ArticlePLoS computational biology2022
RNA length has a non-trivial effect in the stability of biomolecular condensates formed by RNA-binding proteins.
Article in PLoS computational biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed.
- Recognition of multimolecular G-quadruplex regulates phase separation of cockayne syndrome B.Nucleic acids research · 2026Article
- Nucleotide-Specific RNA Conformations and Dynamics as Precursors to Ribonucleoprotein Condensates.Journal of the American Chemical Society · 2025Article
- Phosphorylation Changes SARS-CoV-2 Nucleocapsid Protein's Structural Dynamics and Its Interaction With RNA.Proteins · 2025Article
- Direct Observation of the Conformational Transitions in Tau and Their Correlation with Phase Behavior.JACS Au · 2025Article
- Charged peptides enriched in aromatic residues decelerate condensate ageing driven by cross-β-sheet formation.Nature communications · 2025Article
- Chemically Informed Coarse-Graining of Electrostatic Forces in Charge-Rich Biomolecular Condensates.ACS central science · 2025Article
- Modeling biomolecular condensates across scales: Atomistic, coarse-grained, and data-driven approaches.Advances in physics: X · 2025Article
- Benchmarking residue-resolution protein coarse-grained models for simulations of biomolecular condensates.PLoS computational biology · 2025Article
- The Effect of Dipeptide Repeat Proteins on FUS/TDP43-RNA Condensation in C9orf72 ALS/FTD.The journal of physical chemistry. B · 2024Article
- Fundamental Aspects of Phase-Separated Biomolecular Condensates.Chemical reviews · 2024Review
- Capturing chemical reactions inside biomolecular condensates with reactive Martini simulations.Communications chemistry · 2024Article
- Aromatic and arginine content drives multiphasic condensation of protein-RNA mixtures.Biophysical journal · 2024Article
- The disordered N-terminal tail of SARS-CoV-2 Nucleocapsid protein forms a dynamic complex with RNA.Nucleic acids research · 2024Article
- Specific protein-RNA interactions are mostly preserved in biomolecular condensates.Science advances · 2024Article
- Direct prediction of intrinsically disordered protein conformational properties from sequence.Nature methods · 2024Article
- Location and Concentration of Aromatic-Rich Segments Dictates the Percolating Inter-Molecular Network and Viscoelastic Properties of Ageing Condensates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Surfactants or scaffolds? RNAs of varying lengths control the thermodynamic stability of condensates differently.Biophysical journal · 2023Article
- Article
- Time-Dependent Material Properties of Aging Biomolecular Condensates from Different Viscoelasticity Measurements in Molecular Dynamics Simulations.The journal of physical chemistry. B · 2023Article
- The effect of polymer length in liquid-liquid phase separation.Cell reports. Physical science · 2023Article
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4 authors.
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Abstract
Biomolecular condensates formed via liquid-liquid phase separation (LLPS) play a crucial role in the spatiotemporal organization of the cell material. Nucleic acids can act as critical modulators in the stability of these protein condensates. To unveil the role of RNA length in regulating the stability of RNA binding protein (RBP) condensates, we present a multiscale computational strategy that exploits the advantages of a sequence-dependent coarse-grained representation of proteins and a minimal coarse-grained model wherein proteins are described as patchy colloids. We find that for a constant nucleotide/protein ratio, the protein fused in sarcoma (FUS), which can phase separate on its own-i.e., via homotypic interactions-only exhibits a mild dependency on the RNA strand length. In contrast, the 25-repeat proline-arginine peptide (PR25), which does not undergo LLPS on its own at physiological conditions but instead exhibits complex coacervation with RNA-i.e., via heterotypic interactions-shows a strong dependence on the length of the RNA strands. Our minimal patchy particle simulations suggest that the strikingly different effect of RNA length on homotypic LLPS versus RBP-RNA complex coacervation is general. Phase separation is RNA-length dependent whenever the relative contribution of heterotypic interactions sustaining LLPS is comparable or higher than those stemming from protein homotypic interactions. Taken together, our results contribute to illuminate the intricate physicochemical mechanisms that influence the stability of RBP condensates through RNA inclusion.
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