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J. Bacteriol., 09 1997, 5621-5624, Vol 179, No. 17
Copyright © 1997, American Society for Microbiology

BglG, the response regulator of the Escherichia coli bgl operon, is phosphorylated on a histidine residue

O Amster-Choder and A Wright
Department of Molecular Biology, Hadassah Medical School, The Hebrew University, Jerusalem, Israel.

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.


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