{
  "abstract": "Proteins can diffuse micrometers in seconds, yet bacterial cells are able to maintain stable protein gradients. The best studied bacterial protein gradient is the Min system of Escherichia coli. In rod-shaped bacteria the MinCD proteins prevent formation of minicells by inhibiting FtsZ polymerization close to the cell poles. In E. coli these proteins oscillate between cell poles within a minute, resulting in an increased MinCD concentration at the poles. This oscillation is caused by the interaction between MinD and the protein MinE, which form an ATP-driven reaction-diffusion system, whereby the ATPase MinD cycles between a monomeric cytosolic and a dimeric membrane attached states. Bacillus subtilis also has MinCD, but lacks MinE. In this case MinCD form a static gradient that requires the transmembrane protein MinJ, located at cell poles and cell division sites. A recent reaction-diffusion model was successful in recreating the MinD gradient in B. subtilis, assuming that MinD cycles between cytosol and membrane, like in E. coli. Here we show that the monomeric and dimeric states of B. subtilis MinD have comparable membrane affinities, that MinD interacts with MinJ as a dimer, and that MinJ is not required for membrane localization of MinD. Based on these new findings we tested different models, using kinetic Monte Carlo simulations, and found that a difference in diffusion rate between the monomer and dimer, rather than a difference in membrane affinity, is important for B. subtilis MinCD gradient formation.",
  "abstract_shown": true,
  "affiliations": [
    "FIND, Geneva, Switzerland",
    "The Bacterial Cell Biology, Swammerdam Institute for Life Sciences, University of Amsterdam, Amsterdam, The Netherlands",
    "The Centre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle upon Tyne, United Kingdom",
    "SUPA, School of Physics and Astronomy, The University of Edinburgh, Edinburgh, Scotland, United Kingdom",
    "Carl Zeiss Meditec AG, Jena, Germany",
    "MRC Laboratory of Molecular Biology, Structural Studies Division, Cambridge, UK"
  ],
  "article_type": null,
  "arxiv": null,
  "author_total": 6,
  "authors": [
    {
      "affs": [
        0,
        1
      ],
      "name": "Laura C. Bohórquez",
      "orcid": "0000-0001-6698-395X"
    },
    {
      "affs": [
        2
      ],
      "name": "Henrik Strahl",
      "orcid": "0000-0003-4416-2178"
    },
    {
      "affs": [
        3
      ],
      "name": "Davide Marenduzzo",
      "orcid": "0000-0003-3974-4915"
    },
    {
      "affs": [
        4,
        2
      ],
      "name": "Martin J. Thiele"
    },
    {
      "affs": [
        5,
        2
      ],
      "name": "Frank Bürmann",
      "orcid": "0000-0002-9428-0933"
    },
    {
      "affs": [
        1
      ],
      "name": "Leendert Willem Hamoen",
      "orcid": "0000-0001-9251-1403"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/7v927m3e03q4y.bib",
  "cited_by": 10,
  "doi": "10.7554/elife.101520.4",
  "fulltext_url": null,
  "id": "7v927m3e03q4y",
  "issns": [
    "2050-084X"
  ],
  "landing_url": "https://doi.org/10.7554/elife.101520.4",
  "language": "en",
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "journal",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "openalex",
      "1311|Bacterial Genetics and Biotechnology"
    ]
  ],
  "openalex": "W4399593935",
  "pdf_url": null,
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-02",
  "publisher": "eLife Sciences Publications Ltd",
  "ris": "https://research.draconitic.com/paper/7v927m3e03q4y.ris",
  "sources": [
    {
      "first_seen": "2026-11-04T13:21:07Z",
      "native_id": "W4399593935",
      "source": "openalex",
      "url": "https://doi.org/10.7554/elife.101520.4"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "openalex:1311|Bacterial Genetics and Biotechnology",
      "subfield": "genetics-genomics"
    }
  ],
  "title": "Membrane affinity difference between MinD monomer and dimer is not crucial for MinD gradient formation in Bacillus subtilis",
  "title_text": "Membrane affinity difference between MinD monomer and dimer is not crucial for MinD gradient formation in Bacillus subtilis",
  "type": "peer-reviewed",
  "updated_at": "2026-11-09T13:21:07Z",
  "url": "https://research.draconitic.com/paper/7v927m3e03q4y",
  "venue": "eLife",
  "versions": []
}