ArticleJournal of bacteriology2008
Fitting periplasmic membrane fusion proteins to inner membrane transporters: mutations that enable Escherichia coli AcrA to function with Pseudomonas aeruginosa MexB.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
34 citing papers in PubMed, 68 citations in OpenAlex.
- Computer Simulations of Multidrug Efflux Pumps of the Resistance-Nodulation-Cell Division Superfamily.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The Art of War withAntibiotics (Basel, Switzerland) · 2023Review
- Molecular Determinants for OMF Selectivity in Tripartite RND Multidrug Efflux Systems.Antibiotics (Basel, Switzerland) · 2022Article
- Common recognition topology of mex transporters ofFrontiers in pharmacology · 2022Article
- A Model for Allosteric Communication in Drug Transport by the AcrAB-TolC Tripartite Efflux Pump.Antibiotics (Basel, Switzerland) · 2022Article
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- Article
- 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
- Structures of the wild-type MexAB-OprM tripartite pump reveal its complex formation and drug efflux mechanism.Nature communications · 2019Article
- Dynamics of Intact MexAB-OprM Efflux Pump: Focusing on the MexA-OprM Interface.Scientific reports · 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
- Tripartite assembly of RND multidrug efflux pumps.Nature communications · 2016Article
- RND-type drug efflux pumps from Gram-negative bacteria: molecular mechanism and inhibition.Frontiers in microbiology · 2015Review
- Interaction of antibacterial compounds with RND efflux pumps in Pseudomonas aeruginosa.Frontiers in microbiology · 2015Review
- Architecture and roles of periplasmic adaptor proteins in tripartite efflux assemblies.Frontiers in microbiology · 2015Review
- Mechanism of coupling drug transport reactions located in two different membranes.Frontiers in microbiology · 2015Review
- Phytochemicals increase the antibacterial activity of antibiotics by acting on a drug efflux pump.MicrobiologyOpen · 2014Article
- Molecular Dynamics Computer Simulations of Multidrug RND Efflux Pumps.Computational and structural biotechnology journal · 2013Review
- Evolution and diversity of periplasmic proteins involved in copper homeostasis in gamma proteobacteria.BMC microbiology · 2012Article
- Evolution combined with genomic study elucidates genetic bases of isobutanol tolerance in Escherichia coli.Microbial cell factories · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
AcrAB-TolC from Escherichia coli is a multidrug efflux complex capable of transenvelope transport. In this complex, AcrA is a periplasmic membrane fusion protein that establishes a functional connection between the inner membrane transporter AcrB of the RND superfamily and the outer membrane channel TolC. To gain insight into the mechanism of the functional association between components of this complex, we replaced AcrB with its close homolog MexB from Pseudomonas aeruginosa. Surprisingly, we found that AcrA is promiscuous and can form a partially functional complex with MexB and TolC. The chimeric AcrA-MexB-TolC complex protected cells from sodium dodecyl sulfate, novobiocin, and ethidium bromide but failed with other known substrates of MexB. We next identified single and double mutations in AcrA and MexB that enabled the complete functional fit between AcrA, MexB, and TolC. Mutations in either the alpha-helical hairpin of AcrA making contact with TolC or the beta-barrel domain lying on MexB improved the functional alignment between components of the complex. Our results suggest that three components of multidrug efflux pumps do not associate in an "all-or-nothing" fashion but accommodate a certain degree of flexibility. This flexibility in the association between components affects the transport efficiency of RND pumps.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.