Activation of contact-dependent antibacterial tRNase toxins by translation elongation factors

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Significance Contact-dependent growth inhibition (CDI) systems enable cells to bind competing bacteria and deliver toxins that cleave nucleic acids or form membrane pores. Here, we characterize a CDI toxin that specifically cleaves transfer RNA (tRNA), thereby blocking protein synthesis and inhibiting bacterial growth. Remarkably, two highly conserved and essential translation factors, EF-Ts and EF-Tu, are critical for this toxic nuclease activity. The toxin binds EF-Tu with high affinity and only cleaves tRNA in complex with the translation factor. EF-Ts appears to increase the rate of tRNA turnover. The activities of two other distinct CDI toxins are also regulated by EF-Ts. We propose that the regulation of toxin activity by the protein synthesis apparatus may play a role in intercellular communication.

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