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Escherichia coli K-12 BW25113 Tripartite Efflux (TE) mutant

ABSTRACT: The inactivation of tolC sensitizes Escherichia coli to perturbations in lipopolysaccharide transport

PROVIDER: PRJNA990483 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR25192920_1.fastq.gz	Fastqsanger.gz
	SRR25192920_2.fastq.gz	Fastqsanger.gz
	SRR25192921_1.fastq.gz	Fastqsanger.gz
	SRR25192921_2.fastq.gz	Fastqsanger.gz
	SRR25687296_1.fastq.gz	Fastqsanger.gz

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Efflux of gepotidacin and zoliflodacin in E. coli

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A TetR-family regulator of an RND efflux system that directs artemisinin resistance in Vibrio cholerae

Project description:Artemisinin (ARS) displayed bactericidal activity against Vibrio cholerae. To assess the mechanistic details of its antibacterial action, we have isolated V. cholerae mutants with enhanced ARS resistance and identified a gene (VCA0767), whose loss-of-function resulted in the ARS resistance phenotypes. This gene (atrR) encodes a TetR family transcriptional regulator, and its deletion mutant displayed the reduction in ARS-induced ROS formation and DNA damage. Transcriptomic analysis revealed that the genes encoding an RND efflux pump operon (vexRAB) and the outer membrane component (tolC) were highly upregulated in the artR mutant, suggesting that AtrR might act as a negative regulator of this operon and tolC. Gene deletion of vexR, vexB or tolC abrogated the ARS resistance of the atrR mutant and, more importantly, the ectopic expression of VexAB-TolC was sufficient for the ARS resistance, indicating that the increased expression of the VexAB-TolC efflux system is necessary and sufficient for the ARS resistance of the atrR mutant. The cytoplasmic accumulation of ARS was compromised in the vexBtolC mutant, suggesting that the VexAB-TolC might be the primary efflux system exporting ARS to reduce its toxicity inside of the bacterial cells. The atrR mutant displayed resistance to erythromycin as well in a VexR-dependent manner. This result suggests that AtrR may act as a global regulator responsible for preventing intracellular accumulation of toxic chemicals by enhancing the RND efflux system.

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Assembly and transport mechanism of tripartite drug efflux systems.

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Real-time visualization of drug resistance acquisition by horizontal gene transfer reveals a new role for AcrAB-TolC multidrug efflux pump

Project description:In our study, we obtained evidence showing that, in the presence of tetracycline, AcrAB-TolC multidrug efflux pump was required for production of protein encoded by a conjugative plasmid acquired by bacterial conjugation. We then address the role of AcrAB-TolC multidrug efflux pump on the level of protein synthesis activity in the presence of tetracycline, which inhibits protein translation by targeting ribosomal 16S rRNA and competing with binding of the anticodon-stem loop of an A-site tRNA. We used a quantitative TMT-nanoLC-mass spectrometry approach to obtained the protein relative abundance ratio before and after incubation with tetracycline, and so in wild-type(MG1655, K12) and AcrAB-TolC mutant strains (ΔacrA, ΔacrB and ΔtolC).

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A genetic platform to investigate the functions of bacterial drug efflux pumps

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