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Papers In Press, published online ahead of print September 8, 2003
Laboratoire de Chimie Bactérienne, CNRS, Marseille 13402
Corresponding Author: bogoerke{at}ibsm.cnrs-mrs.fr
Activity of antiterminator protein BglG regulating the beta-glucoside operon in Escherichia coli is controlled by the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS) in a dual manner. It requires phosphorylation by HPr to be active, whereas phosphorylation by the beta-glucoside specific transport protein EIIBgl inhibits its activity. BglG and its relatives carry two PTS regulation domains (PRD1 and PRD2), each containing two conserved histidines. For BglG, histidine H208 in PRD2 was reported to be the negative phosphorylation site. In contrast, other antiterminators of this family are negatively regulated by phosphorylation of the first histidine in PRD1, and presumably activated by phosphorylation of the histidines in PRD2. In this work, a screen for mutant BglG proteins that escape repression by EIIBgl yielded exchanges of nine residues within PRD1, including conserved histidines H101 and H160, and C-terminally truncated proteins. Genetic and phosphorylation analyses indicate that H101 in PRD1 is phosphorylated by EIIBgl and that H160 contributes to negative regulation. H208 in PRD2 is essential for BglG activity, suggesting that it is phosphorylated by HPr. Surprisingly, phosphorylation by HPr is not fully abolished by exchanges of H208. However, phosphorylation by HPr is inhibited by exchanges in PRD1 and the phosphorylation of these mutants is restored in the presence of wild type BglG. These results suggest that the activating phosphoryl group is transiently donated from HPr to PRD1 and subsequently transferred to H208 of a second BglG monomer. The active, H208-phosphorylated BglG dimer can subsequently be inhibited in its activity by EIIBgl catalyzed phosphorylation at H101.
J. Biol. Chem, 10.1074/jbc.M308002200
Submitted on July 23, 2003
Revised on August 26, 2003
Accepted on September 8, 2003
Regulation of the Escherichia coli antiterminator protein BglG by phosphorylation at multiple sites and evidence for transfer of phosphoryl groups between monomers
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