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Multidrug resistance mediated by a bacterial homolog of the human multidrug transporter MDR1.
- H. V. van Veen, K. Venema, W. Konings
- BiologyProceedings of the National Academy of Sciences…
- 1 October 1996
The gene cloning and functional characterization in Escherichia coli of LmrA, a lactococcal structural and functional homolog of the human multidrug resistance P-glycoprotein MDR1, is reported, offering a useful prokaryotic model for future studies on the molecular mechanism of MDR 1-like multidrog transporters.
Distribution and Physiology of ABC-Type Transporters Contributing to Multidrug Resistance in Bacteria
- J. Lubelski, W. Konings, A. Driessen
- BiologyMicrobiology and Molecular Biology Reviews
- 1 September 2007
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.
Bacteriocins: mechanism of membrane insertion and pore formation
Lactic acid bacteria produce several types of pore forming peptides that contain (methyl)lanthionine residues that may form intramolecular thioether rings, which generally have a broad spectrum of activity and form unstable pores.
Pediocin PA-1, a bacteriocin from Pediococcus acidilactici PAC1.0, forms hydrophilic pores in the cytoplasmic membrane of target cells
- M. Chikindas, M. García-Garcerá, G. Venema
- BiologyApplied and Environmental Microbiology
- 1 November 1993
The data suggest that pediocin PA-1 functions in a voltage-independent manner but requires a specific protein in the target membrane, while it is less effective with membranes derived from immune cells.
Generation of a proton motive force by histidine decarboxylation and electrogenic histidine/histamine antiport in Lactobacillus buchneri
- D. Molenaar, J. Bosscher, B. ten Brink, A. Driessen, W. Konings
- BiologyJournal of Bacteriology
- 1 May 1993
The data suggest that the generation of metabolic energy from histidine decarboxylation results from an electrogenic histidine/histamine exchange and indirect proton extrusion due to the combined action of the decar boxylase and carrier-mediated exchange.
Insights into ABC Transport in Archaea
- S. Albers, S. Koning, W. N. Konings, A. Driessen
- BiologyJournal of bioenergetics and biomembranes
- 1 February 2004
Examination of the signal peptides of binding proteins of 14 archaeal genomes showed clear differences between euryarchaeote and crenarchaeotes, and a profiling and comparison of ABC transporters in the three sequenced pyrococcal strains was performed.
Cellobiose Uptake in the Hyperthermophilic ArchaeonPyrococcus furiosus Is Mediated by an Inducible, High-Affinity ABC Transporter
- S. Koning, M. Elferink, W. N. Konings, A. Driessen
- Biology, EngineeringJournal of bacteriology
- 1 September 2001
The cellobiose binding protein (CbtA) was purified from P. furiosus membranes to homogeneity as a 70-kDa glycoprotein and belongs to a gene cluster that encodes a transporter that belongs to the Opp family of ABC transporters.
Bioenergetics and solute transport in lactococci.
Detailed studies of the transport processes of lactic acid bacteria during growth and starvation have been performed in cytoplasmic membrane vesicles of these organisms in which a foreign proton pump has been introduced to generate a high proton motive force.
Bioenergetics and cytoplasmic membrane stability of the extremely acidophilic, thermophilic archaeon Picrophilus oshimae
Observations suggest that the loss of viability and cell integrity above pH 4.0 is due to an impairment of the barrier function of the cytoplasmic membrane.
The Lactococcal lmrP Gene Encodes a Proton Motive Force- dependent Drug Transporter (*)
- H. Bolhuis, G. Poelarends, H. V. van Veen, B. Poolman, A. Driessen, W. Konings
- BiologyThe Journal of Biological Chemistry
- 3 November 1995
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.