RNA length has a non-trivial effect in the stability of biomolecular condensates formed by RNA-binding proteins
Fig 4
Density of LLPS-stabilizing intermolecular contacts within condensates as a function of RNA length plotted separately for protein–protein interactions (black symbols) and protein–RNA interactions (green symbols) for FUS–polyU (a) and PR25–polyU mixtures (b). The temperature at which the intermolecular contacts were computed was T/Tc,FUS = 0.99 for FUS–RNA systems, and T/Tc,FUS = 0.85 for PR25–RNA mixtures. Error bars depict the computed standard deviation in the number of molecular contacts. (c) Representative snapshot of a bulk FUS–polyU condensate to illustrate the employed cut-off distance (Rc) criterion to identify protein--protein and protein--RNA contacts. The same color code described in Fig 1 applies here. (d) Critical temperature versus RNA length for FUS–RNA (red) and PR25–RNA (blue) systems. The RNA/protein mass ratio of all systems was kept constant at 0.096 for FUS–RNA systems and at 1.20 for PR25–RNA mixtures.