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Structural basis for the increased processivity of D-family DNA polymerases in complex with PCNA

Author

Listed:
  • Clément Madru

    (Institut Pasteur and CNRS UMR 3528)

  • Ghislaine Henneke

    (Université de Brest, Laboratoire de Microbiologie des Environnements Extrêmes)

  • Pierre Raia

    (Institut Pasteur and CNRS UMR 3528
    Sorbonne Université, École Doctorale Complexité du Vivant (ED515))

  • Inès Hugonneau-Beaufet

    (Institut Pasteur and CNRS UMR 3528)

  • Gérard Pehau-Arnaudet

    (Utech UBI, Institut Pasteur, CNRS UMR 3528)

  • Patrick England

    (Institut Pasteur, CNRS UMR 3528)

  • Erik Lindahl

    (Stockholm University
    KTH Royal Institute of Technology)

  • Marc Delarue

    (Institut Pasteur and CNRS UMR 3528)

  • Marta Carroni

    (Stockholm University)

  • Ludovic Sauguet

    (Institut Pasteur and CNRS UMR 3528)

Abstract

Replicative DNA polymerases (DNAPs) have evolved the ability to copy the genome with high processivity and fidelity. In Eukarya and Archaea, the processivity of replicative DNAPs is greatly enhanced by its binding to the proliferative cell nuclear antigen (PCNA) that encircles the DNA. We determined the cryo-EM structure of the DNA-bound PolD–PCNA complex from Pyrococcus abyssi at 3.77 Å. Using an integrative structural biology approach — combining cryo-EM, X-ray crystallography, protein–protein interaction measurements, and activity assays — we describe the molecular basis for the interaction and cooperativity between a replicative DNAP and PCNA. PolD recruits PCNA via a complex mechanism, which requires two different PIP-boxes. We infer that the second PIP-box, which is shared with the eukaryotic Polα replicative DNAP, plays a dual role in binding either PCNA or primase, and could be a master switch between an initiation and a processive phase during replication.

Suggested Citation

  • Clément Madru & Ghislaine Henneke & Pierre Raia & Inès Hugonneau-Beaufet & Gérard Pehau-Arnaudet & Patrick England & Erik Lindahl & Marc Delarue & Marta Carroni & Ludovic Sauguet, 2020. "Structural basis for the increased processivity of D-family DNA polymerases in complex with PCNA," Nature Communications, Nature, vol. 11(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-15392-9
    DOI: 10.1038/s41467-020-15392-9
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    Cited by:

    1. Leonardo Betancurt-Anzola & Markel Martínez-Carranza & Marc Delarue & Kelly M. Zatopek & Andrew F. Gardner & Ludovic Sauguet, 2023. "Molecular basis for proofreading by the unique exonuclease domain of Family-D DNA polymerases," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    2. Anastasiia Chaban & Leonid Minakhin & Ekaterina Goldobina & Brain Bae & Yue Hao & Sergei Borukhov & Leena Putzeys & Maarten Boon & Florian Kabinger & Rob Lavigne & Kira S. Makarova & Eugene V. Koonin , 2024. "Tail-tape-fused virion and non-virion RNA polymerases of a thermophilic virus with an extremely long tail," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    3. Claudia Lancey & Muhammad Tehseen & Souvika Bakshi & Matthew Percival & Masateru Takahashi & Mohamed A. Sobhy & Vlad S. Raducanu & Kerry Blair & Frederick W. Muskett & Timothy J. Ragan & Ramon Crehuet, 2021. "Cryo-EM structure of human Pol κ bound to DNA and mono-ubiquitylated PCNA," Nature Communications, Nature, vol. 12(1), pages 1-14, December.

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