The transfer of a bacterial transmembrane function to eukaryotic cells.
This communication reports our preliminary studies on the reconstitution of the bacterial dicarboxylate transport system into rat myoblasts and mouse L-cells. Purified dicarboxylate membrane transport components (SBP 1 and SBP 2) from Escherichia coli K12 were added to rat myoblasts and mouse L-cells. These components were readily incorporated into the cell membranes. The rat myoblasts, as well as the mouse L-cells, were unable to transport succinate by themselves, or in the presence of either one of the transport components. However, when both components were added to the cells, the latter acquired the ability to transport succinate. There was a direct relationship between the amount of transport components added and the rate of succinate uptake. The newly acquired dicarboxylate transport system exhibited similar substrate affinity and specificity as the E. coli dicarboxylate transport system. The above findings suggest that it is possible to transfer a bacterial transmembrane function into eukaryotic cell membrane, and that these proteins can function normally in a foreign environment.
D001693:Biological Transport, Active; D002352:Carrier Proteins / Q000378:metabolism*; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism*; D003998:Dicarboxylic Acids / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D007444:Inulin / Q000378:metabolism; D007700:Kinetics; D007739:L Cells / Q000378:metabolism
D002352:Carrier Proteins; D003998:Dicarboxylic Acids; D007444:Inulin