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Caldanaerobacter subterraneus subsp. tengcongensis MB4

ABSTRACT: RNA-Seq of Thermoanaerobacter tengcongensis MB4

PROVIDER: PRJNA202960 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR851139_1.fastq.gz	Fastqsanger.gz
	SRR851139_2.fastq.gz	Fastqsanger.gz
	SRR851140_1.fastq.gz	Fastqsanger.gz
	SRR851140_2.fastq.gz	Fastqsanger.gz
	SRR851141_1.fastq.gz	Fastqsanger.gz

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Caldanaerobacter subterraneus subsp. tengcongensis MB4

Project description:Thermoanaerobacter tengcongensis MB4 Transcriptome at different temperatures

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Caldanaerobacter subterraneus subsp. tengcongensis MB4 isolate:JCM 11007

Project description:Thermoanaerobacter tengcongensis MB4 genome sequencing

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Caldanaerobacter subterraneus subsp. tengcongensis MB4

Project description:Caldanaerobacter subterraneus subsp. tengcongensis MB4 Transcriptome or Gene expression

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Caldanaerobacter subterraneus subsp. tengcongensis

Project description:Caldanaerobacter subterraneus subsp. tengcongensis Genome sequencing and assembly

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Crystal structure of acetylxylan esterase from Caldanaerobacter subterraneus subsp. tengcongensis.

Project description:The acetylxylan esterases (AXEs) classified into carbohydrate esterase family 4 (CE4) are metalloenzymes that catalyze the deacetylation of acetylated carbohydrates. AXE from Caldanaerobacter subterraneus subsp. tengcongensis (TTE0866), which belongs to CE4, is composed of three parts: a signal sequence (residues 1-22), an N-terminal region (NTR; residues 23-135) and a catalytic domain (residues 136-324). TTE0866 catalyzes the deacetylation of highly substituted cellulose acetate and is expected to be useful for industrial applications in the reuse of resources. In this study, the crystal structure of TTE0866 (residues 23-324) was successfully determined. The crystal diffracted to 1.9 Å resolution and belonged to space group I212121. The catalytic domain (residues 136-321) exhibited a (β/α)7-barrel topology. However, electron density was not observed for the NTR (residues 23-135). The crystal packing revealed the presence of an intermolecular space without observable electron density, indicating that the NTR occupies this space without a defined conformation or was truncated during the crystallization process. Although the active-site conformation of TTE0866 was found to be highly similar to those of other CE4 enzymes, the orientation of its Trp264 side chain near the active site was clearly distinct. The unique orientation of the Trp264 side chain formed a different-shaped cavity within TTE0866, which may contribute to its reactivity towards highly substituted cellulose acetate.

| S-EPMC8561816 | biostudies-literature

Caldanaerobacter subterraneus subsp. tengcongensis MB4

Project description:Hyperthermophilic eubacterium

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Functional analysis of the N-terminal region of acetylxylan esterase from Caldanaerobacter subterraneus subsp. tengcongensis.

Project description:Acetylxylan esterase from Caldanaerobacter subterraneus subsp. tengcongensis (TTE0866) has an N-terminal region (NTR; residues 23-135) between the signal sequence (residues 1-22) and the catalytic domain (residues 136-324), which is of unknown function. Our previous study revealed the crystal structure of the wild-type (WT) enzyme containing the NTR and the catalytic domain. Although the structure of the catalytic domain was successfully determined, that of the NTR was undetermined, as its electron density was unclear. In this study, we investigated the role of the NTR through functional and structural analyses of NTR truncation mutants. Based on sequence and secondary structure analyses, NTR was confirmed to be an intrinsically disordered region. The truncation of NTR significantly decreased the solubility of the proteins at low salt concentrations compared with that of the WT. The NTR-truncated mutant easily crystallized in a conventional buffer solution. The crystal exhibited crystallographic properties comparable with those of the WT crystals suitable for structural determination. These results suggest that NTR plays a role in maintaining the solubility and inhibiting the crystallization of the catalytic domain.

| S-EPMC9527590 | biostudies-literature

Thermostable lipases from the extreme thermophilic anaerobic bacteria Thermoanaerobacter thermohydrosulfuricus SOL1 and Caldanaerobacter subterraneus subsp. tengcongensis.

Project description:Two novel genes encoding for heat and solvent stable lipases from strictly anaerobic extreme thermophilic bacteria Thermoanaerobacter thermohydrosulfuricus (LipTth) and Caldanaerobacter subterraneus subsp. tengcongensis (LipCst) were successfully cloned and expressed in E. coli. Recombinant proteins were purified to homogeneity by heat precipitation, hydrophobic interaction, and gel filtration chromatography. Unlike the enzymes from mesophile counterparts, enzymatic activity was measured at a broad temperature and pH range, between 40 and 90 degrees C and between pH 6.5 and 10; the half-life of the enzymes at 75 degrees C and pH 8.0 was 48 h. Inhibition was observed with 4-(2-aminoethyl)-benzenesulfonyl fluoride hydrochloride and phenylmethylsulfonylfluorid indicating that serine and thiol groups play a role in the active site of the enzymes. Gene sequence comparisons indicated very low identity to already described lipases from mesophilic and psychrophilic microorganisms. By optimal cultivation of E. coli Tuner (DE3) cells in 2-l bioreactors, a massive production of the recombinant lipases was achieved (53-2200 U/l) Unlike known lipases, the purified robust proteins are resistant against a large number of organic solvents (up to 99%) and detergents, and show activity toward a broad range of substrates, including triacylglycerols, monoacylglycerols, esters of secondary alcohols, and p-nitrophenyl esters. Furthermore, the enzyme from T. thermohydrosulfuricus is suitable for the production of optically pure compounds since it is highly S-stereoselective toward esters of secondary alcohols. The observed E values for but-3-yn-2-ol butyrate and but-3-yn-2-ol acetate of 21 and 16, respectively, make these enzymes ideal candidates for kinetic resolution of synthetically useful compounds.

| S-EPMC2757599 | biostudies-literature

Label-free based proteomic study of Thermoanaerobacter tengcongensis

Project description:In order to study the protein responsive network to thermal stress, the proteome analysis of Thermoanaerobacter tengcongensis, a kind of anaerobic thermophilic eubacterium, were performed.

2014-03-30 | PXD000864 | Pride

Temperature-dependent Proteome Study of Thermoanaerobacter tengcongensis

Project description:Comprehensive and quantitative information of the thermophile proteome is an important source for understanding of the survival mechanism under high growth temperature. Thermoanaerobacter tengcongensis (T. tengcongensis), a typical anaerobic thermophilic eubacterium, was selected to quantitatively evaluate its protein abundance changes in response to four different temperatures. Thermoanaerobacter tengcongensis proteins were trypsine digested, separated with high-pH RP, and identified with MS/MS analysis. The raw MS/MS data were converted into MGF format by Proteome Discoverer 1.2 (Thermo Fisher Scientific, Waltham, MA, USA). And the exported MGF files were searched by Mascot 2.3.02 (Matrix Science, Boston, MA, USA) against the database with all 2588 predicted proteins in T. tengcongensis downloaded from NCBI (NCBI reference sequence: NC_003869.1). An automatic decoy database search was performed. Several parameters in Mascot were set for peptide searching, tolerance of one missed cleavage of trypsin, Carbamidomethyl (C),iTRAQ8plex (K) and iTRAQ8plex (N-term) as fixed modification, iTRAQ8plex (Y),Oxidation (M) as variable modification. The precursor mass tolerance was 10 ppm, and the product ion tolerance was 0.02 Da.

2013-08-13 | PXD000264 | Pride

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