Fig. 1: Lack of NatA activity (naa10Δ) causes the downregulation of mitochondrial and ribosomal proteins.

A Scheme of the performed proteome profiling experiments. Yeast were harvested at active growth phase and lysates were digested using the proteome capture aggregation method (PAC) prior High-pH fractionation (HpH). Quantification was performed by using label-free intensities (LFQ; label-free quantitation). n = 3 replicate cultures per condition. B Right: Venn diagram depicting all proteins quantified in the deep proteome profiling from this dataset compared to complete yeast log-phase proteome reported in ref. ³⁶. Left: Venn diagram depicting numbers of all proteins quantified in the deep proteome profiling, (Proteome, n = 4330). C Differential expression profiling of the WT and naa10Δ strains in a volcano plot. Significant regulated proteins at 1% and 5% false discovery rate (FDR) are delimited by dashed and solid lines, respectively (FDR controlled, two-sided t test, randomizations = 250, s0 = 0.1). Ribosomal proteins from large (RPL) and small subunit (RPS) are colored in blue and green, respectively. D Violin plot of the cellular component (CC) gene ontology annotation of the log10 fold detected proteome ratios. Kruskal–Wallis test with two-sided Wilcoxon post hoc test, multiple test correction according to Benjamin–Hochberg, ns P > 0.05, *P < = 0.05, **P < = 0.01, ***P < = 0.001, ****P < = 0.0001; box bounds correspond to quartiles of the distribution (center: median; limits: 1st and 3rd quartile; whiskers: +/− 1.5 IQR). (n  =  3, n = independent cultures per condition). Source data are provided as a Source Data file (B–D).