Affiliation:
1. Department of Molecular Biology, Hadassah Medical School, The Hebrew University, Jerusalem, Israel.
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.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
29 articles.
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