ArticleJournal of bacteriology2009
The C-terminal domain of AcrA is essential for the assembly and function of the multidrug efflux pump AcrAB-TolC.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 60 citations in OpenAlex.
- Overexpression of the Multidrug Efflux Pump AcrAB-TolC in Escherichia coli for In Situ Cryo-ET Study.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Structures and Efflux Mechanisms of the AcrAB-TolC Pump.Sub-cellular biochemistry · 2024Article
- Conformational restriction shapes the inhibition of a multidrug efflux adaptor protein.Nature communications · 2023Article
- A role for the periplasmic adaptor protein AcrA in vetting substrate access to the RND efflux transporter AcrB.Scientific reports · 2022Article
- In situ structure of the AcrAB-TolC efflux pump at subnanometer resolution.Structure (London, England : 1993) · 2022Article
- Mechanistic Duality of Bacterial Efflux Substrates and Inhibitors: Example of Simple Substituted Cinnamoyl and Naphthyl Amides.ACS infectious diseases · 2021Article
- Structural and Functional Diversity of Resistance-Nodulation-Cell Division Transporters.Chemical reviews · 2021Review
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- Multidrug Efflux Pumps and the Two-Faced Janus of Substrates and Inhibitors.Accounts of chemical research · 2021Article
- Periplasmic Targets for the Development of Effective Antimicrobials against Gram-Negative Bacteria.ACS infectious diseases · 2020Review
- Identification of binding residues between periplasmic adapter protein (PAP) and RND efflux pumps explains PAP-pump promiscuity and roles in antimicrobial resistance.PLoS pathogens · 2019Article
- Conformational Dynamics of AcrA Govern Multidrug Efflux Pump Assembly.ACS infectious diseases · 2019Article
- Identification of Binding Sites for Efflux Pump Inhibitors of the AcrAB-TolC Component AcrA.Biophysical journal · 2019Article
- Identification ofMicrobiology insights · 2019Article
- Small Molecule Condensin Inhibitors.ACS infectious diseases · 2018Article
- Novel RpoS-Dependent Mechanisms Strengthen the Envelope Permeability Barrier during Stationary Phase.Journal of bacteriology · 2017Article
- Reviving Antibiotics: Efflux Pump Inhibitors That Interact with AcrA, a Membrane Fusion Protein of the AcrAB-TolC Multidrug Efflux Pump.ACS infectious diseases · 2017Article
- AcrB-AcrA Fusion Proteins That Act as Multidrug Efflux Transporters.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
- Mechanism of coupling drug transport reactions located in two different membranes.Frontiers in microbiology · 2015Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Periplasmic membrane fusion proteins (MFPs) are essential components of multidrug efflux pumps and type I protein secretion systems of gram-negative bacteria. Located in the periplasm, MFPs function by creating a physical link between inner membrane transporters and outer membrane channels. The most conserved sequence of MFPs is located in their distal C-terminal domain. However, neither the structure nor the function of this domain is known. In this study, we investigated the structural and functional role of the C-terminal domain of Escherichia coli AcrA, a periplasmic component of the multidrug efflux pump AcrAB-TolC. Using trypsin proteolysis, we identified the proteolytically labile sites in the C-terminal domain (amino acid residues 315 to 397) of AcrA in vitro. We next used these sites as a map to evaluate the structural integrity of this domain of AcrA inside the periplasm. We found that the C-terminal domain of AcrA is protected from trypsin when the tripartite efflux pump AcrAB-TolC is assembled. In contrast, this domain remains proteolytically labile in cells producing only one of the AcrB or TolC components of the complex. Site-directed mutagenesis of 12 highly conserved amino acid residues of the C-terminal domain of AcrA showed that a single G363C substitution dramatically impairs the multidrug efflux activity of AcrAB-TolC. The G363C mutant interacts with both AcrB and TolC but fails to properly assemble into a functional complex. We conclude that the C-terminal domain of AcrA plays an important role in the assembly and function of AcrAB-TolC efflux pump.
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