TY - JOUR T1 - Sequence-encoded and Composition-dependent Protein-RNA Interactions Control Multiphasic Condensate Morphologies JF - bioRxiv DO - 10.1101/2020.08.30.273748 SP - 2020.08.30.273748 AU - Taranpreet Kaur AU - Muralikrishna Raju AU - Ibraheem Alshareedah AU - Richoo B. Davis AU - Davit A. Potoyan AU - Priya R. Banerjee Y1 - 2020/01/01 UR - http://biorxiv.org/content/early/2020/12/10/2020.08.30.273748.abstract N2 - Multivalent protein-protein and protein-RNA interactions are the drivers of biological phase separation. Biomolecular condensates typically contain a dense network of multiple proteins and RNAs, and their competing molecular interactions play key roles in regulating the condensate composition and structure. Employing a ternary system comprising of a prion-like polypeptide (PLP), arginine-rich polypeptide (RRP), and RNA, we show that competition between the PLP and RNA for a single shared partner, the RRP, leads to RNA-induced demixing of PLP-RRP condensates into stable coexisting phases−homotypic PLP condensates and heterotypic RRP-RNA condensates. The morphology of these biphasic condensates (non-engulfing/ partial engulfing/ complete engulfing) is determined by the RNA-to-RRP stoichiometry and the hierarchy of intermolecular interactions, providing a glimpse of the broad range of multiphasic patterns that are accessible to these condensates. Our findings provide a minimal set of physical rules that govern the composition and spatial organization of multicomponent and multiphasic biomolecular condensates.Competing Interest StatementThe authors have declared no competing interest. ER -