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Emergence of order in condensates composed of multi-valent, multi-domain proteins

Many RNA-binding proteins (RBPs) that assemble into membraneless organelles, have a common architecture including disordered prion-like domain (PLD) and folded RNA-binding domain (RBD). An enrichment of PLD within the condensed phase gives rise to formation, on longer time scales, amyloid-like fibrils (aging). In this study, we employ coarse-grained Langevin dynamics simulations to explore the physical basis for the structural diversity in condensed phases of multi-domain RBPs. We discovered a highly cooperative first order transition between disordered (liquid-like) structures and an ordered (solid-like) phase whereby chains of PLD organize in fibrils with high nematic orientational order. Cooperativity of this liquid-solid transition makes fibril formation highly malleable to mutations or post-translational modifications. An interplay between homo-domain (PLD-PLD) and hetero-domain (PLD-RBD) interactions results in variety of structures with distinct spatial architectures. Our results provide a mechanistic understanding of how multi-domain RBPs could form assemblies with distinct structural and, potentially, material properties.