Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2005-3-3
pubmed:abstractText
To understand better the mechanisms of resistance-nodulation-division (RND)-type multidrug efflux pumps, we examined the Escherichia coli AcrD pump, whose typical substrates, aminoglycosides, are not expected to diffuse spontaneously across the lipid bilayer. The hexahistidine-tagged AcrD protein was purified and reconstituted into unilamellar proteoliposomes. Its activity was measured by the proton flux accompanying substrate transport. When the interior of the proteoliposomes was acidified, the addition of aminoglycosides to the external medium stimulated proton efflux and the intravesicular accumulation of radiolabeled gentamicin, suggesting that aminoglycosides can be captured and transported from the external medium in this system (corresponding to cytosol). This activity required the presence of AcrA within the proteoliposomes. Interestingly, the increase in proton efflux also occurred when aminoglycosides were present only in the intravesicular space. This result suggested that AcrD can also capture aminoglycosides from the periplasm to extrude them into the medium in intact cells, acting as a "periplasmic vacuum cleaner."
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-10377390, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-10473554, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-10692383, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-10894736, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-10931319, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-10941792, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-11257026, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-11566977, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-11858709, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-12374972, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-12426336, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-12738864, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-12949086, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-13129936, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-14523004, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-1454821, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-15117957, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-15226509, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-15743933, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-2026607, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-2447086, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-6261798, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-7517935, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-7651136, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-7986004, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-8021163, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-8550435, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-8824631, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-8830678, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-9710669, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-9711542, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-9721312, http://linkedlifedata.com/resource/pubmed/commentcorrection/15743938-9878415
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acids, http://linkedlifedata.com/resource/pubmed/chemical/AcrA protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Aminoglycosides, http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Gentamicins, http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proteolipids, http://linkedlifedata.com/resource/pubmed/chemical/Streptomycin, http://linkedlifedata.com/resource/pubmed/chemical/Tritium, http://linkedlifedata.com/resource/pubmed/chemical/proteoliposomes
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9193
pubmed:author
pubmed:issnType
Print
pubmed:volume
187
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1923-9
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Aminoglycosides are captured from both periplasm and cytoplasm by the AcrD multidrug efflux transporter of Escherichia coli.
pubmed:affiliation
Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.