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. 2022 Apr 12;50(8):4713–4731. doi: 10.1093/nar/gkac228

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© The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 8. — Model of tRNA cleavage by CdiA–CT^EC869 in the presence of translation factors. The Tu:GTP:Ts complex acts as a scaffold for tRNA cleavage by CdiA–CT^EC869. First, CdiA–CT^EC869 delivered into the cell is recruited to the Tu:GTP:Ts complex to form the CdiA–CT:Tu:GTP:Ts complex. Substrate aa-tRNA (or tRNA) is recognized by CdiA–CT:Tu:GTP:Ts and forms CdiA–CT:Tu:GTP:Ts:aa-tRNA(tRNA). Ts in the CdiA–CT:Tu:GTP:Ts complex increases the affinity of tRNA for the complex and induces a structural change in tRNA and/or CdiA–CT to promote productive catalysis by CdiA–CT. CdiA–CT might interact with Tu:GTP and form CdiA–CT:Tu:GTP, and aa-tRNA (tRNA) could be recognized by the complex. However, aa-tRNA (tRNA) cannot be cleaved by CdiA–CT due to the low affinity of aa-tRNA (tRNA) to the CdiA–CT:Tu:GTP complex. Association of Ts to CdiA–CT:Tu:GTP or association of CdiA–CT to Tu:GTP:Ts is required for aa-tRNA (tRNA) binding and cleavage by CdiA–CT. It is not clear whether CdiA–CT first associates with Tu:GTP and then Ts is recruited to form CdiA–CT:Tu:GTP:Ts or CdiA–CT associates with Tu:GTP:Ts to form CdiA–CT:Tu:GTP:Ts.