The periplasmic galactose binding protein of Escherichia coli.

Abstract

A specific high affinity galactose transport system called P(betag) can be induced by trace amounts of galactose in the medium by virtue of its own ability to capture and accumulate galactose. The transport system is coregulated with the production of a high affinity periplasmic galactose binding protein, which constitutes but one part of the transport system. Some transport negative mutants still remain producers of this binding protein. A close correlation exists between production of the active binding protein and the presence of galactose chemotaxis. The hypothesis, that this binding protein is a common element of the specific galactose transport system, P(betag), and of galactose chemotaxis is supported by observations on structural mutants, being defective in galactose binding protein as well as showing a lack of galactose chemotaxis. The binding protein is a monomer with two binding sites for galactose. Binding of one or two of the galactose molecules elicits specific conformational changes of the galactose binding protein (lowered affinity for galactose, increase of charges of the protein, increased fluorescence of tryptophan residues). The importance of these features for transport and for chemotaxis is discussed (70).