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Dictyoglomus turgidum DSM 6724

ABSTRACT: Hot spring isolate

PROVIDER: PRJNA29175 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR018125.fastq.gz	Fastqsanger.gz
	SRR018126.fastq.gz	Fastqsanger.gz
	SRR018127.fastq.gz	Fastqsanger.gz
	SRR018128.fastq.gz	Fastqsanger.gz
	SRR018129.fastq.gz	Fastqsanger.gz

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Expression, crystallization and preliminary X-ray crystallographic analysis of cellobiose 2-epimerase from Dictyoglomus turgidum DSM 6724.

Project description:Cellobiose 2-epimerase epimerizes and isomerizes ?-1,4- and ?-1,4-gluco-oligosaccharides. N-Acyl-D-glucosamine 2-epimerase (DT_epimerase) from Dictyoglomus turgidum has an unusually high catalytic activity towards its substrate cellobiose. DT_epimerase was expressed, purified and crystallized. Crystals were obtained of both His-tagged DT_epimerase and untagged DT_epimerase. The crystals of His-tagged DT_epimerase diffracted to 2.6?Å resolution and belonged to the monoclinic space group P2?, with unit-cell parameters a=63.9, b=85.1, c=79.8?Å, ?=110.8°. With a Matthews coefficient VM of 2.18?Å3?Da(-1), two protomers were expected to be present in the asymmetric unit with a solvent content of 43.74%. The crystals of untagged DT_epimerase diffracted to 1.85?Å resolution and belonged to the orthorhombic space group P2?2?2?, with unit-cell parameters a=55.9, b=80.0, c=93.7?Å. One protomer in the asymmetric unit was expected, with a corresponding VM of 2.26?Å3?Da(-1) and a solvent content of 45.6%.

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The Complete Genome Sequence of Hyperthermophile <i>Dictyoglomus turgidum</i> DSM 6724™ Reveals a Specialized Carbohydrate Fermentor.

Project description:Here we report the complete genome sequence of the chemoorganotrophic, extremely thermophilic bacterium, Dictyoglomus turgidum, which is a Gram negative, strictly anaerobic bacterium. D. turgidum and D. thermophilum together form the Dictyoglomi phylum. The two Dictyoglomus genomes are highly syntenic, and both are distantly related to Caldicellulosiruptor spp. D. turgidum is able to grow on a wide variety of polysaccharide substrates due to significant genomic commitment to glycosyl hydrolases, 16 of which were cloned and expressed in our study. The GH5, GH10, and GH42 enzymes characterized in this study suggest that D. turgidum can utilize most plant-based polysaccharides except crystalline cellulose. The DNA polymerase I enzyme was also expressed and characterized. The pure enzyme showed improved amplification of long PCR targets compared to Taq polymerase. The genome contains a full complement of DNA modifying enzymes, and an unusually high copy number (4) of a new, ancestral family of polB type nucleotidyltransferases designated as MNT (minimal nucleotidyltransferases). Considering its optimal growth at 72°C, D. turgidum has an anomalously low G+C content of 39.9% that may account for the presence of reverse gyrase, usually associated with hyperthermophiles.

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Enhanced features of Dictyoglomus turgidum Cellulase A engineered with carbohydrate binding module 11 from Clostridium thermocellum.

Project description:Lignocellulosic biomass (LCB) is a low-cost and abundant source of fermentable sugars. Enzymatic hydrolysis is one of the main ways to obtain sugars from biomass, but most of the polysaccharide-degrading enzymes are poorly efficient on LCB and cellulases with higher performances are required. In this study, we designed a chimeric protein by adding the carbohydrate binding module (CBM) of the cellulosomal enzyme CtLic26A-Cel5E (endoglucanase H or CelH) from Clostridium (Ruminiclostridium) thermocellum to the C-terminus of Dtur CelA, an interesting hyperthermostable endoglucanase from Dictyoglomus turgidum. The activity and binding rate of both native and chimeric enzyme were evaluated on soluble and insoluble polysaccharides. The addition of a CBM resulted in a cellulase with enhanced stability at extreme pHs, higher affinity and activity on insoluble cellulose.

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