{
  "abstract": "Influenza virus polymerase transcribes or repli- cates the segmented RNA genome (vRNA) into respectively viral mRNA or full-length copies and ini- tiates RNA synthesis by binding the conserved 30 and 50 vRNA ends (the promoter). In recent structures of promoter-bound polymerase, the cap-binding and endonuclease domains are configured for cap snatching, which generates capped transcription primers. Here, we present a FluB polymerase struc- ture with a bound complementary cRNA 50 end that exhibits a major rearrangement of the subdomains within the C-terminal two-thirds of PB2 (PB2-C). Notably, the PB2 nuclear localization signal (NLS)- containing domain translocates 90 A˚ to bind to the endonuclease domain. FluA PB2-C alone and RNA-free FluC polymerase are similarly arranged. Biophysical and cap-dependent endonuclease as- says show that in solution the polymerase explores different conformational distributions depending on which RNA is bound. The inherent flexibility of the po- lymerase allows it to adopt alternative conformations that are likely important during polymerase matura- tion into active progeny RNPs.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 13,
  "authors": [
    {
      "name": "Eric Thierry"
    },
    {
      "name": "Delphine Guilligay"
    },
    {
      "name": "Jan Kosinski"
    },
    {
      "name": "Thomas Bock"
    },
    {
      "name": "Stephanie Gaudon"
    },
    {
      "name": "Adam Round"
    },
    {
      "name": "Alexander Pflug"
    },
    {
      "name": "Narin Hengrung"
    },
    {
      "name": "Kamel El Omari"
    },
    {
      "name": "Florence Baudin"
    },
    {
      "name": "Darren J Hart"
    },
    {
      "name": "Martin Beck"
    },
    {
      "name": "Stephen Cusack"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/70axswmg0rm9s.bib",
  "cited_by": 150,
  "doi": "10.1016/j.molcel.2015.11.016",
  "fulltext_url": null,
  "id": "70axswmg0rm9s",
  "issns": [
    "1097-2765",
    "1097-4164"
  ],
  "landing_url": "https://hal.science/hal-05797560v1",
  "language": "en",
  "licence": "CC-BY-NC-ND-4.0",
  "licence_label": "CC BY-NC-ND 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nc-nd/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "hal",
      "0.sdv"
    ],
    [
      "openalex",
      "2713|Influenza Virus Research Studies"
    ]
  ],
  "openalex": "W2238439239",
  "pdf_url": "https://hal.science/hal-05797560/document",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-13",
  "publisher": "Cell Press",
  "ris": "https://research.draconitic.com/paper/70axswmg0rm9s.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:56Z",
      "native_id": "hal-05797560",
      "source": "hal",
      "url": "https://hal.science/hal-05797560v1"
    }
  ],
  "subjects": [
    {
      "field": "medicine",
      "origin": "openalex:2713|Influenza Virus Research Studies",
      "subfield": "epidemiology-public-health"
    }
  ],
  "title": "Influenza Polymerase Can Adopt an Alternative Configuration Involving a Radical Repacking of PB2 Domains",
  "title_text": "Influenza Polymerase Can Adopt an Alternative Configuration Involving a Radical Repacking of PB2 Domains",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:56Z",
  "url": "https://research.draconitic.com/paper/70axswmg0rm9s",
  "venue": "Molecular Cell",
  "versions": []
}