Proton-dependent multidrug efflux systems.

  title={Proton-dependent multidrug efflux systems.},
  author={Ian T. Paulsen and M. H. Brown and Ronald A. Skurray},
  journal={Microbiological reviews},
  volume={60 4},
Multidrug efflux systems display the ability to transport a variety of structurally unrelated drugs from a cell and consequently are capable of conferring resistance to a diverse range of chemotherapeutic agents. This review examines multidrug efflux systems which use the proton motive force to drive drug transport. These proteins are likely to operate as multidrug/proton antiporters and have been identified in both prokaryotes and eukaryotes. Such proton-dependent multidrug efflux proteins… 

The Multidrug Transporters Belonging to Major Facilitator Superfamily (MFS) in Mycobacterium tuberculosis

The inventory of the drug transporters subfamily, included in the major facilitator superfamily (MFS), encoded by the complete genome of Mycobacterium tuberculosis, revealed 16 open reading frames encoding putative drug efflux pumps belonging to MFS, and it is demonstrated that two of them function asDrug efflux proteins.

Multidrug efflux systems in Gram-negative bacteria

Genome analysis has confirmed the broad distribution of multidrug efflux systems in Gramnegative as well as in Gram-positive bacteria, and found that Escherichia coli and Pseudomonas aeruginosa have most of the hitherto identified and studiedMultidrug Efflux systems.

Antibiotic efflux pumps.

Distribution and Physiology of ABC-Type Transporters Contributing to Multidrug Resistance in Bacteria

This review focuses on recent advances in the analysis of ABC-type MDR transporters in bacteria, which can help to understand their molecular mode of action and may eventually lead to the development of new strategies to counteract their actions, thereby increasing the effectiveness of drug-based therapies.

Structure of the multidrug resistance efflux transporter EmrE from Escherichia coli.

  • Che MaG. Chang
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 2004
The structure of EmrE, a tetramer comprised of two conformational heterodimers related by a pseudo two-fold symmetry axis perpendicular to the cell membrane, can serve as an ideal model for understanding the general structural basis of proton:drug antiport for other drug efflux systems.

MFS transporters of Candida species and their role in clinical drug resistance.

This review focuses on the recent developments in MFS of Candida and highlights their role in drug transport by using the example of the relatively well characterized promiscuous Mdr1 efflux pump of the pathogenic yeast C. albicans.

[Active efflux as the multidrug resistance mechanism].

Investigations into efflux pumps and their substrate profiles and regulatory mechanisms have led to the discovery of new therapeutics and pump inhibitors that could potentially become alternative and effective antimicrobial drugs.

Multidrug transporters in prokaryotic and eukaryotic cells: physiological functions and transport mechanisms

This review will summarize important new insights into the role that P-glycoprotein and its bacterial homologue LmrA in particular, play in the physiology of the cell and the molecular basis of drug transport by these proteins will be discussed.



Proton motive force-driven and ATP-dependent drug extrusion systems in multidrug-resistant Lactococcus lactis

The partial inhibition of ethidium efflux by ortho-vanadate and nigericin in the DauR and RhoR strains suggest that a proton motive force-dependent and an ATP-dependent system are expressed simultaneously, the first report of an ATP -dependent transport system in prokaryotes which confers multidrug resistance to the organism.

Efflux-mediated multidrug resistance in Bacillus subtilis: similarities and dissimilarities with the mammalian system.

The results show that the transport of structurally unrelated molecules can be mediated by members of different families of membrane transporters.

The Lactococcal lmrP Gene Encodes a Proton Motive Force- dependent Drug Transporter (*)

Results indicate that in the absence of the functional drug-proton antiporter LmrP, L. lactis is able to overexpress another, ATP-dependent, drug extrusion system, and substantiate earlier studies on the isolation and characterization of drug-resistant mutants of L. latis.

A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of gram-negative bacteria

The phylogenies of these proteins correlate with the types of transport systems with which they function as well as with the natures of the substrates transported, providing circumstantial evidence as to how they may allow localized fusion of the two gram-negative bacterial cell membranes.

Is the multidrug transporter a flippase?

The multidrug resistance (mdr1) gene product functions as an ATP channel.

The data presented here show that cells with increased levels of the P-glycoprotein release ATP to the medium in proportion to the concentration of the protein in their plasma membrane, and measurements of whole-cell and single-channel currents with patch-clamp electrodes indicate that this protein serves as an ATP-conducting channel in the plasma membrane.

Multidrug resistance pumps in bacteria: variations on a theme.

  • K. Lewis
  • Biology
    Trends in biochemical sciences
  • 1994