ArticleScientific reports2016
Substrate-dependent dynamics of the multidrug efflux transporter AcrB of Escherichia coli.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Genome-Scale Engineering Importing Property of Escherichia coli for Improving Production of 3-Hydroxypropionic Acid.Microbial biotechnology · 2026Article
- Targeted isolation of TolC-dependent phages reveals dual strategies for combating multidrug-resistant avianFrontiers in microbiology · 2026Article
- RND/HAE-1 members in the Pseudomonadota phylum: exploring multidrug resistance.Biophysical reviews · 2025Review
- Transporter excess and clustering facilitate adaptor protein shuttling for bacterial efflux.Cell reports. Physical science · 2025Article
- Highly inclined light sheet allows volumetric super-resolution imaging of efflux pumps distribution in bacterial biofilms.Scientific reports · 2024Article
- A palette of fluorophores that are differentially accumulated by wild-type and mutant strains ofMicrobiology (Reading, England) · 2021Article
- Article
- Loss of the Periplasmic Chaperone Skp and Mutations in the Efflux Pump AcrAB-TolC Play a Role in Acquired Resistance to Antimicrobial Peptides inFrontiers in microbiology · 2020Article
- Article
- Involvement of multiple influx and efflux transporters in the accumulation of cationic fluorescent dyes by Escherichia coli.BMC microbiology · 2019Article
- Structures of the wild-type MexAB-OprM tripartite pump reveal its complex formation and drug efflux mechanism.Nature communications · 2019Article
- Mapping the Dynamic Functions and Structural Features of AcrB Efflux Pump Transporter Using Accelerated Molecular Dynamics Simulations.Scientific reports · 2018Article
- Thermal proteome profiling in bacteria: probing protein stateMolecular systems biology · 2018Article
- A photo-cross-linking approach to monitor folding and assembly of newly synthesized proteins in a living cell.The Journal of biological chemistry · 2018Article
- Adaptor protein mediates dynamic pump assembly for bacterial metal efflux.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The resistance-nodulation-cell division (RND)-type xenobiotic efflux system plays a major role in the multidrug resistance of gram-negative bacteria. The only constitutively expressed RND system of Escherichia coli consists of the inner membrane transporter AcrB, the membrane fusion protein AcrA, and the outer membrane channel TolC. The latter two components are shared with another RND-type transporter AcrD, whose expression is induced by environmental stimuli. Here, we demonstrate how RND-type ternary complexes, which span two membranes and the cell wall, form in vivo. Total internal reflection fluorescence (TIRF) microscopy revealed that most fluorescent foci formed by AcrB fused to green fluorescent protein (GFP) were stationary in the presence of TolC but showed lateral displacements when tolC was deleted. The fraction of stationary AcrB-GFP foci decreased with increasing levels of AcrD. We propose that the AcrB-containing complex becomes unstable upon the induction of AcrD, which presumably replaces AcrB, a process we call "transporter exchange." This instability is suppressed by AcrB-specific substrates, suggesting that the ternary complex is stabilised when it is in action. These results suggest that the assembly of the RND-type efflux system is dynamically regulated in response to external stimuli, shedding new light on the adaptive antibiotic resistance of bacteria.
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