{
  "abstract": "Ring-shaped helicases must be opened and loaded onto DNA to initiate genome replication. In bacteria, most species lack canonical AAA+ helicase loaders and instead rely on DciA, an evolutionarily conserved, ATP-independent factor whose mechanism has remained unclear. Here we define how DciA remodels the bacterial replicative helicase DnaB. A 3.5 Å cryo-EM structure reveals a DnaB6·DciA3 complex in which DciA binds the periphery of the helicase and stabilizes a right-handed open-helical conformation with a single cracked interface. Three DciA molecules dock onto alternate linker-helix/docking-helix modules, while one N-terminal domain (NTD) engages the cracked interface, occupying the pocket vacated by the displaced linker helix and acting as a wedge to promote ring opening. Functional analyses reveal how DciA couples ATPase suppression with efficient helicase loading through coordinated actions of its NTDs and C-terminal domains. Together, these findings define a minimal, ATP-independent mechanism for helicase loading and show how an ancestral loader remodels DnaB to overcome a fundamental topological barrier.",
  "abstract_shown": true,
  "affiliations": [
    "Centro de Investigaciones Biológicas Margarita Salas, CSIC , 28040 Madrid ,"
  ],
  "article_type": "research article",
  "arxiv": null,
  "author_total": 2,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Lidia Araújo-Bazán",
      "orcid": "0000-0002-8750-7706"
    },
    {
      "affs": [
        0
      ],
      "name": "Ernesto Arias-Palomo",
      "orcid": "0000-0002-2706-7411"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/4kyzj49x3y0pq.bib",
  "cited_by": 0,
  "doi": "10.1093/nar/gkag977",
  "fulltext_url": "https://europepmc.org/articles/PMC13696075",
  "id": "4kyzj49x3y0pq",
  "issns": [
    "0305-1048",
    "1362-4962"
  ],
  "landing_url": "https://academic.oup.com/nar/article/doi/10.1093/nar/gkag977/8959889",
  "language": "eng",
  "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": [
    [
      "openalex",
      "1311|Bacterial Genetics and Biotechnology"
    ]
  ],
  "openalex": "W7223563939",
  "pdf_url": "https://academic.oup.com/nar/article-pdf/54/19/gkag977/72218644/gkag977.pdf",
  "pmcid": "PMC13696075",
  "pmid": "42927770",
  "published": "2026-10-01",
  "publisher": "Oxford University Press (OUP)",
  "ris": "https://research.draconitic.com/paper/4kyzj49x3y0pq.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:18:50Z",
      "native_id": "10.1093/nar/gkag977",
      "source": "crossref",
      "url": "https://academic.oup.com/nar/article/doi/10.1093/nar/gkag977/8959889"
    },
    {
      "first_seen": "2026-10-30T12:21:18Z",
      "native_id": "MED:42927770",
      "source": "europepmc",
      "url": "https://europepmc.org/article/MED/42927770"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "openalex:1311|Bacterial Genetics and Biotechnology",
      "subfield": "genetics-genomics"
    }
  ],
  "title": "Structural basis of DnaB ring opening by the ancestral helicase loader DciA",
  "title_text": "Structural basis of DnaB ring opening by the ancestral helicase loader DciA",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:21:18Z",
  "url": "https://research.draconitic.com/paper/4kyzj49x3y0pq",
  "venue": "Nucleic Acids Research",
  "versions": []
}