{
  "abstract": "The bacterial actin homolog MreB plays a key role in rod cell shape determination. We recently showed that MreB from the Gram-positive bacterium Geobacillus stearothermophilus (MreBGs) polymerizes into straight pairs of protofilaments in the presence of both ATP and a lipid surface. Membrane interaction is thought to be mediated by electrostatic interactions with anionic lipids, with final anchoring relying on two spatially close hydrophobic motifs that protrude from the MreBGs monomers, forming a putative membrane-insertion domain. Here, we determined the binding properties of ATP and ADP to MreBGs using fluorescence anisotropy and monitored ATP-mediated binding and polymer formation on lipid bilayers using liposome-binding assays and atomic force microscopy, respectively. Finally, we used solid-state NMR to visualize the interaction between the membrane and MreBGs at the atomic level. Our findings reveal that divalent cations are required for nucleotide binding and that, unlike eukaryotic actin, MreBGs has similar affinity for both ATP and ADP. We also show that monomeric MreBGs establishes peripheral contacts with the membrane likely through electrostatic interactions, while Mg⋅ATP-induced MreBGs filaments insert into the lipid bilayer without interfering with the membrane lamellar phase and have a significant local fluidifying effect.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 11,
  "authors": [
    {
      "name": "Ingrid E Adriaans"
    },
    {
      "name": "Ana Álvarez-Mena"
    },
    {
      "name": "Céline Dinet"
    },
    {
      "name": "Estelle Morvan"
    },
    {
      "name": "Kee Siang Lim"
    },
    {
      "name": "Erick J Dufourc"
    },
    {
      "name": "Richard Wong"
    },
    {
      "name": "Arnaud Chastanet"
    },
    {
      "name": "Alphée Michelot"
    },
    {
      "name": "Rut Carballido-López"
    },
    {
      "name": "Birgit Habenstein"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/1dhyre5zz0xv0.bib",
  "cited_by": 1,
  "doi": "10.1016/j.bpj.2026.06.003",
  "fulltext_url": null,
  "id": "1dhyre5zz0xv0",
  "issns": [
    "0006-3495",
    "1542-0086"
  ],
  "landing_url": "https://hal.science/hal-05784575v1",
  "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.sdv"
    ],
    [
      "openalex",
      "1312|Lipid Membrane Structure and Behavior"
    ]
  ],
  "openalex": "W7163408868",
  "pdf_url": "https://hal.science/hal-05784575/document",
  "pmcid": null,
  "pmid": "42237545",
  "published": "2026-06-03",
  "publisher": "Biophysical Society",
  "ris": "https://research.draconitic.com/paper/1dhyre5zz0xv0.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:50Z",
      "native_id": "hal-05784575",
      "source": "hal",
      "url": "https://hal.science/hal-05784575v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Lipid Membrane Structure and Behavior",
      "subfield": "molecular-biology"
    }
  ],
  "title": "ATP-driven membrane binding and polymerization of bacterial actin MreB promotes local membrane fluidization",
  "title_text": "ATP-driven membrane binding and polymerization of bacterial actin MreB promotes local membrane fluidization",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:50Z",
  "url": "https://research.draconitic.com/paper/1dhyre5zz0xv0",
  "venue": "Biophysical Journal",
  "versions": []
}