Pseudobacteroides cellulosolvens
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA291110 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Other | ||||
| SRR2127984_1.fastq.gz | Fastqsanger.gz | |||
| SRR2127984_2.fastq.gz | Fastqsanger.gz | |||
| SRR3313895.fastq.gz | Fastqsanger.gz | |||
| SRR5272700_subreads.fastq.gz | Fastqsanger.gz |
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Similar Datasets
Project description:Eubacterium cellulosolvens overview
| PRJNA46173 | ENA
Project description:[Eubacterium] cellulosolvens LD2006 Genome sequencing and assembly
| PRJNA223050 | ENA
Project description:Pseudobacteroides cellulosolvens genome sequencing
| PRJNA290984 | ENA
Project description:Eubacterium cellulosolvens 6 genome sequencing project
| PRJNA45821 | ENA
Project description:Background (Pseudo)Bacteroides cellulosolvens is a cellulolytic bacterium producing the most extensive and intricate cellulosomal system known in nature. Recently, an elaborate architecture of B. cellulosolvens cellulosomal system was revealed from its genome sequence analysis, and first evidence on the interactions between its structural and enzymatic components were detected in vitro. Yet, the cellulolytic potential of the bacterium in carbohydrate deconstruction may reside only within complete high-molecular weight protein complexes, which are secreted from the bacterium. Results The current proteome-wide work reveals patterns of protein expression of various cellulosomal components, and explores the differential expression signature upon bacterial growth two carbon sources, either cellobiose or microcrystalline cellulose. Mass spectrometry analysis of the bacterial secretome fraction revealed the expression of 24 scaffoldin structural units and 166 dockerin-bearing enzymes, in addition to free enzymatic subunits. All these components comprise cell-free and cell-bound cellulosomes for more efficient carbohydrate degradation. Various glycoside hydrolase (GH) family memebers were represented among 102 carbohydrate-degrading enzymes, including the most abundant GH48 exoglucanase. Specific cellulosomal components were associatred with different carbon sources, in cellulosomal fractions of different molecular weights. Overall, microcrystalline cellulose-derived cellulosomes showed higher expression levels of the structural and enzymatic components, and exhibited the highest degradation activity on five different carbohydrates. The cellulosomal activity of B. cellulosolvens showed high degradation rates that are very promising in biotechnological terms and were compatible with the activity levels exhibited by C. thermocellum purified cellulosomes. Conclusions The current research demonstrates the involvement of key cellulosomal factors participating in the mechanism of carbohydrate degradation by B. cellulosolvens. The powerful ability of the bacterium to exhibit different degradation strategies of various carbon sourcesis revealed. Thus, a novel components reservoir of degradation machineries that may serve for subsequent cellulosomal research, as a pool for designing new cellulolytic cocktails for biotechnological purposes.
2019-11-13 | PXD012663 | Pride
Project description:Pseudobacteroides cellulosolvens ATCC 35603 = DSM 2933 Genome sequencing and assembly
| PRJNA221003 | ENA
Project description:Eubacterium cellulosolvens cleaved the flavone C-glucosides homoorientin and isovitexin to their aglycones luteolin and apigenin, respectively. The corresponding isomers, orientin and vitexin, or other polyphenolic C-glucosides were not deglycosylated. E. cellulosolvens also cleaved several O-coupled glucosides of flavones and isoflavones to their corresponding aglycones.
| S-EPMC3485936 | biostudies-literature
Project description:A cellulosomal scaffoldin gene, termed cipBc, was identified and sequenced from the mesophilic cellulolytic anaerobe Bacteroides cellulosolvens. The gene encodes a 2,292-residue polypeptide (excluding the signal sequence) with a calculated molecular weight of 242,437. CipBc contains an N-terminal signal peptide, 11 type II cohesin domains, an internal family III cellulose-binding domain (CBD), and a C-terminal dockerin domain. Its CBD belongs to family IIIb, like that of CipV from Acetivibrio cellulolyticus but unlike the family IIIa CBDs of other clostridial scaffoldins. In contrast to all other scaffoldins thus far described, CipBc lacks a hydrophilic domain or domain X of unknown function. The singularity of CipBc, however, lies in its numerous type II cohesin domains, all of which are very similar in sequence. One of the latter cohesin domains was expressed, and the expressed protein interacted selectively with cellulosomal enzymes, one of which was identified as a family 48 glycosyl hydrolase on the basis of partial sequence alignment. By definition, the dockerins, carried by the cellulosomal enzymes of this species, would be considered to be type II. This is the first example of authentic type II cohesins that are confirmed components of a cellulosomal scaffoldin subunit rather than a cell surface anchoring component. The results attest to the emerging diversity of cellulosomes and their component sequences in nature.
| S-EPMC111372 | biostudies-literature
Project description:Background(Pseudo) Bacteroides cellulosolvens is an anaerobic, mesophilic, cellulolytic, cellulosome-producing clostridial bacterium capable of utilizing cellulose and cellobiose as carbon sources. Recently, we sequenced the B. cellulosolvens genome, and subsequent comprehensive bioinformatic analysis, herein reported, revealed an unprecedented number of cellulosome-related components, including 78 cohesin modules scattered among 31 scaffoldins and more than 200 dockerin-bearing ORFs. In terms of numbers, the B. cellulosolvens cellulosome system represents the most intricate, compositionally diverse cellulosome system yet known in nature.ResultsThe organization of the B. cellulosolvens cellulosome is unique compared to previously described cellulosome systems. In contrast to all other known cellulosomes, the cohesin types are reversed for all scaffoldins i.e., the type II cohesins are located on the enzyme-integrating primary scaffoldin, whereas the type I cohesins are located on the anchoring scaffoldins. Many of the type II dockerin-bearing ORFs include X60 modules, which are known to stabilize type II cohesin-dockerin interactions. In the present work, we focused on revealing the architectural arrangement of cellulosome structure in this bacterium by examining numerous interactions between the various cohesin and dockerin modules. In total, we cloned and expressed 43 representative cohesins and 27 dockerins. The results revealed various possible architectures of cell-anchored and cell-free cellulosomes, which serve to assemble distinctive cellulosome types via three distinct cohesin-dockerin specificities: type I, type II, and a novel-type designated R (distinct from type III interactions, predominant in ruminococcal cellulosomes).ConclusionsThe results of this study provide novel insight into the architecture and function of the most intricate and extensive cellulosomal system known today, thereby extending significantly our overall knowledge base of cellulosome systems and their components. The robust cellulosome system of B. cellulosolvens, with its unique binding specificities and reversal of cohesin-dockerin types, has served to amend our view of the cellulosome paradigm. Revealing new cellulosomal interactions and arrangements is critical for designing high-efficiency artificial cellulosomes for conversion of plant-derived cellulosic biomass towards improved production of biofuels.
| S-EPMC5590126 | biostudies-literature
Project description:An overview of small RNAs sequences existing in seed development and contrasted with vegetative tissues of the soybean
2012-10-09 | GSE36728 | GEO