Studies on bacterial chemotaxis. IV. Interaction of maltose receptor with a membrane-bound chemosensing component

Highly purified maltose receptor of Escherichia coli was bound to Sepharose 4B via a long spacer and affinity chromatography was performed to isolate the membrane-bound proteins having affinity for the maltose receptor. The experiments were carried out either in the presence of maltose or in the absence of maltose and the proteins absorbed on the mattix were identified by two-dimensional gel electrophoresis. The results showed that the maltose receptor interacted with the product of tar gene, one of the methyl-accepting chemotaxis proteins, only in the presence of maltose.