PMID:9287026

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Citation

Amster-Choder, O and Wright, A (1997) BglG, the response regulator of the Escherichia coli bgl operon, is phosphorylated on a histidine residue. J. Bacteriol. 179:5621-4

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.

Links

PubMed PMC179442

Keywords

Bacterial Proteins/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Histidine/analogs & derivatives; Histidine/analysis; Histidine/metabolism; Membrane Proteins/genetics; Operon/genetics; Phosphorylation; Protein Kinases/genetics; RNA-Binding Proteins/metabolism

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