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.
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.
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.
Kinetics and consequences of binding of nona- and dodecapeptides to the oligopeptide binding protein (OppA) of Lactococcus lactis.
Overall, the data suggest that the slow dissociation rate constants for the larger peptides are rate determining in the translocation of peptides across the membrane.
The plasma membrane of Saccharomyces cerevisiae: structure, function, and biogenesis.
- M. E. van der Rest, A. H. Kamminga, A. Nakano, Y. Anraku, B. Poolman, W. Konings
- BiologyMicrobiological reviews
- 1 June 1995
The use of artificial membranes, like secretory vesicles and plasma membranes fused with proteoliposomes, as model systems for studies on the mechanism and regulation of transport is evaluated.
Mechanisms of multidrug transporters.
- H. Bolhuis, H. V. van Veen, B. Poolman, A. Driessen, W. Konings
- BiologyFEMS Microbiology Reviews
- 1 August 1997
Current knowledge about the occurrence, mechanism and molecular basis of (multi-)drug resistance especially as found in bacteria is summarized.
Multidrug resistance in Lactococcus lactis: evidence for ATP‐dependent drug extrusion from the inner leaflet of the cytoplasmic membrane.
- H. Bolhuis, H. W. Veen, D. Molenaar, B. Poolman, A. Driessen, W. Konings
- BiologyEMBO Journal
- 1 August 1996
Results demonstrate that the lactococcal MDR transporter functions as a ‘hydrophobic vacuum cleaner’, expelling drugs from the inner leaflet of the lipid bilayer, thereby demonstrating the ability of amphiphilic substrates to partition in the inner Leaflets of the membrane is a prerequisite for recognition by multidrug transporters.
Regulation of the glutamate-glutamine transport system by intracellular pH in Streptococcus lactis
The dependence of glutamate transport on the accumulation of potassium ions in potassium-filled and -depleted cells is caused by the regulation of intracellular pH by potassium movement.
Specificity Mutants of the Binding Protein of the Oligopeptide Transport System of Lactococcus lactis
- A. Picon, Edmund R. S. Kunji, F. Lanfermeijer, W. Konings, B. Poolman
- BiologyJournal of Bacteriology
- 15 March 2000
The kinetic properties of wild-type and mutant oligopeptide binding proteins of Lactococcus lactis were determined and imply that the rate of transport is determined to a large extent by the donated peptide from the OppA protein to the translocator complex.
The bacteriocin lactococcin A specifically increases permeability of lactococcal cytoplasmic membranes in a voltage-independent, protein-mediated manner
The combined results obtained with cells, vesicles, and liposomes suggest that the specificity of lactococcin A may be mediated by a receptor protein associated with the cytoplasmic membrane.