The role of ribose-binding protein in transport and chemotaxis in Escherichia coli K12

Abstract

The ribose-binding protein of Escherichia coli [Willis, R. C., and Furlong, C. E. (1974) J. Biol. Chem. 249, 6926–6929] has been shown to be a required common receptor component for high-affinity ribose transport and for chemotaxis toward this attractant. Mutants devoid of the ribose-binding protein are missing high-affinity ribose transport and do not respond chemotactically to this sugar, whereas the response to other attractants is normal. Eight independently isolated ribose-positive revertant strains regained the binding protein, high-affinity ribose transport, and ribose chemotaxis. One revertant which grows slowly on ribose as a sole carbon source did not regain the binding protein, high-affinity transport, or ribose chemotaxis.