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An oxygen-sensitive toxin-antitoxin system.

Oriol Marimon1, João M C Teixeira1, Tiago N Cordeiro1

  • 1Biomolecular NMR Laboratory, Organic Chemistry Section, Inorganic and Organic Chemistry Department, University of Barcelona, Baldiri Reixac 10-12, Barcelona 08028, Spain.

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Summary
This summary is machine-generated.

Yersinia YmoB protein and its variant can function as antitoxins in E. coli, replacing TomB. This interaction enhances Hha toxin oxidation, destabilizing it via a unique oxygen-dependent mechanism.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Structural Biology

Background:

  • Toxin-antitoxin (TA) systems regulate cellular processes.
  • The Hha-TomB system from Escherichia coli is oxygen-dependent.
  • Orthologues of TA system components can exhibit functional conservation.

Purpose of the Study:

  • To investigate the functional replacement of E. coli TomB by its Yersinia orthologue, YmoB.
  • To elucidate the mechanism of interaction between Hha and YmoB variants.
  • To characterize the structural basis of the Hha-YmoB interaction.

Main Methods:

  • Functional assays in E. coli to test antitoxin activity.
  • Nuclear Magnetic Resonance (NMR) spectroscopy for structural determination.
  • Homology modeling to predict protein structures.

Main Results:

  • YmoB and [C117S]YmoB successfully replaced TomB as antitoxins.
  • [C117S]YmoB exhibited transient interaction with Hha, unlike stable TA complexes.
  • The interaction promoted spontaneous oxidation of Hha's cysteine residue, destabilizing the toxin.
  • Structural analysis revealed a conserved buried cysteine in YmoB/TomB, accessible via an oxygen-sized channel.

Conclusions:

  • Yersinia YmoB functions as an antitoxin in E. coli.
  • The Hha-YmoB interaction mechanism involves oxygen-dependent cysteine oxidation and toxin destabilization.
  • Structural features facilitate oxygen access and interaction with the toxin.