Fig. 7: The ampholytic nature of the motif drives protein aggregation upon depletion of U34-enzymes.
From: Wobble tRNA modification and hydrophilic amino acid patterns dictate protein fate
a, b Axial forces profile on nascent chain caused by the electrostatic interaction in the ribosome exit tunnel (a) wild-type KIF4A; (b) ERRRK deleted KIF4A. The axial forces profiles and local mechanical work acting on the two chains are different upon incorporation of residues 596–646 at the peptidyl-transferase center (PTC). Schematic representation of ribosome–protein interaction, on the left. c Anti-Flag immunofluorescence of MCF7 cells depleted or not of ELP3 and overexpressing KIF4A-WT or KIF4A-Del in control or after 6 h of treatment with 100 μM chloroquine. Arrows depict KIF4A aggregates (n = 2 replicates). d Amyloid aggregation profiles of KIF4A-WT and KIF4A-Del calculated by using the TANGO algorithm.
