Figure 5.

Protein aggregation in nat1Δ and map1Δ strains. (A) Alterations in protein association levels of various components of Nat complexes to the ribosome were assessed by mass spectrometry and quantified by Max Quant. Changes in ribosome-association are shown as log₂-fold changes. Names of protein constituting the complexes are given below. Asterisks indicate the significance of fold changes (* P ≤ 0.05, ** P ≤ 0.01). (B) Relative levels of acetylated N-termini in ΔES27Lb cells as compared to wildtype cells. All proteins for which N-terminal peptides could be reliably detected in the MS dataset were tested for their acetylation status which was further quantified. Data is shown as log₂ fold change. Each dot represents a single protein. The P-value signifies the significance of the shift of distribution of acetylation frequencies between wildtype and ΔES27Lb. The box highlights the group of proteins with significantly reduced acetylation levels in the ΔES27Lb strain. (C) SDS polyacrylamide gel of aggregated proteins isolated from the ΔES27Lb strain or from cells chromosomally lacking Map1 (map1Δ) or Nat1 (nat1Δ). Coomassie-stained proteins from total lysates serve as loading control (input). Bar graph on the right shows quantifications of aggregates normalized to ΔES27Lb. Data are mean ± SD.