Amino acid residues crucial for specificity of toxin–antitoxin interactions in the homologous Axe–Txe and YefM–YoeB complexes


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Abstract

Toxin–antitoxin complexes are ubiquitous in bacteria. The specificity of interactions between toxins and antitoxins from homologous but non-interacting systems was investigated. Based on molecular modeling, selected amino acid residues were changed to assess which positions were crucial in the specificity of toxin–antitoxin interaction in the related Axe–Txe and YefM–YoeB complexes. No cross-interactions between wild-type proteins were detected. However, a single amino acid substitution that converts a Txe-specific residue to a YoeB-specific residue reduced, but did not abolish, Txe interaction with the Axe antitoxin. Interestingly, this alteration (Txe-Asp83Tyr) promoted functional interactions between Txe and the YefM antitoxin. The interactions between Txe-Asp83Tyr and YefM were sufficiently strong to abolish Txe toxicity and to allow effective corepression by YefM-Txe-Asp83Tyr of the promoter from which yefMyoeB is expressed. We conclude that Asp83 in Txe is crucial for the specificity of toxin–antitoxin interactions in the Axe–Txe complex and that swapping this residue for the equivalent residue in YoeB relaxes the specificity of the toxin–antitoxin interaction.Structured digital abstractAxe and Txe physically interact by two hybrid (View interaction)YoeB and YefM physically interact by two hybrid (View interaction)The specificity of interactions between toxins and antitoxins from homologous but non-interacting systems was investigated. Based on molecular modeling, selected amino acid residues were changed to assess which positions were crucial in specificity of toxin-antitoxin interactions in the related Axe-Txe and YefM-YoeB complexes. We conclude that Asp83 in Txe is crucial for specificity of toxin–antitoxin interactions in the Axe-Txe complex.

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