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Fused in sarcoma undergoes cold denaturation: Implications for phase separation.

Sara S Félix1,2,3, Douglas V Laurents3, Javier Oroz3

  • 1UCIBIO, Department of Chemistry, NOVA School of Science and Technology, Universidade NOVA de Lisboa, Caparica, Portugal.

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Summary

Metabolites and cold stress influence the liquid-liquid phase separation (LLPS) of full-length fused in sarcoma (FUS) protein. FUS folded domains, particularly the zinc-finger domain, undergo cold denaturation, promoting LLPS and stress granule assembly.

Keywords:
cold denaturationcold stressfused in sarcoma (FUS)liquid-liquid phase separation (LLPS)nuclear magnetic resonance (NMR)

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Liquid-liquid phase separation (LLPS) of fused in sarcoma (FUS) protein is primarily linked to its disordered domains and is temperature-dependent.
  • The contribution of FUS folded domains to LLPS is not well understood due to studies often using fragmented domains.

Purpose of the Study:

  • To investigate the impact of metabolites on full-length (FL) FUS LLPS.
  • To explore the behavior of FUS folded domains under varying conditions using biophysical techniques.
  • To elucidate the role of FUS globular domains in LLPS, especially under cold stress.

Main Methods:

  • Turbidity assays and differential interference contrast (DIC) microscopy to study FL FUS LLPS.
  • Nuclear magnetic resonance (NMR) spectroscopy to analyze the conformational behavior of FUS folded domains.
  • Investigating the effect of various metabolites (glucose, glutamate, NaCl, Zn2+, Ca2+) and pH on FUS LLPS.

Main Results:

  • FL FUS LLPS is modulated by metabolite concentrations, with optimal LLPS observed at low glucose and glutamate levels, moderate salt and divalent cation concentrations, and isoelectric pH.
  • The FUS RNA recognition motif (RRM) and zinc-finger (ZnF) domains exhibit cold denaturation above 0°C, influenced by the ZnF domain's stability.
  • Cold unfolding of FUS domains exposes hydrophobic residues, facilitating LLPS-promoting interactions.

Conclusions:

  • FUS folded domains play an active role in LLPS under cold stress conditions.
  • These findings provide novel insights into the environmental regulation of FUS LLPS.
  • The study suggests a mechanism for FUS involvement in stress granule assembly via cold-induced domain behavior.