Structural and hydrodynamic properties of an intrinsically disordered region of a germ cell-specific protein on phase separation

Membrane encapsulation is frequently used by the cell to sequester biomolecules and compartmentalize their function. Cells also concentrate molecules into phase-separated protein or protein/nucleic acid "membraneless organelles" that regulate a host of biochemical processes. Here, we use solution NMR spectroscopy to study phase-separated droplets formed from the intrinsically disordered N-terminal 236 residues of the germ-granule protein Ddx4. We show that the protein within the concentrated phase of phase-separated Ddx4, [Formula: see text], diffuses as a particle of 600-nm hydrodynamic radius dissolved in water. However, NMR spectra reveal sharp resonances with chemical shifts showing [Formula: see text] to…

• CI
  Canadian Institutes of Health Research

  Awards: MOP-82928, MOP-133408
• BA
  Biotechnology and Biological Sciences Research Council

  Award: BB/J014346/1