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The Bacillus subtilis glpD leader and antiterminator protein GlpP provide a target for glucose repression in Escherichia coli.

Expression of the Bacillus subtilis glpD gene which encodes glycerol-3-phosphate (G3P) dehydrogenase is regulated by the GlpP protein which, in the presence of G3P, causes antitermination of transcription of glpD. The glpD gene leader fused to lacZ was integrated into the chromosome of Escherichia coli deleted for the lac operon and carrying the B. subtilis glpP gene on a plasmid. beta-Galactosidase activity of this strain was increased by the addition of G3P. When G3P and glucose, glucose-6-phosphate or fructose-6-phosphate were added, beta-galactosidase activity was reduced showing that GlpP mediates catabolite repression of transcription from the glpD leader in the absence of any other B. subtilis protein.