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(Received for publication, May 17, 1996)
From the Department of Microbiology, Groningen Biomolecular
Sciences and Biotechnology Institute, University of Groningen,
Kerklaan 30, NL-9751 NN Haren, The Netherlands
The gene encoding the secondary multidrug
transporter LmrP of Lactococcus lactis was heterologously
expressed in Escherichia coli. The energetics and mechanism
of drug extrusion mediated by LmrP were studied in membrane vesicles of
E. coli. LmrP-mediated extrusion of tetraphenyl phosphonium
(TPP+) from right-side-out membrane vesicles and uptake of
the fluorescent membrane probe
1-[4-(trimethylamino)phenyl]-6-phenylhexa-1,3,5-triene
(TMA-DPH) into inside-out membrane vesicles are driven by the membrane
potential (
Volume 271, Number 39,
Issue of September 27, 1996
pp. 24123-24128
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
) and the transmembrane proton gradient (pH),
pointing to an electrogenic drug/proton antiport mechanism. Ethidium
bromide, a substrate for LmrP, inhibited the LmrP-mediated
TPP+ extrusion from right-side-out membrane vesicles,
showing that LmrP is capable of transporting structurally unrelated
drugs. Kinetic analysis of LmrP-mediated TMA-DPH transport revealed a
direct relation between the transport rate and the amount of TMA-DPH
associated with the cytoplasmic leaflet of the lipid bilayer. This
observation indicates that drugs are extruded from the inner leaflet of
the cytoplasmic membrane into the external medium. This is the first
report that shows that drug extrusion by a secondary multidrug
resistance (MDR) transporter occurs by a ``hydrophobic vacuum
cleaner'' mechanism in a similar way as was proposed for the primary
lactococcal MDR transporter, LmrA.
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