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MazF-induced growth inhibition and persister generation in Escherichia coli

Arti Tripathi1, Pooja C Dewan, Shahbaz Ahmed

  • 1From the Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India and.

The Journal of Biological Chemistry
|December 31, 2013
PubMed

Insights

MazEF toxin-antitoxin systems induce reversible bacterial growth arrest, enhancing survival during antibiotic stress. This persistence mechanism depends on ClpP and Lon proteases, not RecA.

Area of Science:

  • Microbiology
  • Bacterial Physiology
  • Molecular Biology

Background:

  • Toxin-antitoxin systems are widespread in bacteria and archaea.
  • MazEF is a type II system in Escherichia coli, with debated roles in cell death, growth inhibition, and persistence.
  • Understanding MazF's function is crucial for bacterial survival mechanisms.

Purpose of the Study:

  • To investigate the role of MazF in bacterial physiology.
  • To determine MazF's involvement in reversible growth inhibition and antibiotic persistence.
  • To elucidate the molecular mechanisms underlying MazF-mediated persistence.

Main Methods:

  • Utilized an inactive active-site mutant (E24A) of MazF to activate wild-type (WT) MazF expression.
  • Ectopic expression of E24A MazF in a WT mazEF strain induced reversible growth arrest.
  • Assessed bacterial survival under antibiotic stress following MazF activation.

Main Results:

  • Ectopic expression of E24A MazF led to reversible growth arrest, with normal growth resuming upon inhibition.
  • MazF-mediated growth arrest increased bacterial survival during antibiotic stress.
  • The persistence phenotype was independent of RecA but dependent on ClpP and Lon proteases.

Conclusions:

  • MazEF plays a significant role in reversible growth inhibition.
  • MazEF contributes to bacterial persistence, a survival strategy against antibiotic stress.
  • The study confirms the involvement of ClpP and Lon proteases in MazF-mediated persistence.
Keywords:
Antibiotic ToleranceAntibioticsBacteriostasisCell DeathInactive, Active-site MutantMutantProtein DegradationProtein SynthesisToxin-Antitoxin

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