@article {Amster-Choder1997-om,
	title = {BglG, the response regulator of the Escherichia coli bgl operon, is phosphorylated on a histidine residue},
	journal = {J. Bacteriol.},
	volume = {179},
	number = {17},
	year = {1997},
	month = {sep},
	pages = {5621{\textendash}5624},
	publisher = {American Society for Microbiology},
	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.},
	author = {Amster-Choder, O and Wright, A}
}
