Fig. 1: Nup98 aggregation propensity depends on the primary sequence.

a Representation of the prion-like domain (PrD-like) propensity⁶⁷ (black line) of Nup98 together with the distribution of specific residues over the sequence (hydrophobic, ILVM, orange; aromatic, FYW, purple; positively charged, KRH, blue; negatively charged, ED, red; polar with amide, QN, pink; polar with hydroxyl, ST, green; glycine, dark yellow; proline, gray; alanine, light green; cysteine, dark purple). b Amino acid sequence of the N-terminal part of Nup98 highlighting FG (red text) and LF (orange background) motifs. c Average aggregation per residue based on the aggregation of the analyzed peptides by NMR after one day at 5 °C with 2 mM peptide concentration. The sequences of the more aggregating peptides are represented with the residue colors from (a). d Cryo-EM structure (PDB-ID 7Q64) of the main polymorph formed by the first aggregation peptide Nup98^FG(85-124). e Solvation energy over the sequence of the Nup98^FG(85-124) peptide. LF motifs are represented into squares and the residue selected for mutation (F102) is highlighted in red. Each independent value from each of the three peptides is represented in blue. The error bars represent the standard deviation. f Structure of the aggregated Nup98^FG(85-124) peptide with solvation energy in blue-red color code. Initial and last residues of each peptide are labeled. The mutated residue (F102) is highlighted in black. Source data are provided as a Source Data file.