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Sequence-encoded and composition-dependent protein-RNA interactions control multiphasic condensate morphologies.

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Competition between prion-like polypeptides (PLP) and RNA for arginine-rich polypeptides (RRP) drives phase separation in biomolecular condensates. This leads to demixing into distinct PLP and RRP-RNA phases, revealing physical rules for condensate organization.

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Biochemistry

Background:

  • Multivalent interactions between proteins and RNA drive biological phase separation.
  • Biomolecular condensates organize cellular functions through complex molecular networks.
  • Understanding condensate composition and structure is crucial for cell biology.

Purpose of the Study:

  • To investigate the role of competing interactions in multicomponent biomolecular condensates.
  • To elucidate the mechanisms of RNA-induced phase separation and demixing.
  • To establish physical rules governing the spatial organization of multiphasic condensates.

Main Methods:

  • Utilized a ternary system with a prion-like polypeptide (PLP), arginine-rich polypeptide (RRP), and RNA.
  • Analyzed the competition between PLP and RNA for RRP binding.
  • Studied the resulting condensate morphology and phase behavior under varying stoichiometry and interaction strengths.

Main Results:

  • Demonstrated RNA-induced demixing of PLP-RRP condensates into distinct PLP and RRP-RNA phases.
  • Showcased how competition for a shared partner (RRP) dictates condensate composition.
  • Revealed that condensate morphology (non-engulfing, partial, or complete engulfing) depends on RNA-to-RRP ratio and interaction hierarchy.

Conclusions:

  • Established a minimal set of physical rules governing multicomponent, multiphasic biomolecular condensates.
  • Provided insights into the dynamic regulation of condensate composition and structure.
  • Highlighted the importance of competing interactions in generating diverse phase behaviors within cells.