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The  Escherichia coli  eukaryote-like serine/threonine kinase, encoded by  yeaG , is expressed in response to diverse stresses, including nitrogen (N) starvation. A role for  yeaG  in bacterial stress response is unknown. Here we reveal for the first time that wild-type  E. coli  displays metabolic heterogeneity following sustained periods of N starvation, with the metabolically active population displaying compromised viability. In contrast, such heterogeneity in metabolic activity is not observed in an  E. coli  ∆ yeaG  mutant, which continues to exist as a single and metabolically active population and thus displays an overall compromised ability to survive sustained periods of N starvation. The mechanism by which  yeaG  acts, involves the transcriptional repression of two toxin/antitoxin modules,  mqsR/mqsA  and  dinJ / yafQ . This, consequently, has a positive effect on the expression of  rpoS , the master regulator of the general bacterial stress response. Overall, results indicate that  yeaG  is required to fully execute the  rpoS -dependent gene expression program to allow  E. coli  to adapt to sustained N starvation and unravels a novel facet to the regulatory basis that underpins adaptive response to N stress.

Adaptation to sustained nitrogen starvation by Escherichia coli requires the eukaryote-like serine/threonine kinase YeaG