TY - JOUR
T1 - BglG, the response regulator of the Escherichia coli bgl operon, is phosphorylated on a histidine residue
AU - Amster-Choder, O.
AU - Wright, A.
PY - 1997
Y1 - 1997
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0030931685&partnerID=8YFLogxK
U2 - 10.1128/jb.179.17.5621-5624.1997
DO - 10.1128/jb.179.17.5621-5624.1997
M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???
C2 - 9287026
AN - SCOPUS:0030931685
SN - 0021-9193
VL - 179
SP - 5621
EP - 5624
JO - Journal of Bacteriology
JF - Journal of Bacteriology
IS - 17
ER -