Ruminiclostridium cellulolyticum
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA247408 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR1286060_1.fastq.gz | Fastqsanger.gz | |||
| SRR1286060_2.fastq.gz | Fastqsanger.gz | |||
| SRR1286061_1.fastq.gz | Fastqsanger.gz | |||
| SRR1286061_2.fastq.gz | Fastqsanger.gz | |||
| SRR1286062_1.fastq.gz | Fastqsanger.gz |
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Similar Datasets
Project description:DNA targeting by Clostridium cellulolyticum CRISPR Cas9 Type II-C system
| PRJNA554628 | ENA
Project description:Clostridium cellulolyticum overview
| PRJNA35941 | ENA
Project description:Cellulose degrading anaerobe
| PRJNA17419 | ENA
Project description:Xyloglucan, a ubiquitous highly branched plant polysaccharide, was found to be rapidly degraded and metabolized by the cellulosome-producing bacterium Ruminiclostridium cellulolyticum. Our study shows that at least four cellulosomal enzymes displaying either endo- or exoxyloglucanase activities, achieve the extracellular degradation of xyloglucan into 4-glucosyl backbone xyloglucan oligosaccharides. The released oligosaccharides (composed of up to 9 monosaccharides) are subsequently imported by a highly specific ATP-binding cassette transporter (ABC-transporter), the expression of the corresponding genes being strongly induced by xyloglucan. This polysaccharide also triggers the synthesis of cytoplasmic β-galactosidase, α-xylosidase, and β-glucosidase that act sequentially to convert the imported oligosaccharides into galactose, xylose, glucose and unexpectedly cellobiose. Thus R. cellulolyticum has developed an energy-saving strategy to metabolize this hemicellulosic polysaccharide that relies on the action of the extracellular cellulosomes, a highly specialized ABC-transporter, and cytoplasmic enzymes acting in a specific order. This strategy appears to be widespread among cellulosome-producing mesophilic bacteria which display highly similar gene clusters encoding the cytosolic enzymes and the ABC-transporter.
| S-EPMC4780118 | biostudies-literature
Project description:The 5’ end RNA molecules transcribed by RNA polymerase II are known to be modified in human cells. Specifically, A-initiated transcripts can be methylated at both the 2’-O position in the ribose (2’-O-methylation, or cap-1) and the N6-position in the base (N6-methylation). Almost all A-initiated transcripts have the cap-1 modification, however, the N6-methylation is optional. As a result, A-initiated transcripts in the cell can be Am (cap-1 only) or m6Am (cap-1 and N6-methylation) modified. To study m6Am, we developed CROWN-seq, which simultaneously obtains the transcription-start information and the stoichiometry of N6-methyl. With CROWN-seq, we found that the previous m6Am mapping studies highly underestimated the diversity of the transcription-start site (nucleotide) of the transcriptome. In this study, we used CROWN-seq to reveal m6Am sites and stoichiometry among different human cell lines. We demonstrated that m6Am stoichiometry in mRNA is in general high, however, m6Am stoichiometry in snRNA, snoRNA, and their pseudogenes is more variable.
2024-12-02 | GSE233655 | GEO
Project description:Ruminiclostridium cellulolyticum (Clostridium cellulolyticum) is a mesophilic cellulolytic anaerobic bacterium that produces a multi-enzymatic system composed of cellulosomes and non-cellulosomal enzymes to degrade plant cell wall polysaccharides. We characterized one of the non-cellulosomal enzymes, Cel5I, composed of a Family-5 Glycoside Hydrolase catalytic module (GH5), a tandem of Family-17 and -28 Carbohydrate Binding Modules (CBM), and three S-layer homologous (SLH) modules, where the latter are expected to anchor the protein on the cell surface. Cel5I is the only putative endoglucanase targeting the cell surface as well as the only putative protein in R. cellulolyticum containing CBM17 and/or CBM28 modules. We characterized different recombinant structural variants from Cel5I. We showed that Cel5I has an affinity for insoluble cellulosic substrates through its CBMs, that it is the most active endoglucanase on crystalline cellulose of R. cellulolyticum characterized to date and mostly localized in the cell envelope of R. cellulolyticum. Its role in vivo was analyzed using a R. cellulolyticum cel5I mutant strain. Absence of Cel5I in the cell envelope did not lead to a significant variation of the phenotype compared to the wild type strain. Neither in terms of cell binding to cellulose, nor for its growth on crystalline cellulose, thus indicating that the protein has a rather subtle role in tested conditions. Cel5I might be more important in a natural environment, at low concentration of degradable glucose polymers, where its role might be to generate higher concentration of short cellodextrins close to the cell surface, facilitating their uptake or for signalization purpose.
