<p>Protein-primed DNA replication is an alternative replication mode solving the end-replication problem of canonical linear DNA replication. In the PRD1 bacteriophage, the ssDNA-binding protein P12 is a key player in this process. We resolved its structure via high-resolution cryo-EM, revealing a unique fold that enables cooperative filament formation and stabilises ssDNA replication intermediates. Our findings enhance the understanding of ssDNA-binding proteins and viral replication mechanisms.</p>

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Kryo-EM enthüllt Mechanismen viraler Replikationsstrategien

  • Lena Klara Träger,
  • Nicolas Huguenin-Dezot

摘要

Protein-primed DNA replication is an alternative replication mode solving the end-replication problem of canonical linear DNA replication. In the PRD1 bacteriophage, the ssDNA-binding protein P12 is a key player in this process. We resolved its structure via high-resolution cryo-EM, revealing a unique fold that enables cooperative filament formation and stabilises ssDNA replication intermediates. Our findings enhance the understanding of ssDNA-binding proteins and viral replication mechanisms.