Fig. 6: Mechanism by which m1G37 influences the conformational energy of tRNAProL and modulates +1 frameshifting. | Nature Communications

Fig. 6: Mechanism by which m1G37 influences the conformational energy of tRNAProL and modulates +1 frameshifting.

From: An RNA modification prevents extended codon-anticodon interactions from facilitating +1 frameshifting

Fig. 6

a Unmodified peptidyl-tRNAProL can undergo +1 frameshifting either during the substep of the elongation cycle in which it is translocated from the A site into the P site (substeps in white background) or at the substep in which it has been translocated into the P site but has not yet undergone transfer of its peptidyl moiety onto the incoming aa-tRNA at the A site (complexes in light green and light orange background and substeps connecting them). Delivery of an aa-tRNA into the A site in the +1 frame stabilizes the P site-bound, +1 frameshifted, unmodified tRNAProL via stabilization of four Watson-Crick (WC) base pairs and an additional hydrogen bond at a fifth pairing (complex in light pink background). b Close-up view of WC base pairing and hydrogen bonding interactions formed within the various substeps and complexes in (a).

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