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

O. Amster-Choder, A. Wright*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

28 Scopus citations

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 BgIF, 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.

Original languageEnglish
Pages (from-to)5621-5624
Number of pages4
JournalJournal of Bacteriology
Volume179
Issue number17
DOIs
StatePublished - 1997
Externally publishedYes

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