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The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding

Author

Listed:
  • Nicolas Tarbouriech

    (Université Grenoble Alpes, CNRS, CEA)

  • Corinne Ducournau

    (Institut de Recherche Biomédicale des Armées)

  • Stephanie Hutin

    (Université Grenoble Alpes, CNRS, CEA)

  • Philippe J. Mas

    (CEA, Université Grenoble Alpes, EMBL)

  • Petr Man

    (Czech Academy of Sciences
    Charles University)

  • Eric Forest

    (Université Grenoble Alpes, CNRS, CEA)

  • Darren J. Hart

    (Université Grenoble Alpes, CNRS, CEA)

  • Christophe N. Peyrefitte

    (Institut de Recherche Biomédicale des Armées
    Fondation Mérieux)

  • Wim P. Burmeister

    (Université Grenoble Alpes, CNRS, CEA)

  • Frédéric Iseni

    (Institut de Recherche Biomédicale des Armées)

Abstract

Vaccinia virus (VACV), the prototype member of the Poxviridae, replicates in the cytoplasm of an infected cell. The catalytic subunit of the DNA polymerase E9 binds the heterodimeric processivity factor A20/D4 to form the functional polymerase holoenzyme. Here we present the crystal structure of full-length E9 at 2.7 Å resolution that permits identification of important poxvirus-specific structural insertions. One insertion in the palm domain interacts with C-terminal residues of A20 and thus serves as the processivity factor-binding site. This is in strong contrast to all other family B polymerases that bind their co-factors at the C terminus of the thumb domain. The VACV E9 structure also permits rationalization of polymerase inhibitor resistance mutations when compared with the closely related eukaryotic polymerase delta–DNA complex.

Suggested Citation

  • Nicolas Tarbouriech & Corinne Ducournau & Stephanie Hutin & Philippe J. Mas & Petr Man & Eric Forest & Darren J. Hart & Christophe N. Peyrefitte & Wim P. Burmeister & Frédéric Iseni, 2017. "The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding," Nature Communications, Nature, vol. 8(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01542-z
    DOI: 10.1038/s41467-017-01542-z
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