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Arginine multivalency stabilizes protein/RNA condensates.

Matteo Paloni1, Giovanni Bussi2, Alessandro Barducci1

  • 1Centre de Biochimie Structurale (CBS), INSERM, CNRS, Université de Montpellier, Montpellier, France.

Protein Science : a Publication of the Protein Society
|May 13, 2021
PubMed
Summary
This summary is machine-generated.

Arginine drives biomolecular condensate formation more effectively than lysine by forming more specific interactions with RNA. This explains how amino acid sequence influences cellular organization through liquid-liquid phase separation (LLPS).

Keywords:
RNA/protein interactioncoacervatesliquid-liquid phase separationmolecular dynamics simulations

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Biomolecular condensates, formed via liquid-liquid phase separation (LLPS), are crucial for cellular organization.
  • LLPS relies on multivalent interactions between flexible biomolecules like proteins and RNA.
  • The specific roles of amino acids in driving LLPS are not fully understood.

Purpose of the Study:

  • To investigate the microscopic origins of differential propensities of arginine and lysine in driving protein/RNA liquid-liquid phase separation (LLPS).
  • To provide a molecular-level understanding of how amino acid sequence influences the formation of biomolecular condensates.

Main Methods:

  • Explicit-solvent atomistic molecular dynamics simulations.
  • Investigated mixtures of polyU oligonucleotides with polyR/polyK peptides.
  • Analyzed intermolecular contacts and binding affinities.

Main Results:

  • Arginine demonstrated a higher affinity for polyU than lysine under various concentrations.
  • Arginine side chains formed more specific interactions (hydrogen bonds, stacking) with oligonucleotides.
  • The multivalency of the arginine guanidinium group facilitates simultaneous coordination of multiple RNA groups.

Conclusions:

  • Arginine's unique chemical properties enhance its ability to stabilize protein/RNA condensates compared to lysine.
  • This study elucidates the molecular basis for arginine's role in driving LLPS and cellular organization.