Interaction of the maltose-binding protein with membrane vesicles of Escherichia coli.
The interaction of the radioactively labeled purified maltose-binding protein of Escherichia coli with membrane vesicles was studied. The maltose-binding protein bound specifically to the vesicles, in the presence of maltose, on few sites. Under conditions in which a potential was imposed across the membrane, the specific binding was (i) increased, (ii) dependent on maltose, and (iii) abolished in a mutant defective in the tar gene product, one of the methyl-accepting chemotaxis proteins. At least 1,300 binding sites were present in the membrane fraction of logarithmically growing cells.
D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D002352:Carrier Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D002633:Chemotaxis; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins; D008320:Maltose / Q000494:pharmacology; D058619:Maltose-Binding Proteins; D008564:Membrane Potentials; D009004:Monosaccharide Transport Proteins; D009154:Mutation; D014634:Valinomycin / Q000494:pharmacology
D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D058619:Maltose-Binding Proteins; D009004:Monosaccharide Transport Proteins; C461599:maltose transport system, E coli; D014634:Valinomycin; D008320:Maltose