Open AccessPhosphorylation of nitrogen regulator I (NRI) of Escherichia coli.
Author(s) -
Verena Weiss,
Boris Magasanik
Publication year - 1988
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.85.23.8919
Subject(s) - phosphate , phosphorylation , chemistry , carbamoyl phosphate synthetase , biochemistry , activator (genetics) , histidine , regulator , escherichia coli , enzyme , gene
It has previously been shown that phosphorylated nitrogen regulator I (NRI-phosphate) is the activator responsible for increasing the transcription of glnA, the structural gene for glutamine synthetase, and that NRII catalyzes the transfer of the gamma-phosphate of ATP to NRI. We have now shown that the reaction of ATP with NRII results in the reversible transfer of the gamma-phosphate of ATP to a histidine residue of NRII. In turn, NRII-phosphate transfers its phosphate reversibly to an aspartic residue of NRI. NRI-phosphate is hydrolyzed to NRI and inorganic phosphate in a divalent cation-requiring autocatalytic reaction.