Partial demixing of RNA-protein complexes leads to intradroplet patterning in phase-separated biological condensates.

ABSTRACT: An emerging mechanism for intracellular organization is liquid-liquid phase separation (LLPS). Found in both the nucleus and the cytoplasm, liquidlike droplets condense to create compartments that are thought to promote and inhibit specific biochemistry. In this work, a multiphase, Cahn-Hilliard diffuse interface model is used to examine RNA-protein interactions driving LLPS. We create a bivalent system that allows for two different species of protein-RNA complexes and model the competition that arises for a shared binding partner, free protein. With this system we demonstrate that the binding and unbinding of distinct RNA-protein complexes leads to diverse spatial pattern formation and dynamics within droplets. Both the initial formation and transient behavior of spatial patterning are su

SUBMITTER: Gasior K 

PROVIDER: S-EPMC6739070 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature