{
  "abstract": "Membrane compartmentalization plays a fundamental role in cellular organization, yet the mechanisms underlying it in prokaryotes remain poorly understood. Here, we investigate MurG, an essential membrane-associated N-acetylglucosamine transferase involved in peptidoglycan biosynthesis and conserved across Gram-positive and Gram-negative bacteria. Combining theoretical thermodynamic modeling with experimental high-speed atomic force and fluorescence microscopy, we show that MurG induces membrane partitions independently of lipid segregation, supporting a mechanism of protein-driven membrane organization. In addition, we show that the lateral mobility and spatial distribution of MurG are strongly influenced by membrane fluidity. These MurG-dependent partitions closely resemble the Regions of Increased Fluidity (RIFs), whose molecular origin had remained unclear. Notably, antibiotics alter MurG domain organization and dynamics, linking membrane partitioning to antibiotic exposure. Altogether, our findings reveal a close interplay between protein clustering, membrane dynamics, and lipid bilayer physical properties, providing new insights into the mechanisms underlying membrane compartmentalization in bacteria.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 7,
  "authors": [
    {
      "name": "Elodie Lafargue"
    },
    {
      "name": "Carlos Marcuello"
    },
    {
      "name": "Thomas M Wood"
    },
    {
      "name": "Nathaniel I Martin"
    },
    {
      "name": "Adai Colom"
    },
    {
      "name": "Marcelo E Guerin"
    },
    {
      "name": "Ignacio Casuso"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/4h3jpccq708s9.bib",
  "cited_by": 0,
  "doi": null,
  "fulltext_url": null,
  "id": "4h3jpccq708s9",
  "issns": [],
  "landing_url": "https://hal.science/hal-05854738v1",
  "language": "en",
  "licence": "CC-BY-NC-4.0",
  "licence_label": "CC BY-NC 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nc/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "hal",
      "0.phys"
    ],
    [
      "hal",
      "0.sde"
    ]
  ],
  "openalex": null,
  "pdf_url": "https://hal.science/hal-05854738/document",
  "pmcid": null,
  "pmid": null,
  "published": "2026-11-06",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/4h3jpccq708s9.ris",
  "sources": [
    {
      "first_seen": "2026-11-07T12:20:25Z",
      "native_id": "hal-05854738",
      "source": "hal",
      "url": "https://hal.science/hal-05854738v1"
    }
  ],
  "subjects": [
    {
      "field": "earth",
      "origin": "hal:0.sde",
      "subfield": "environmental-science"
    },
    {
      "field": "physics",
      "origin": "hal:0.phys",
      "subfield": "general"
    }
  ],
  "title": "MurG self-organizes into distinct protein-induced microdomains within fluid lipid membranes",
  "title_text": "MurG self-organizes into distinct protein-induced microdomains within fluid lipid membranes",
  "type": "preprint",
  "updated_at": "2026-11-08T12:20:49Z",
  "url": "https://research.draconitic.com/paper/4h3jpccq708s9",
  "venue": "HAL",
  "versions": []
}