Elimination of GlnKAmtB affects serine biosynthesis and improves growth and stress tolerance of Escherichia coli under nutrient-rich conditions

FEMS Microbiol Lett. 2020 Dec 22;367(23):fnaa197. doi: 10.1093/femsle/fnaa197.

Abstract

Nitrogen is a most important nutrient resource for Escherichia coli and other bacteria that harbor the glnKamtB operon, a high-affinity ammonium uptake system highly interconnected with cellular metabolism. Although this system confers an advantage to bacteria when growing under nitrogen-limiting conditions, little is known about the impact of these genes on microbial fitness under nutrient-rich conditions. Here, the genetically tractable E. coli BW25113 strain and its glnKamtB-null mutant (JW0441) were used to analyze the impact of GlnK-AmtB on growth rates and oxidative stress tolerance. Strain JW0441 showed a shorter initial lag phase, higher growth rate, higher citrate synthase activity, higher oxidative stress tolerance and lower expression of serA than strain BW25113 under nutrient-rich conditions, suggesting a fitness cost to increase metabolic plasticity associated with serine metabolism. The overexpression of serA in strain JW0441 resulted in a decreased growth rate and stress tolerance in nutrient-rich conditions similar to that of strain BW25113, suggesting that the negative influence on bacterial fitness imposed by GlnK-AmtB can be traced to the control of serine biosynthesis. Finally, we discuss the potential applications of glnKamtB mutants in bioproduction processes.

Keywords: ammonium uptake; evolutionary innovation; growth rate; lag phase; oxidative stress.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cation Transport Proteins / genetics*
  • Cation Transport Proteins / metabolism
  • Escherichia coli / genetics*
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / genetics*
  • Escherichia coli Proteins / metabolism
  • Industrial Microbiology
  • Mutation
  • Nucleotidyltransferases / genetics*
  • Nucleotidyltransferases / metabolism
  • Operon / genetics
  • PII Nitrogen Regulatory Proteins / genetics*
  • PII Nitrogen Regulatory Proteins / metabolism
  • Serine / biosynthesis*
  • Serine / genetics

Substances

  • AmtB protein, E coli
  • Cation Transport Proteins
  • Escherichia coli Proteins
  • PII Nitrogen Regulatory Proteins
  • Serine
  • glnK protein, E coli
  • Nucleotidyltransferases