{
  "abstract": "Living cells exhibit a complex organization comprising numerous compartments, among which are RNA- and protein-rich membraneless, liquidlike organelles known as biomolecular condensates. Energy-consuming processes regulate their formation and dissolution, with (de)phosphorylation by specific enzymes being among the most commonly involved reactions. By employing a model system consisting of a phosphorylatable peptide and homopolymeric RNA, and thanks to time-resolved ultra-small-angle x-ray scattering enabling us to probe a wide range of length and time scales, we elucidate how enzymatic activity remodels the growth kinetics and the internal structure of biomolecular condensates. Under a passive condition, we reveal a nucleation-driven coalescence mechanism maintained over four decades in time, similar to the coarsening of simple binary fluid mixtures. Coarse-grained molecular-dynamics simulations show that peptide-decorated RNA chains assembled immediately after mixing constitute the basic subunits. In contrast, actively formed condensates initially display a networklike internal structure, which gradually matures upon dephosphorylation prior to coalescence. Both pathways lead to a steady state, but fluorescence recovery after photobleaching indicates a peptide diffusivity that is twice as high in actively formed condensates consistent with their loosely packed internal structure. This study contributes to linking effectively cellular active processes such as post-translational modifications to the formation and dissolution pathways of membraneless organelles, impacting other fields including synthetic biology.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 10,
  "authors": [
    {
      "name": "Tamizhmalar Sundararajan"
    },
    {
      "name": "Matteo Boccalini"
    },
    {
      "name": "Roméo Suss"
    },
    {
      "name": "Sandrine Mariot"
    },
    {
      "name": "Emerson R da Silva"
    },
    {
      "name": "Fernando C Giacomelli"
    },
    {
      "name": "Austin Hubley"
    },
    {
      "name": "Theyencheri Narayanan"
    },
    {
      "name": "Alessandro Barducci"
    },
    {
      "name": "Guillaume Tresset"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/3cmab8ptj3sng.bib",
  "cited_by": 1,
  "doi": "10.1103/n8nd-sgs6",
  "fulltext_url": null,
  "id": "3cmab8ptj3sng",
  "issns": [
    "2835-8279",
    "2835-8279"
  ],
  "landing_url": "https://hal.science/hal-05796880v1",
  "language": "en",
  "licence": "CC-BY-4.0",
  "licence_label": "CC BY 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "hal",
      "0.phys"
    ],
    [
      "hal",
      "1.phys.phys"
    ],
    [
      "hal",
      "2.phys.phys.phys-bio-ph"
    ],
    [
      "openalex",
      "1312|RNA Research and Splicing"
    ]
  ],
  "openalex": "W7201832083",
  "pdf_url": "https://hal.science/hal-05796880/document",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-08",
  "publisher": "American Physical Society",
  "ris": "https://research.draconitic.com/paper/3cmab8ptj3sng.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:56Z",
      "native_id": "hal-05796880",
      "source": "hal",
      "url": "https://hal.science/hal-05796880v1"
    }
  ],
  "subjects": [
    {
      "field": "physics",
      "origin": "hal:2.phys.phys.phys-bio-ph",
      "subfield": "biological-medical"
    }
  ],
  "title": "Enzymatically Driven Remodeling of Growth Kinetics and Internal Structure in Biomolecular Condensates",
  "title_text": "Enzymatically Driven Remodeling of Growth Kinetics and Internal Structure in Biomolecular Condensates",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:56Z",
  "url": "https://research.draconitic.com/paper/3cmab8ptj3sng",
  "venue": "PRX Life",
  "versions": []
}