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. 2021 Mar 23;12:1830. doi: 10.1038/s41467-021-21942-6

Fig. 3. Apramycin induces proteotoxic misreading and inhibits translocation.

Fig. 3

a Single amino acid substitutions induced by Apr and Str. Errors induced predominantly by Apr (16 µM) are shown in cold colors; those induced by Str (8 µM) in warm colors. Shown are means ± SD of three technical replicates (n = 3). b Error clusters in Apr-treated cells (red) compared to single errors (gray). Shown are means ± SD of three technical replicates (n = 3). We note a better correlation for single errors (Pearson coefficient 0.72) than for error clusters (0.41), suggesting that the mechanisms that govern cluster formation are not identical to those for single errors and depend on the AGA used. c Growth defect and error load at increasing Apr concentrations. At growth-inhibitory concentration of Apr the median error frequency approaches that after Str treatment. Data from Supplementary Fig. 5b; Shown are means ± SD of three technical replicates (n = 3). d Induction of the heat shock response. The chaperones IbpA/IbpB are significantly induced upon Apr (16 µM) and Str (8 µM) treatment as quantified by SRM. Shown are means ± SD of three technical replicates (n = 3) calculated taking into account their individual peptide-based stoichiometries. e Products of the in-vitro translation of SlyD mRNA. Translation products are separated by SDS PAGE and detected using the fluorescence of the N-terminal BODIPY-Met. f Time courses of in-vitro translation of SlyD mRNA at different Apr concentrations. Translation products were detected as in (e). g Rate of in-vitro translation (aa/s) at different Apr concentrations for SlyD mRNA (white bars) and poly(U) mRNA (gray bars). Shown are means ± SD of three technical replicates (n = 3). See also Supplementary Fig. 5 and Source data file.