title: Phosphorylation of nitrogen regulator I (NRI) of Escherichia coli.
abstract: 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.
authors.affiliation: Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
authors.forename: V
authors.initials: V
authors.lastname: Weiss
authors.forename: B
authors.initials: B
authors.lastname: Magasanik
mesh_terms: D000244:Adenosine Diphosphate / Q000378:metabolism; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism*; D004355:Drug Stability; D004926:Escherichia coli / Q000378:metabolism*; D006639:Histidine / Q000031:analogs & derivatives / Q000302:isolation & purification; D007700:Kinetics; D010766:Phosphorylation
chemical_list: D001426:Bacterial Proteins; D006639:Histidine; D000244:Adenosine Diphosphate; C005436:phosphohistidine