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. 2023 Dec 15;52(2):513–524. doi: 10.1093/nar/gkad1188

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© The Author(s) 2023. 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 3. — Transfer of identity elements into other tRNA^Pyl sequences promotes MaPylRS recognition. (A) Mm tRNA^Pyl variant cloverleaf structures. Bases that are changed or missing are represented with an orange circle. (B) In vitro assays with Mm tRNA^Pyl variants show the effect of tRNA mutations on aminoacylation efficiency with MaPylRS. (C) In vivo fluorescent readthrough assays with Mm tRNA^Pyl variants show the effect of tRNA mutations on translation with MaPylRS. (D) Dh tRNA^Pyl variant cloverleaf structures. Bases that are changed or missing are represented with a pink circle. (E) In vitro assays with Dh tRNA^Pyl variants show the effect of tRNA mutations on aminoacylation efficiency with MaPylRS. (F) In vivo fluorescent readthrough assays with Dh tRNA^Pyl variants show the effect of tRNA mutations on translation with MaPylRS. Data shown is the average of at least three biological replicates with the error bars representing the standard deviation. Percent activity is calculated with Ma tRNA^Pyl at 100%. Statistical analysis performed with a paired t-test and significance represented as stars.