BglG, the response regulator of the Escherichia coli bgl operon, is phosphorylated on a histidine residue.
We have shown previously that the activity of BglG, the response regulator of the bgl system, as a transcriptional antiterminator is modulated by the sensor BglF, which reversibly phosphorylates BglG. We show here that the phosphoryl group on BglG is present as a phosphoramidate, based on the sensitivity of phosphorylated BglG to heat, hydroxylamine, and acidic but not basic conditions. By analyzing the products of base-hydrolyzed phosphorylated BglG by thin-layer chromatography, we show that the phosphorylation occurs on a histidine residue. This result supports the notion that the bgl system is a member of a new family of bacterial sensory systems.
Amster-Choder
O
O
Department of Molecular Biology, Hadassah Medical School, The Hebrew University, Jerusalem, Israel.
Wright
A
A
D001426:Bacterial Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins; D006639:Histidine / Q000031:analogs & derivatives / Q000032:analysis / Q000378:metabolism*; D008565:Membrane Proteins / Q000235:genetics; D009876:Operon / Q000235:genetics; D010766:Phosphorylation; D011494:Protein Kinases / Q000235:genetics; D016601:RNA-Binding Proteins / Q000378:metabolism*
D001426:Bacterial Proteins; C079638:BglF protein, E coli; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D016601:RNA-Binding Proteins; C064872:antiterminator proteins, Bacteria; D006639:Histidine; D011494:Protein Kinases; C005436:phosphohistidine