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Staphylococcus aureus subsp. aureus NCTC 8325

ABSTRACT: Sequence selectivity of macrolide-induced translational regulation

PROVIDER: PRJNA245830 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR1265840.fastq.gz	Fastqsanger.gz
	SRR1265841.fastq.gz	Fastqsanger.gz
	SRR1265842.fastq.gz	Fastqsanger.gz
	SRR1265843.fastq.gz	Fastqsanger.gz
	SRR1265834.fastq.gz	Fastqsanger.gz

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Similar Datasets

Predictive characterization of hypothetical proteins in Staphylococcus aureus NCTC 8325.

Project description:Staphylococcus aureus is one of the most common hospital acquired infections. It colonizes immunocompromised patients and with the number of antibiotic resistant strains increasing, medicine needs new treatment options. Understanding more about the proteins this organism uses would further this goal. Hypothetical proteins are sequences thought to encode a functional protein but for which little to no evidence of that function exists. About half of the genomic proteins in reference strain S. aureus NCTC 8325 are hypothetical. Since annotation of these proteins can lead to new therapeutic targets, a high demand to characterize hypothetical proteins is present. This work examines 35 hypothetical proteins from the chromosome of S. aureus NCTC 8325. Examination includes physiochemical characterization; sequence homology; structural homology; domain recognition; structure modeling; active site depiction; predicted protein-protein interactions; protein-chemical interactions; protein localization; protein stability; and protein solubility. The examination revealed some hypothetical proteins related to virulent domains and protein-protein interactions including superoxide dismutase, O-antigen, bacterial ferric iron reductase and siderophore synthesis. Yet other hypothetical proteins appear to be metabolic or transport proteins including ABC transporters, major facilitator superfamily, S-adenosylmethionine decarboxylase, and GTPases. Progress evaluating some hypothetical proteins, particularly the smaller ones, was incomplete due to limited homology and structural information in public repositories. These data characterizing hypothetical proteins will contribute to the scientific understanding of S. aureus by identifying potential drug targets and aiding in future drug discovery.

| S-EPMC5267966 | biostudies-literature

Staphylococcus aureus subsp. aureus NCTC 8325

Project description:The nucleoid occlusion factor Noc controls DNA replication initiation in Staphylococcus aureus [WGS-Seq]

| PRJNA393027 | ENA

Staphylococcus aureus subsp. aureus NCTC 8325

Project description:Typical laboratory strain

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Staphylococcus aureus subsp. aureus NCTC 8325

Project description:Transcriptome analysis of the eukaryotic-type ser/thr kinase PknB in Staphylococcus aureus

| PRJNA116575 | ENA

Staphylococcus aureus subsp. aureus NCTC 8325

Project description:Staphylococcus aureus subsp. aureus NCTC 8325 Raw sequence reads

| PRJNA279231 | ENA

Staphylococcus aureus subsp. aureus NCTC 8325

Project description:The nucleoid occlusion factor Noc controls DNA replication initiation in Staphylococcus aureus [Tn-seq]

| PRJNA393999 | ENA

Staphylococcus aureus subsp. aureus NCTC 8325

Project description:Effect of different Two-component systems system deletion in S. aureus NCTC8325

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Staphylococcus aureus subsp. aureus NCTC 8325

Project description:Effect of SAOUHSC_02810 deletion in S. aureus NCTC8325

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Staphylococcus aureus subsp. aureus NCTC 8325

Project description:Effect of TetR family regulator SAOUHSC_02897 deletion in S. aureus NCTC8325

| PRJNA231982 | ENA

Cloning, overexpression, purification, crystallization and preliminary X-ray diffraction analysis of an atypical two-cysteine peroxiredoxin (SAOUHSC_01822) from Staphylococcus aureus NCTC 8325.

Project description:An atypical two-cysteine peroxidase, SAOUHSC_01822, from the virulent Staphylococcus aureus strain NCTC 8325 plays a major role in the response of the bacterium to oxidative stress. The protein was cloned, expressed, purified to homogeneity and crystallized. The protein was crystallized from 2 M ammonium sulfate, 0.1 M Na HEPES pH 7, 2%(v/v) PEG 400. A complete diffraction data set was collected to 2.3 angstrom resolution using a Rigaku MicroMax HF007 Cu K alpha X-ray generator and a Rigaku R-AXIS IV(+)(+) detector. The crystals belonged to space group P2(1), with unit-cell parameters a = 43.50, b = 149.35, c = 73.73 angstrom, beta = 104.4 degrees, and contained four molecules in the asymmetric unit.

| S-EPMC2777037 | biostudies-literature

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