significantly Improves the Xylan Degradation Activity of the Caldicellulosiruptor bescii Exoproteome.Applied and environmental microbiology · 2021Article
- Deletion of a Peptidylprolyl Isomerase Gene Results in the Inability ofApplied and environmental microbiology · 2020Article
- Caldicellulosiruptor bescii Adheres to Polysaccharides via a Type IV Pilin-Dependent Mechanism.Applied and environmental microbiology · 2020Article
- Insights into Thermophilic Plant Biomass Hydrolysis fromMicroorganisms · 2020Review
- The GH10 and GH48 dual-functional catalytic domains from a multimodular glycoside hydrolase synergize in hydrolyzing both cellulose and xylan.Biotechnology for biofuels · 2019Article
- Creation of a functional hyperthermostable designer cellulosome.Biotechnology for biofuels · 2019Article
- Expression of a Cellobiose Phosphorylase from Thermotoga maritima in Caldicellulosiruptor bescii Improves the Phosphorolytic Pathway and Results in a Dramatic Increase in Cellulolytic Activity.Applied and environmental microbiology · 2018Article
- High activity CAZyme cassette for improving biomass degradation in thermophiles.Biotechnology for biofuels · 2018Article
- Expression of an endoglucanase-cellobiohydrolase fusion protein inBiotechnology for biofuels · 2018Article
- Article
- Deletion of a single glycosyltransferase inBiotechnology for biofuels · 2018Article
- The diversity and specificity of the extracellular proteome in the cellulolytic bacteriumBiotechnology for biofuels · 2018Article
- Functional Analysis of the Glucan Degradation Locus in Caldicellulosiruptor bescii Reveals Essential Roles of Component Glycoside Hydrolases in Plant Biomass Deconstruction.Applied and environmental microbiology · 2017Article
- Heterologous expression of a β-D-glucosidase in Caldicellulosiruptor bescii has a surprisingly modest effect on the activity of the exoproteome and growth on crystalline cellulose.Journal of industrial microbiology & biotechnology · 2017Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The extremely thermophilic, Gram-positive bacteria Caldicellulosiruptor bescii and Caldicellulosiruptor obsidiansis efficiently degrade both cellulose and hemicellulose, which makes them relevant models for lignocellulosic biomass deconstruction to produce sustainable biofuels. To identify the shared and unique features of secreted cellulolytic apparatuses from C. bescii and C. obsidiansis, label-free quantitative proteomics was used to analyze protein abundance over the course of fermentative growth on crystalline cellulose. Both organisms' secretomes consisted of more than 400 proteins, of which the most abundant were multidomain glycosidases, extracellular solute-binding proteins, flagellin, putative pectate lyases, and uncharacterized proteins with predicted secretion signals. Among the identified proteins, 53 to 57 significantly changed in abundance during cellulose fermentation in favor of glycosidases and extracellular binding proteins. Mass spectrometric characterizations, together with cellulase activity measurements, revealed a substantial abundance increase of a few bifunctional multidomain glycosidases composed of glycosidase (GH) domain family 5, 9, 10, 44, or 48 and family 3 carbohydrate binding (CBM3) modules. In addition to their orthologous cellulases, the organisms expressed unique glycosidases with different domain organizations: C. obsidiansis expressed the COB47_1671 protein with GH10/5 domains, while C. bescii expressed the Athe_1857 (GH10/48) and Athe_1859 (GH5/44) proteins. Glycosidases containing CBM3 domains were selectively enriched via binding to amorphous cellulose. Preparations from both bacteria contained highly thermostable enzymes with optimal cellulase activities at 85°C and pH 5. The C. obsidiansis preparation, however, had higher cellulase specific activity and greater thermostability. The C. bescii culture produced more extracellular protein and additional SDS-PAGE bands that demonstrated glycosidase activity.
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