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Ammonium assimilation in E. coli is regulated by two paralogous proteins(GlnB and GlnK), which orchestrate interactions with regulators of geneexpression, transport proteins and metabolic pathways. Yet how they conjointlymodulate the activity of glutamine synthetase (GS), the key enzyme for nitrogenassimilation, is poorly understood. We combine experiments and theory to studythe dynamic roles of GlnB and GlnK during nitrogen starvation and upshift. Wemeasure time-resolved in vivo concentrations of metabolites, total andpost-translationally modified proteins, and develop a concise biochemical modelof GlnB and GlnK that incorporates competition for active and allosteric sites,as well as functional sequestration of GlnK. The model predicts the responsesof GS, GlnB and GlnK under time-varying external ammonium level in the wildtype and two genetic knock-outs. Our results show that GlnK is tightlyregulated under nitrogen-rich conditions, yet it is expressed during ammoniumrun-out and starvation. This suggests a role for GlnK as a buffer of nitrogenshock after starvation, and provides a further functional link between nitrogenand carbon metabolisms.

GlnK facilitates the dynamic regulation of bacterial nitrogen assimilation