Fig. 5: Thermal stability of translation-related and ribosomal proteins is affected stronger than their abundance.

a Scatter plot of abundance and stability values for proteins involved in translation and chaperoning functions for T1 (30 min LB), T2 (30 min TET), and T4 (3 h TET) respectively, comparing K-12 scores (x-axis) against ED1a scores (y-axis). A two-sided t-test was applied based on the effect size distribution resulting from the respective K-12 vs. ED1a scores. P values were adjusted using the Benjamini-Hochberg method. Each dot represents a protein; orange and red coloring indicates a significant difference between K-12 and ED1a scores (P_adj < 0.05, confidence interval 0.95). Exact p values for each protein can be found in Supplementary Data 1. b Scatter plot of abundance (blue) and stability values (green) for ribosomal proteins for T1 (30 min LB), T2 (30 min TET), and T4 (3 h TET) comparing K-12 scores (x-axis) against ED1a scores (y-axis). Each dot represents a protein. The two insets in each plot depict 70 S ribosome structures shaded according to the respective thermal stability score values of the respective protein components (upper left corner: coloring based on ED1a scores; lower right corner: coloring based on K-12 scores). The PDB model was combined from coordinates fetched from PDB 3J7Z, PDB 7K00, and PDB 6H4N. Proteins with increased stability are colored turquoise, proteins with decreased stability are colored tan, and proteins with unchanged stability are colored white.