Fig. 6: A simplified model for RFC catalysis of termination. | Nature Communications

Fig. 6: A simplified model for RFC catalysis of termination.

From: Ataluren binds to multiple protein synthesis apparatus sites and competitively inhibits release factor-dependent termination

Fig. 6: A simplified model for RFC catalysis of termination.The alternative text for this image may have been generated using AI.

This model, consistent with all of our results, as well as with recent published results of others37, posits that ataluren inhibition results from the cooperative binding of (n) molecules of ataluren to the pretermination complex P5 in competition with RFC binding. It also invokes a hypothetical complex C3 resulting from an at least partial rate-determining conformational change, following cleavage of the tRNA-peptide ester bond to account for the similarity in the rate constants of tRNA, peptide, and eRF1 release (see text). The question marks associated with possible eRF1 release are shown to indicate our current uncertainty as to whether eRF1 release is coordinated with either peptide or tRNA release, or proceeds independently of either.

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