ArticleJournal of bacteriology2016
AcrB-AcrA Fusion Proteins That Act as Multidrug Efflux Transporters.
Article in Journal of bacteriology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Genomic insights into Serratia bockelmanii strain 201: unlocking its potential for plant growth promotion and salt stress tolerance.BMC microbiology · 2026Article
- Molecular and Drug Resistance Characteristics ofMicroorganisms · 2025Article
- EvgS/EvgA, the unorthodox two-component system regulating bacterial multiple resistance.Applied and environmental microbiology · 2023Review
- Conformational restriction shapes the inhibition of a multidrug efflux adaptor protein.Nature communications · 2023Article
- Acetylome and Succinylome Profiling ofAntibiotics (Basel, Switzerland) · 2022Article
- Molecular Determinants for OMF Selectivity in Tripartite RND Multidrug Efflux Systems.Antibiotics (Basel, Switzerland) · 2022Article
- The effects of magainin 2-derived and rationally designed antimicrobial peptides on Mycoplasma pneumoniae.PloS one · 2022Article
- Ever-Adapting RND Efflux Pumps in Gram-Negative Multidrug-Resistant Pathogens: A Race against Time.Antibiotics (Basel, Switzerland) · 2021Review
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- Mutations in the TolC Periplasmic Domain Affect Substrate Specificity of the AcrAB-TolC Pump.Frontiers in molecular biosciences · 2020Article
- Pan-genome diversification and recombination in Cronobacter sakazakii, an opportunistic pathogen in neonates, and insights to its xerotolerant lifestyle.BMC microbiology · 2019Article
- Conformational Dynamics of AcrA Govern Multidrug Efflux Pump Assembly.ACS infectious diseases · 2019Article
- Multiomics Assessment of Gene Expression in a Clinical Strain of CTX-M-15-Producing ST131Frontiers in microbiology · 2019Article
- Genome sequencing and assessment of plant growth-promoting properties of a Serratia marcescens strain isolated from vermicompost.BMC genomics · 2018Article
- Amino Acid Substitution in the Major Multidrug Efflux Transporter Protein AcrB Contributes to Low Susceptibility to Azithromycin in Haemophilus influenzae.Antimicrobial agents and chemotherapy · 2017Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
unlabelledThe AcrAB-TolC system in Escherichia coli is an intrinsic RND-type multidrug efflux transporter that functions as a tripartite complex of the inner membrane transporter AcrB, the outer membrane channel TolC, and the adaptor protein AcrA. Although the crystal structures of each component of this system have been elucidated, the crystal structure of the whole complex has not been solved. The available crystal structures have shown that AcrB and TolC function as trimers, but the number of AcrA molecules in the complex is now under debate. Disulfide chemical cross-linking experiments have indicated that the stoichiometry of AcrB-AcrA-TolC is 1:1:1; on the other hand, recent cryo-electron microscopy images of AcrAB-TolC suggested a 1:2:1 stoichiometry. In this study, we constructed 1:1-fixed AcrB-AcrA fusion proteins using various linkers. Surprisingly, all the 1:1-fixed linker proteins showed drug export activity under both acrAB-deficient conditions and acrAB acrEF double-pump-knockout conditions regardless of the lengths of the linkers. Finally, we optimized a shorter linker lacking the conformational freedom imparted by the AcrB C terminus. These results suggest that a complex with equal amounts of AcrA and AcrB is sufficient for drug export function. IMPORTANCE: The structure and stoichiometry of the RND-type multidrug exporter AcrB-AcrA-TolC complex are still under debate. Recently, electron microscopic images of the AcrB-AcrA-TolC complex have been reported, suggesting a 1:2:1 stoichiometry. However, we report here that the AcrB-AcrA 1:1 fusion protein is active for drug export under acrAB-deficient conditions and also under acrAB acrEF double-deficient conditions, which eliminate the aid of free AcrA and its close homolog AcrE, indicating that the AcrB-AcrA 1:1 stoichiometry is enough for drug export function. In addition, the AcrB-AcrA fusion protein can function without the aid of free AcrA. We believe that these results are very important for considering the structure and mechanism of AcrAB-TolC-mediated multidrug export.
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