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. 2023 Jan 3;14:30. doi: 10.1038/s41467-022-35684-6

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 5 — a In vitro translation assay using mitochondrial or cytosolic ribosomes. Up to five amino-acylated tRNAs were added to the translation mixture. Elongation was assessed by measuring incorporation of radioactively labeled amino acids (*). Specificity of mitoribosomal translation was tested by the absence of mtEFG1 or by addition of fusidic acid. Means and SD of n = 3 independent experiments. Unpaired two-tailed t-test (*P < 0.05; **P < 0.01; ***P < 0.001; ns = not significant). Only relevant statistics are highlighted. b Schematic representation of the in vitro mitochondrial translation termination assay. Post-translocation complexes (POST2) containing fMQ-tRNA^Q* in the P-site and either canonical stop codon UAG or non-canonical stop codons AGA/AGG in the A-site were prepared. MtRF1a/mtRF1-dependent release of dipeptide was assayed by co-sedimentation. Radioactive glutamine was used for detection. c In vitro release activity of mtRF1a and mtRF1 at UAG/AGA/AGG codons. Means and SD of n = 3 independent experiments. Unpaired two-tailed t-test (*P < 0.05; **P < 0.01; ***P < 0.001).