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. 1997 Sep;179(17):5621–5624. doi: 10.1128/jb.179.17.5621-5624.1997

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

O Amster-Choder 1, A Wright 1
PMCID: PMC179442  PMID: 9287026

Abstract

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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Selected References

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