ArticleJournal of industrial microbiology & biotechnology2011
Glycoside hydrolases as components of putative carbohydrate biosensor proteins in Clostridium thermocellum.
Article in Journal of industrial microbiology & biotechnology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 47 citations in OpenAlex.
- The final proteolytic step in transmembrane signaling of multiple RsgI anti-σ factors in Clostridium thermocellum.Bioscience reports · 2025Article
- Current models in bacterial hemicellulase-encoding gene regulation.Applied microbiology and biotechnology · 2024Review
- Unique Fn3-like biosensor in σProtein science : a publication of the Protein Society · 2024Article
- Insight into the autoproteolysis mechanism of the RsgI9 anti-σ factor from Clostridium thermocellum.Proteins · 2024Article
- Essential autoproteolysis of bacterial anti-σ factor RsgI for transmembrane signal transduction.Science advances · 2023Article
- Expression profiling of Clostridium thermocellum B8 during the deconstruction of sugarcane bagasse and straw.World journal of microbiology & biotechnology · 2023Article
- The structure of the Clostridium thermocellum RsgI9 ectodomain provides insight into the mechanism of biomass sensing.Proteins · 2022Article
- Utilization of Monosaccharides byMicroorganisms · 2021Article
- Genome-Wide Transcription Factor DNA Binding Sites and Gene Regulatory Networks inFrontiers in microbiology · 2021Article
- Transcriptomic analysis of a Clostridium thermocellum strain engineered to utilize xylose: responses to xylose versus cellobiose feeding.Scientific reports · 2020Article
- Caldicellulosiruptor bescii Adheres to Polysaccharides via a Type IV Pilin-Dependent Mechanism.Applied and environmental microbiology · 2020Article
- A Novel Subfamily of Endo-β-1,4-Glucanases in Glycoside Hydrolase Family 10.Applied and environmental microbiology · 2019Article
- Unraveling essential cellulosomal components of the (Biotechnology for biofuels · 2019Article
- Inducing effects of cellulosic hydrolysate components of lignocellulose on cellulosome synthesis in Clostridium thermocellum.Microbial biotechnology · 2018Article
- Regulation of biomass degradation by alternative σ factors in cellulolytic clostridia.Scientific reports · 2018Article
- LacI Transcriptional Regulatory Networks in Clostridium thermocellum DSM1313.Applied and environmental microbiology · 2017Article
- The LacI family protein GlyR3 co-regulates theBiotechnology for biofuels · 2017Article
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- Crucial roles of single residues in binding affinity, specificity, and promiscuity in the cellulosomal cohesin-dockerin interface.The Journal of biological chemistry · 2015Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The composition of the cellulase system in the cellulosome-producing bacterium, Clostridium thermocellum, has been reported to change in response to growth on different carbon sources. Recently, an extensive carbohydrate-sensing mechanism, purported to regulate the activation of genes coding for polysaccharide-degrading enzymes, was suggested. In this system, CBM modules, comprising extracellular components of RsgI-like anti-σ factors, were proposed to function as carbohydrate sensors, through which a set of cellulose utilization genes are activated by the associated σ(I)-like factors. An extracellular module of one of these RsgI-like proteins (Cthe_2119) was annotated as a family 10 glycoside hydrolase, RsgI6-GH10, and a second putative anti-σ factor (Cthe_1471), related in sequence to Rsi24, was found to contain a module that resembles a family 5 glycoside hydrolase (termed herein Rsi24C-GH5). The present study examines the relevance of these two glycoside hydrolases as sensors in this signal-transmission system. The RsgI6-GH10 was found to bind xylan matrices but exhibited low enzymatic activity on this substrate. In addition, this glycoside hydrolase module was shown to interact with crystalline cellulose although no hydrolytic activity was detected on cellulosic substrates. Bioinformatic analysis of the Rsi24C-GH5 showed a glutamate-to-glutamine substitution that would presumably preclude catalytic activity. Indeed, the recombinant module was shown to bind to cellulose, but showed no hydrolytic activity. These observations suggest that these two glycoside hydrolases underwent an evolutionary adaptation to function as polysaccharide binding agents rather than enzymatic components and thus serve in the capacity of extracellular carbohydrate sensors.
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