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Dynamic yet well-defined organization of the FUS RGG3 dense phase.

Anton A Polyansky1,2, Benjamin Frühbauer3,4, Bojan Žagrović5,6

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Intrinsically disordered protein regions (IDRs) form biomolecular condensates through dynamic interactions. Microsecond simulations reveal how transient molecular events create large-scale organization in these essential cellular structures.

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Area of Science:

  • Biochemistry
  • Biophysics
  • Cell Biology

Background:

  • Intrinsically disordered protein regions (IDRs) are crucial for forming biomolecular condensates, essential for cellular compartmentalization.
  • The microscopic mechanisms governing IDR behavior within condensates are not fully understood.

Purpose of the Study:

  • To investigate the atomistic details of IDR behavior in a dense phase using molecular dynamics simulations.
  • To elucidate the relationship between molecular interactions and the emergent large-scale organization of biomolecular condensates.

Main Methods:

  • Microsecond-level molecular dynamics simulations of a model dense phase.
  • Atomistic resolution analysis of a 73-residue arginine- and glycine-rich IDR (RGG3) from FUS protein.
  • Fractal formalism to analyze the multi-scale topology of protein clusters.

Main Results:

  • RGG3 IDRs exhibit dynamic behavior in the dense phase with minimal loss of configurational entropy and only a slight decrease in diffusion.
  • Despite transient interactions and heterogeneous interfaces, RGG3 forms statistically defined motifs and a multi-scale topology.
  • Analysis of bound water suggests a significant contribution of solvent entropy to condensate formation thermodynamics.

Conclusions:

  • A well-defined, multi-scale organization of disordered protein condensates emerges from heterogeneous, transient molecular interactions.
  • Solvent entropy plays a key role in the thermodynamics of biomolecular condensate formation.
  • Understanding IDR dynamics provides insights into cellular compartmentalization mechanisms.