title: Adaptation to sustained nitrogen starvation by Escherichia coli requires the eukaryote-like serine/threonine kinase YeaG.
abstract: 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.
authors.affiliation: MRC Centre for Molecular Microbiology and Infection, Imperial College London, UK.
authors.forename: Rita
authors.initials: R
authors.lastname: Figueira
authors.affiliation: MRC Centre for Molecular Microbiology and Infection, Imperial College London, UK.
authors.forename: Daniel R
authors.initials: DR
authors.lastname: Brown
authors.affiliation: MRC Centre for Molecular Microbiology and Infection, Imperial College London, UK.
authors.forename: Delfim
authors.initials: D
authors.lastname: Ferreira
authors.affiliation: MRC Centre for Molecular Microbiology and Infection, Imperial College London, UK.
authors.forename: Matthew J G
authors.initials: MJ
authors.lastname: Eldridge
authors.affiliation: MRC Centre for Molecular Microbiology and Infection, Imperial College London, UK.
authors.forename: Lynn
authors.initials: L
authors.lastname: Burchell
authors.affiliation: MRC Centre for Molecular Microbiology and Infection, Imperial College London, UK.
authors.forename: Zhensheng
authors.initials: Z
authors.lastname: Pan
authors.affiliation: MRC Centre for Molecular Microbiology and Infection, Imperial College London, UK.
authors.forename: Sophie
authors.initials: S
authors.lastname: Helaine
authors.affiliation: MRC Centre for Molecular Microbiology and Infection, Imperial College London, UK.
authors.forename: Sivaramesh
authors.initials: S
authors.lastname: Wigneshweraraj
mesh_terms: D000222:Adaptation, Physiological; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D001427:Bacterial Toxins / Q000235:genetics / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism; D048168:Escherichia coli K12 / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D017353:Gene Deletion; D009584:Nitrogen / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*; D012808:Sigma Factor / Q000235:genetics / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004268:DNA-Binding Proteins; C523349:DinJ protein, E coli; D029968:Escherichia coli Proteins; C555039:MqsA protein, E coli; C508571:MqsR protein, E coli; D012808:Sigma Factor; C523350:YafQ protein, E coli; C069567:sigma factor KatF protein, Bacteria; D017346:Protein Serine-Threonine Kinases; C528225:YeaG protein, E coli; D009584:Nitrogen