Understanding how coacervation of two viral proteins drives the formation of membrane- less compartments
Recent studies have shown that micron-scale membrane-less compartments have typical properties of liquids and are formed by liquid-liquid phase separation (Hyman 2014). The separation is typically induced by multivalent interactions between proteins composed of multiple modular interaction domains and/or proteins containing intrinsically disordered regions (IDRs), or by RNA or DNA molecules that provide multiple binding sites for other nucleic acid molecules or proteins (Brangwynne 2015; Banani 2017). It results in the co-existence of a condensed phase in which the interacting macromolecules are concentrated and a second phase in which they are diluted. However, little is known about the organisation of the condensed liquid phase, about its physicochemical properties or about the dependence of the
process on the nature of the attractive interactions, their valence, interaction strength, and
Our primary goal is to reconstitute this biological coacervation process in vitro with highly purified proteins and to investigate the role of different solution parameters on this process. The overall goal is to use neutron scattering and neutron diffraction experiments on different instruments at the ILL to probe these molecular processes at different time and length scales and to use complementary methods to better understand the assembly of intracellular membrane-less compartments and to decipher the aspects of protein chemistry and of polymer physics that lead to liquid-like states. This multidisciplinary project is at the interface between soft-matter physics and biophysics (biochemistry) and it relies on a collaboration between a team at the IBS and a team of the Large Scale Structure group at the ILL.