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Open AccessJournal ArticleDOI

Cross-Linked Complex between Oligomeric Periplasmic Lipoprotein AcrA and the Inner-Membrane-Associated Multidrug Efflux Pump AcrB from Escherichia coli

Helen I. Zgurskaya, +1 more
- 01 Aug 2000 - 
- Vol. 182, Iss: 15, pp 4264-4267
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TLDR
It is shown that AcrA protein forms oligomers, most probably trimers, in this oligomeric form, and interacts specifically with AcrB transporter independently of substrate and TolC.
Abstract
In Escherichia coli, the intrinsic levels of resistance to multiple antimicrobial agents are produced through expression of the three-component multidrug efflux system AcrAB-TolC. AcrB is a proton-motive-force-dependent transporter located in the inner membrane, and AcrA and TolC are accessory proteins located in the periplasm and the outer membrane, respectively. In this study, these three proteins were expressed separately, and the interactions between them were analyzed by chemical cross-linking in intact cells. We show that AcrA protein forms oligomers, most probably trimers. In this oligomeric form, AcrA interacts specifically with AcrB transporter independently of substrate and TolC.

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Molecular Basis of Bacterial Outer Membrane Permeability Revisited

TL;DR: This review summarizes the development in the field since the previous review and begins to understand how this bilayer of the outer membrane can retard the entry of lipophilic compounds, owing to increasing knowledge about the chemistry of lipopolysaccharide from diverse organisms and the way in which lipopoly Saccharide structure is modified by environmental conditions.
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Efflux‐mediated heavy metal resistance in prokaryotes

TL;DR: The complement of efflux systems of 63 sequenced prokaryotes was compared with that of the heavy metal resistant bacterium Ralstonia metallidurans and showed that heavy metal resistance is the result of multiple layers of resistance systems with overlapping substrate specificities, but unique functions.
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Multidrug Resistance in Bacteria

TL;DR: This review discusses the current knowledge on the molecular mechanisms involved in both types of resistance in bacteria.
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Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems

TL;DR: The availability of an increasing number of high-resolution structures has provided a valuable framework for interpretation of recent studies, and realistic models have been proposed to explain how these fascinating molecular machines use complex dynamic processes to fulfill their numerous biological functions.
Journal ArticleDOI

Efflux-Mediated Drug Resistance in Bacteria

TL;DR: Fluoroquinolones and β-lactams of the latest generations are likely to select for overproduction mutants of these pumps and make the bacteria resistant in one step to practically all classes of antibacterial agents.
References
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Journal ArticleDOI

Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form.

TL;DR: The percentage recovery of functional activity depended on the respective protein complex studied and was zero for some complexes, but almost quantitative for others, and the recovery of all respiratory chain complexes was almost quantitative.
Journal ArticleDOI

AcrAB efflux pump plays a major role in the antibiotic resistance phenotype of Escherichia coli multiple-antibiotic-resistance (Mar) mutants.

TL;DR: The AcrAB system is identified as the major pump responsible for making the Mar mutants resistant to many agents, including tetracycline, chloramphenicol, ampicillin, nalidixic acid, and rifampin.
Journal ArticleDOI

Genes acrA and acrB encode a stress‐induced efflux system of Escherichia coli

TL;DR: The results suggest that one major physiological function of AcrAB is to protect E. coli against cephalothin and other hydrophobic inhibitors and mar (multiple‐antibiotic‐resistant) mutants.
Journal ArticleDOI

Molecular cloning and characterization of acrA and acrE genes of Escherichia coli.

TL;DR: The DNA fragment containing the acrA locus of the Escherichia coli chromosome has been cloned by using a complementation test and nucleotide sequence indicates the presence of two open reading frames (ORFs) that encodes a 397-residue lipoprotein with a 24-amino-acid signal peptide at its N terminus.
Journal ArticleDOI

Evidence that TolC is required for functioning of the Mar/AcrAB efflux pump of Escherichia coli.

TL;DR: A study examining the influence of TolC on AcrA, AcrR, and MarR1 mutants indicates that functional TolC is required for the operation of the AcrAB efflux system and for the expression of the Mar phenotype.
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