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Salmonella enterica subsp. enterica serovar Typhimurium

ABSTRACT: Dual RNA-seq – Comparative RNA-seq (in vitro medium shift experiment)

OTHER RELATED OMICS DATASETS IN: GSE67950GSE67759GSE67951GSE67757GSE67948GSE67952GSE67758

PROVIDER: PRJNA281341 | ENA |

REPOSITORIES: ENA

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Dataset's files

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			Action	DRS
	SRR2981440.fastq.gz	Fastqsanger.gz
	SRR2981450.fastq.gz	Fastqsanger.gz
	SRR2981441.fastq.gz	Fastqsanger.gz
	SRR2981451.fastq.gz	Fastqsanger.gz
	SRR2981442.fastq.gz	Fastqsanger.gz

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Salmonella enterica serovar Typhimurium strain 14028s transcriptome response to lettuce media

Project description:Summary: Salmonella enterica serovar Typhimurium strain 14028s transcriptome response to lettuce medium (LM) and lettuce root exudates (LX) to minimal medium (MM). Purpose: Salmonella mRNA profile, when grown in different media was compared to minimal medium to reveal environment specific transcriptional changes. Methods: mRNA profiles were generated using Illumina HiSeq in triplicates. The sequences were analysed using Bowtie2 followed by Cufflinks.

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Salmonella enterica serovar Typhimurium strain 14028s transcriptome response to tomato media

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RNA-seq data from mouse BMDMs infected with Salmonella enterica serovar Typhimurium

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Salmonella enterica serovar Typhimurium 4/74 transcriptomics using strand-specific RNA-seq

Project description:Bacterial transcription networks typically consist of hundreds of transcription factors and thousands of promoters. However, current attempts to map bacterial promoters have failed to report the true complexity of bacterial transcription. The differential RNA-seq (dRNA-seq) approaches only identified a subset of promoters because they involved few growth conditions. Here, we present a simplified approach for global promoter identification in bacteria, based upon the analysis of RNA-seq data from multiple environmental conditions. RNA was extracted from Salmonella enterica serovar Typhimurium (S. Typhimurium) grown in 22 different environmental conditions, which were devised to reflect the pathogenic lifestyle of S. Typhimurium. Individual RNA samples were combined into two pools for sequencing. In just two runs of strand-specific RNA-seq and dRNA-seq of the pooled sample we identified 3701 promoters (Pool sample). In further experiments, we found that individual in vitro conditions stimulate the expression of about 60% of the S. Typhimurium genome, whereas the suite of 22 conditions induced expression of 87% of S. Typhimurium genes. We discovered environmental conditions that induce many genes within Salmonella pathogenicity islands and identified 78 new sRNAs. In S. Typhimurium there is now experimental evidence for 280 sRNAs, and we classified them in terms of location and Hfq-binding.

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Project description:To elucidated the regulatory effect of DsrA on the oxidative resistance in Salmonella enterica serovar Typhimurium. RNA sample of wild-type and DsrA-deletion strain that grown in LB medium or H2O2 stress were extracted. Three biological replicates were carried out per sample. RNA sample was sequenced with Illumina HiSeq 4000 System. DESeq2 method was used to calculate the differentially expressed genes. qRT–PCR and gene mutation were used to validate RNA-seq result.

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Salmonella enterica serovar Typhimurium 4/74 transcriptomics using strand-specific RNA-seq

2013-12-18 | E-GEOD-49829 | biostudies-arrayexpress

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RNA-seq of wild-type and ∆metJ Salmonella enterica serovar Typhimurium (14028s)

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Aspartic peptide hydrolases in Salmonella enterica serovar typhimurium.

Project description:Two well-characterized enzymes in Salmonella enterica serovar Typhimurium and Escherichia coli are able to hydrolyze N-terminal aspartyl (Asp) dipeptides: peptidase B, a broad-specificity aminopeptidase, and peptidase E, an Asp-specific dipeptidase. A serovar Typhimurium strain lacking both of these enzymes, however, can still utilize most N-terminal Asp dipeptides as sources of amino acids, and extracts of such a strain contain additional enzymatic activities able to hydrolyze Asp dipeptides. Here we report two such activities from extracts of pepB pepE mutant strains of serovar Typhimurium identified by their ability to hydrolyze Asp-Leu. Although each of these activities hydrolyzes Asp-Leu at a measurable rate, the preferred substrates for both are N-terminal isoAsp peptides. One of the activities is a previously characterized isoAsp dipeptidase from E. coli, the product of the iadA gene. The other is the product of the serovar Typhimurium homolog of E. coli ybiK, a gene of previously unknown function. This gene product is a member of the N-terminal nucleophile structural family of amidohydrolases. Like most other members of this family, the mature enzyme is generated from a precursor protein by proteolytic cleavage and the active enzyme is a heterotetramer. Based on its ability to hydrolyze an N-terminal isoAsp tripeptide as well as isoAsp dipeptides, the enzyme appears to be an isoAsp aminopeptidase, and we propose that the gene encoding it be designated iaaA (isoAsp aminopeptidase). A strain lacking both IadA and IaaA in addition to peptidase B and peptidase E has been constructed. This strain utilizes Asp-Leu as a leucine source, and extracts of this strain contain at least one additional, as-yet-uncharacterized, peptidase able to cleave Asp dipeptides.

| S-EPMC95209 | biostudies-literature

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