ArticleJournal of bacteriology2010
Functional relationships between the AcrA hairpin tip region and the TolC aperture tip region for the formation of the bacterial tripartite efflux pump AcrAB-TolC.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- The Resistance-Nodulation-Division efflux pump EefABC is highly conserved within lineages ofMicrobial genomics · 2026Article
- Lpp positions peptidoglycan at the AcrA-TolC interface in the AcrAB-TolC multidrug efflux pump.Biophysical journal · 2021Article
- Insight into the AcrAB-TolC Complex Assembly Process Learned from Competition Studies.Antibiotics (Basel, Switzerland) · 2021Article
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- The coordinated action of RNase III and RNase G controls enolase expression in response to oxygen availability in Escherichia coli.Scientific reports · 2019Article
- Structures of the wild-type MexAB-OprM tripartite pump reveal its complex formation and drug efflux mechanism.Nature communications · 2019Article
- Recent paradigm shift in the assembly of bacterial tripartite efflux pumps and the type I secretion system.Journal of microbiology (Seoul, Korea) · 2019Review
- ATP-Binding Cassette Transporter VcaM from Vibrio cholerae is Dependent on the Outer Membrane Factor Family for Its Function.International journal of molecular sciences · 2018Article
- Opening the Channel: the Two Functional Interfaces of Pseudomonas aeruginosa OpmH with the Triclosan Efflux Pump TriABC.Journal of bacteriology · 2016Article
- Non-equivalent roles of two periplasmic subunits in the function and assembly of triclosan pump TriABC from Pseudomonas aeruginosa.Molecular microbiology · 2015Article
- Molecular architecture of the bacterial tripartite multidrug efflux pump focusing on the adaptor bridging model.Journal of microbiology (Seoul, Korea) · 2015Review
- Functional analysis of Vibrio vulnificus RND efflux pumps homologous to Vibrio cholerae VexAB and VexCD, and to Escherichia coli AcrAB.Journal of microbiology (Seoul, Korea) · 2015Article
- The ins and outs of RND efflux pumps in Escherichia coli.Frontiers in microbiology · 2015Review
- Architecture and roles of periplasmic adaptor proteins in tripartite efflux assemblies.Frontiers in microbiology · 2015Review
- Structure of the tripartite multidrug efflux pump AcrAB-TolC suggests an alternative assembly mode.Molecules and cells · 2015Article
- Functional analysis of TolC homologs in Vibrio vulnificus.Current microbiology · 2014Article
- Genetic assessment of the role of AcrB β-hairpins in the assembly of the TolC-AcrAB multidrug efflux pump of Escherichia coli.Molecular microbiology · 2014Article
- Interaction between the α-barrel tip of Vibrio vulnificus TolC homologs and AcrA implies the adapter bridging model.Journal of microbiology (Seoul, Korea) · 2014Article
- Interaction mediated by the putative tip regions of MdsA and MdsC in the formation of a Salmonella-specific tripartite efflux pump.PloS one · 2014Article
- Molecular basis of active copper resistance mechanisms in Gram-negative bacteria.Cell biology and toxicology · 2013Review
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Authors and funding
7 authors.
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Abstract
Tripartite efflux pumps found in Gram-negative bacteria are involved in antibiotic resistance and toxic-protein secretion. In this study, we show, using site-directed mutational analyses, that the conserved residues located in the tip region of the alpha-hairpin of the membrane fusion protein (MFP) AcrA play an essential role in the action of the tripartite efflux pump AcrAB-TolC. In addition, we provide in vivo functional data showing that both the length and the amino acid sequence of the alpha-hairpin of AcrA can be flexible for the formation of a functional AcrAB-TolC pump. Genetic-complementation experiments further indicated functional interrelationships between the AcrA hairpin tip region and the TolC aperture tip region. Our findings may offer a molecular basis for understanding the multidrug resistance of pathogenic bacteria.
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