A multi-step nucleation process determines the kinetics of prion-like domain phase separation

Erik W. Martin (), Tyler S. Harmon, Jesse B. Hopkins, Srinivas Chakravarthy, J. Jeremías Incicco, Peter Schuck, Andrea Soranno and Tanja Mittag ()
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Erik W. Martin: St. Jude Children’s Research Hospital
Tyler S. Harmon: The Max Planck Institute for the Physics of Complex Systems
Jesse B. Hopkins: Illinois Institute of Technology
Srinivas Chakravarthy: Illinois Institute of Technology
J. Jeremías Incicco: Washington University in St. Louis
Peter Schuck: National Institutes of Health
Andrea Soranno: Washington University in St. Louis
Tanja Mittag: St. Jude Children’s Research Hospital

Nature Communications, 2021, vol. 12, issue 1, 1-12

Abstract: Abstract Compartmentalization by liquid-liquid phase separation (LLPS) has emerged as a ubiquitous mechanism underlying the organization of biomolecules in space and time. Here, we combine rapid-mixing time-resolved small-angle X-ray scattering (SAXS) approaches to characterize the assembly kinetics of a prototypical prion-like domain with equilibrium techniques that characterize its phase boundaries and the size distribution of clusters prior to phase separation. We find two kinetic regimes on the micro- to millisecond timescale that are distinguished by the size distribution of clusters. At the nanoscale, small complexes are formed with low affinity. After initial unfavorable complex assembly, additional monomers are added with higher affinity. At the mesoscale, assembly resembles classical homogeneous nucleation. Careful multi-pronged characterization is required for the understanding of condensate assembly mechanisms and will promote understanding of how the kinetics of biological phase separation is encoded in biomolecules.

Date: 2021
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DOI: 10.1038/s41467-021-24727-z

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