| S-EPMC4976890 | biostudies-literature
Project description:BackgroundAnaerobic, mesophilic, and cellulolytic Ruminiclostridium cellulolyticum produces an efficient cellulolytic extracellular complex named cellulosome, which consist of a non-catalytic multi-functional integrating subunit, organizing the various catalytic subunits into the complex. Main components of cellulosome were encoded by the cip-cel operon in R. cellulolyticum, and their stoichiometry is controlled by the mechanism of selective RNA processing and stabilization, which allows to confer each processed RNA portion from the cip-cel mRNA on different fates due to their stability and resolve the potential contradiction between the equimolar stoichiometry of transcripts with a within a transcription unit and the non-equimolar stoichiometry of subunits.ResultsIn this work, RNA processing events were found to occur at six intergenic regions (IRs) harboring stem-loop structures in cip-cel operon. These stem-loops not only stabilize processed transcripts at their both ends, but also act as cleavage signals specifically recognized by endoribonucleases. We further demonstrated that cleavage sites were often located downstream or 3' end of their associated stem-loops that could be classified into two types, with distinct GC-rich stems being required for RNA cleavage. However, the cleavage site in IR4 was found to be located upstream of the stem-loop, as determined by the bottom AT-pair region of this stem-loop, together with its upstream structure. Thus, our findings reveal the structural requirements for processing of cip-cel transcripts, which can be potentially used to control the stoichiometry of gene expression in an operon.ConclusionsOur findings reveal that stem-loop structures acting as RNA cleavage signals not only can be recognized by endoribonucleases and determine the location of cleavage sites but also determine the stoichiometry of their flanking processed transcripts by controlling stability in cip-cel operon. These features represent a complexed regulation of cellulosome in the post-transcriptional level, which can be exploited for designing synthetic elements to control gene expression.
| S-EPMC10311766 | biostudies-literature
Project description:R. cellulolyticum strains (the parent strain, ΔccpA, ΔccpB and Δcph) were cultivated in defined VM medium with cellulose (10 g/L).Since ΔccpA and Δcph could not grow on cellulose, we performed an incubation experiment to understand how ΔccpA and Δcph respond to cellulose. Specifically, the parent strain, ΔccpA and Δcph were grown to an OD600 of 0.5-0.6 in 50 ml defined VM media with cellobiose as the carbon source. Each strain had three biological replicates. Bacterial cells from each biological replicate were then collected by centrifugation at 4000 g and washed twice with the defined VM medium (no carbon added). Finally, washed cells from each biological replicate were inoculated into the defined VM medium with 10 g/L cellulose. During shaking incubation at 34°C, samples were collected at five time points (0,1, 3, 6, 12 hours). After centrifugation at 4°C, 5000×g for 10 min, cell pellets were immediately flash frozen with liquid nitrogen and then stored at -80°C for further use. For ΔccpB, ΔccpB and the parent strain were cultivated with six biological replicates and collected at mid-exponential growth phase.
2022-06-19 | E-MTAB-11774 | biostudies-arrayexpress
Project description:Cellulolytic microorganisms play a key role in the global carbon cycle by decomposing structurally diverse plant biopolymers from dead plant matter. These microorganisms, in particular anaerobes such as Ruminiclostridium cellulolyticum that are capable of degrading and catabolizing several different polysaccharides, require a fine-tuned regulation of the biosynthesis of their polysaccharide-degrading enzymes. In this study, we present a bacterial regulatory system involved in the regulation of genes enabling the metabolism of the ubiquitous plant polysaccharide xyloglucan. The characterization of R. cellulolyticum knockout mutants suggests that the response regulator XygR and its cognate histidine kinase XygS are essential for growth on xyloglucan. Using in vitro and in vivo analyses, we show that XygR binds to the intergenic region and activates the expression of two polycistronic transcriptional units encoding an ABC transporter dedicated to the uptake of xyloglucan oligosaccharides and the two-component system itself together with three intracellular glycoside hydrolases responsible for the sequential intracellular degradation of the imported oligosaccharides into mono- and disaccharides. Interestingly, XygR also upregulates the expression of a distant gene coding for the most active extracellular cellulosomal xyloglucanase of R. cellulolyticum by binding to the upstream intergenic region.IMPORTANCERuminiclostridium cellulolyticum is a Gram-positive, mesophilic, anaerobic, cellulolytic, and hemicellulolytic bacterium. The last property qualifies this species as a model species for the study of hemicellulose degradation, import of degradation products, and overall regulation of these phenomena. In this study, we focus on the regulation of xyloglucan dextrin import and intracellular degradation and show that the two components of the two-component regulation system XygSR are essential for growth on xyloglucan and that the response regulator XygR regulates the transcription of genes involved in the extracellular degradation of the polysaccharide, the import of degradation products, and their intracellular degradation.
| S-EPMC7531976 | biostudies-literature
Project description:Here a differential mRNA-sequencing (dRNA-Seq) strategy was employed to distinguish transcriptional start-sites (TSs) and post-transcriptional processed sites (PSs) of transcripts in the cellulolytic mesophile Clostridium cellulolyticum. PS-harboring genes usually encode heteromultimeric complexes such as flagella, ribosomes, F-type ATPases, and cellulosomes. Intriguingly, PSs located in intergenic reigons (iPSs) were appear to be associated with a particular set of operons that expressed as a complex ratio, in which stem-loops were often found at upstream and/or downstream of highly-expressed processed transcripts; among operons, the folding free energy (deltaG) of the stem-loops is negatively correlated with polarity in transcript level of the operon.
2015-04-27 | GSE57652 | GEO