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Structure of the processive human Pol δ holoenzyme.

Claudia Lancey1, Muhammad Tehseen2, Vlad-Stefan Raducanu2

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The study reveals the structure of human DNA polymerase delta (Pol δ) with proliferating cell nuclear antigen (PCNA), clarifying how it replicates DNA and processes Okazaki fragments with flap endonuclease 1 (FEN1). This provides insight into genome replication mechanisms.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • DNA polymerase delta (Pol δ) and proliferating cell nuclear antigen (PCNA) are crucial for eukaryotic lagging strand DNA replication.
  • Processing of Okazaki fragments by Pol δ, PCNA, and flap endonuclease 1 (FEN1) is essential for DNA ligation and genome integrity.

Purpose of the Study:

  • To determine the high-resolution cryo-electron microscopy (cryo-EM) structure of the human Pol δ-DNA-PCNA complex.
  • To elucidate the structural mechanisms of Pol δ-PCNA interaction and FEN1 recruitment during DNA replication.

Main Methods:

  • High-resolution cryo-electron microscopy (cryo-EM) was used to visualize the human Pol δ-DNA-PCNA complex.
  • Structures were determined in the absence and presence of flap endonuclease 1 (FEN1).

Main Results:

  • The structure shows Pol δ anchored to a PCNA monomer via its C-terminal domain, with the catalytic core positioned on top of PCNA.
  • PCNA stabilizes the exiting DNA and recruits FEN1 in a 'toolbelt' fashion to an unoccupied monomer.
  • Alternative holoenzyme conformations highlight interactions maintaining PCNA orientation during DNA synthesis.

Conclusions:

  • The study provides a detailed structural basis for the function of Pol δ in human genome replication.
  • The findings clarify the roles of PCNA and FEN1 in coordinating lagging strand synthesis and Okazaki fragment processing.