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Geobacillus thermodenitrificans subsp. thermodenitrificans DSM 465

ABSTRACT: Geobacillus thermodenitrificans subsp. thermodenitrificans DSM 465 Genome sequencing and assembly

PROVIDER: PRJNA224955 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	AYKT01.dat.gz	Other
	AYKT01.fasta.gz	Fasta.gz
	AYKT01.master.dat	Other
	AYKT01.dat.gz	Other

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Geobacillus thermodenitrificans subsp. thermodenitrificans DSM 465 isolate:DSM 465

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Transcriptome analysis of collagen-adhered S. gallolyticus subsp. gallolyticus [DSM 16831]

Project description:Streptococcus gallolyticus subsp. gallolyticus is a commensal of the human gastrointestinal tract and a pathogen of infective endocarditis and other biofilm-associated infections with exposed collagen. Therefore, this study focuses on the characterization of the biofilm formation and collagen adhesion of S. gallolyticus subsp. gallolyticus under different conditions. It has been observed that lysozyme triggers biofilm formation divergently in the analyzed S. gallolyticus subsp. gallolyticus strains. The transcriptome analysis was performed for two strains which form more biofilm in the presence of lysozyme. Lysozyme leads to higher expression of genes of transcription and translation, of the dlt operon (cell wall modification), of hydrogen peroxide resistance proteins and of two immunity proteins which could be involved in biofilm formation. Furthermore, the adhesion ability of 73 different S. gallolyticus subsp. gallolyticus strains to collagen type I and IV was analyzed. High adhesion ability was observed for the strain UCN 34, whereas the strain DSM 16831 adhered only marginally to collagen. The full genome microarray analysis revealed strain-dependent gene expression due to adhesion. The expression of genes of a transposon and a phage region in strain DSM 16831 were increased, which corresponds to lateral gene transfer. Adherence to collagen leads to a change in the expression of genes of nutrients uptake in the strain UCN 34.

2017-05-17 | GSE98953 | GEO

Geobacillus thermodenitrificans strain:BIM B-1973

Project description:Geobacillus thermodenitrificans strain:BIM B-1973 Genome sequencing and assembly

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Recombinant l-glutaminase obtained from <i>Geobacillus thermodenitrificans</i> DSM-465: characterization and <i>in silico</i> elucidation of conserved structural domains.

Project description:Glutaminase (GLS) is an enzyme essential for amino acid metabolism; in particular, it acts as a catalyst in glutaminolysis, a reaction exploited by the malignant cells to meet the nutrient requirements for their accelerated growth and proliferation. Via regulating the initial reaction of the glutaminolysis pathway, glutaminase offers an intriguing target for the development of anticancer drugs. In the present study, we produced a recombinant glutaminase from Geobacillus thermodenitrificans DSM-465 in E. coli. The enzyme was purified to electrophoretic homogeneity, with 40% recovery and 22.36 fold purity. It exhibited a molecular weight of 33 kDa, with an optimum pH and temperature of 9 and 70 °C, respectively. The K M value of the purified enzyme was 104 μM for l-glutamine. A 3D model was built for the enzyme using Swiss-Model and subjected to molecular docking with the substrate and potential inhibitors. Moreover, the subject enzyme was compared with the human kidney type GLS-K by ConSurf and TM-align servers for evolutionary conserved residues and structural domains. Despite having less than 40% amino acid identity, the superimposed monomers of both enzymes exhibited ∼94% structural identity. With a positional difference, the active site residues Ser65, Asn117, Glu162, Asn169, Tyr193, Tyr245, and Val263 found in the bacterial enzyme were also conserved in the human GLS-K. Molecular docking results have shown that CB-839 is the best inhibitor for GLS-GT and UPGL00004 is the best inhibitor for GLS-K, as designated by the binding free energy changes, i.e. ΔG -388.7 kJ mol-1 and ΔG -375 kJ mol-1, respectively. Moreover, six potential inhibitory molecules were ranked according to their binding free energy change values for both enzymes. The information can be used for the in vivo anticancer studies.

| S-EPMC9060542 | biostudies-literature

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