Fig. 3: Loss of tRNA wobble enzymes leads to a global decrease in protein synthesis. | Nature Communications

Fig. 3: Loss of tRNA wobble enzymes leads to a global decrease in protein synthesis.

From: mTORC1 cooperates with tRNA wobble modification to sustain the protein synthesis machinery

Fig. 3: Loss of tRNA wobble enzymes leads to a global decrease in protein synthesis.

a, b Changes in protein synthesis of (a) Ctu1 iKO and (b) Elp3 iKO EPP2 cells, measured using the mass spectrometry (MS) based quantitative analysis of the newly synthesized proteome (QuaNPA) workflow (n = 3 experimental replicates). c Codon-specific changes in ribosome A site occupancy in Ctu1 iKO EPP2 cells, analyzed by diricore. VAA codons (i.e., AAA/CAA/GAA), which are recognized by U34 wobble tRNAs, are highlighted. Data are represented as mean (n = 5 independent experiments); p values were calculated by out-of-frame analysis and are shown for significant increases. d, e Correlation of mRNA codon usage deviation and change in the newly synthesized proteome (NSP) of (d) Ctu1 iKO and (e) Elp3 iKO EPP2 cells (n = 3 experimental replicates). Newly synthesized proteome data are represented as decile ranks of log2FC (i.e., 1 = 10 % most decreased proteins in iKO/Ctrl). In box plots, centre line represents median, upper and lower bounds of the box 75th and 25th percentiles, whiskers 10th to 90th percentiles; p values were calculated by two-tailed Wilcoxon rank test. Grey line represents median codon usage of all quantified proteins. Source data are provided as a Source Data file.

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