Functional symmetry of the beta-galactoside carrier in Escherichia coli.
Cytoplasmic membrane vesicles with either normal or inverted orientation were prepared from Escherichia coli. The lactose transport activity of these vesicle preparations was compared. The parameters measured were net efflux, counterflux, and K+/valinomycin-induced active uptake of lactose. With membrane vesicles derived from both wild-type and cytochrome-deficient strains the right-side-out and inverted membrane preparations showed similar rates of lactose flux in all assays. According to these criteria, the activity of the beta-galactoside transport protein is inherently symmetrical. One major difference was observed between the native and inverted vesicle preparations: the inverted vesicles had approximately twice the specific activity of native vesicles in the counterflux and K+/valinomycin-induced uptake assays. This difference can be largely ascribed to the presence in the normal vesicle preparation of vesicles with a high passive permeability to lactose. Such vesicles are apparently absent from the inverted vesicle preparations.
D001693:Biological Transport, Active; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism / Q000648:ultrastructure; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D005697:Galactosides / Q000378:metabolism*; D006027:Glycosides / Q000378:metabolism*; D007700:Kinetics; D007785:Lactose / Q000378:metabolism; D010101:Oxygen Consumption; D013050:Spectrometry, Fluorescence; D014634:Valinomycin / Q000494:pharmacology
D005697:Galactosides; D006027:Glycosides; D014634:Valinomycin; D007785:Lactose