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A Bacillus anthracis RNA binding protein post-transcriptionally regulates two component signaling through RNA turnover

ABSTRACT: A Bacillus anthracis RNA binding protein post-transcriptionally regulates two component signaling through RNA turnover

PROVIDER: PRJNA795436 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR17483800_1.fastq.gz	Fastqsanger.gz
	SRR17483800_2.fastq.gz	Fastqsanger.gz
	SRR17483801_1.fastq.gz	Fastqsanger.gz
	SRR17483801_2.fastq.gz	Fastqsanger.gz
	SRR17483802_1.fastq.gz	Fastqsanger.gz

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A Bacillus anthracis RNA binding protein post-transcriptionally regulates two component signaling through RNA turnover [RNA-Seq]

Project description:A Bacillus anthracis RNA binding protein post-transcriptionally regulates two component signaling through RNA turnover [RNA-Seq]

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A Bacillus anthracis RNA binding protein post-transcriptionally regulates two component signaling through RNA turnover [RIP-Seq]

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A Bacillus anthracis RNA binding protein post-transcriptionally regulates two component signaling through RNA turnover [RNA-Seq]

Project description:To uncover the effects of KrrA regulation on gene transcription and define the bacterial response imposed by this regulation, a transcriptomic study was carried out in which Bacillus anthracis krrA was compared to WT in two growth conditions: LB in the presence or absence of ‘205.

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A Bacillus anthracis RNA binding protein post-transcriptionally regulates two component signaling through RNA turnover [RIP-Seq]

Project description:Formaldehyde cross-linking RNA immunoprecipitation coupled with illumina sequencing (fRIP-seq) was performed to pinpoint the direct RNA targets of KrrA using a FLAG-tagged KrrA construct that is driven by a constitutive promoter Plgt (pOS1.PlgtkrrA-FLAG).

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A Bacillus anthracis RNA binding protein post-transcriptionally regulates two component signaling through RNA turnover

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Transcriptional response of Bacillus anthracis to targocil and role of EdsRS in regulating this response

Project description:Bacillus anthracis is a spore-forming bacterium that causes devastating infections and has been used as a bioterror agent. This pathogen can survive hostile environments through the signaling activity of two-component systems, which couple environmental sensing with transcriptional activation to initiate a coordinated response to stress. In this work, we describe the identification of a two-component system, EdsRS, which mediates the B. anthracis response to the antimicrobial compound targocil. Targocil is a cell envelope-targeting compound that is toxic to B. anthracis at high concentrations. Exposure to targocil causes damage to the cellular barrier and activates EdsRS to induce expression of a previously uncharacterized cardiolipin synthase, which we have named ClsT. Both EdsRS and ClsT are required for protection against targocil-dependent damage. Induction of clsT by EdsRS during targocil treatment results in an increase in cardiolipin levels, which protects B. anthracis from envelope damage. Together, these results reveal a two-component system signaling response to an envelope-targeting antimicrobial induces production of a phospholipid associated with stabilization of the membrane. Cardiolipin is then used to repair envelope damage and promote B. anthracis viability.

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Project description:The spore forming pathogen Bacillus anthracis is the etiologic agent of anthrax in humans and animals. It cycles through infected hosts as vegetative cells and is eventually introduced into the environment where it generates an endospore resistant to many harsh conditions. The endospores are subsequently ingested by the next host to begin the next cycle. Outbreaks of anthrax occur regularly worldwide in wildlife and livestock, and the potential for human infection exists whenever humans encounter infected animals. It is also possible to encounter intentional releases of anthrax spores, as was the case in October 2001. Consequently, it is important to be able to rapidly establish the provenance of infectious strains of B. anthracis. Here, we compare protein expression in seven low-passage wild isolates and four laboratory strains of B. anthracis grown under identical conditions using LC-MS/MS proteomic analysis. Of the 1,023 total identified proteins, 96 had significant abundance differences between wild and laboratory strains. Of those, 28 proteins directly related to sporulation were upregulated in wild isolates, with expression driven by Spo0A, CodY, and AbrB/ScoC. In addition, we observed evidence of changes in cell division and fatty acid biosynthesis between the two classes of strains, despite being grown under identical experimental conditions. These results suggest wild B. anthracis cells are more highly tuned to sporulate than their laboratory cousins, and this difference should be exploited as a method to differentiate between laboratory adapted cultures and low passage wild strains isolated during an anthrax outbreak. This knowledge should distinguish between intentional releases and exposure to strains in nature providing a basis for the type of response by public health officials and investigators.

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