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DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart,...
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The basic reaction of homologous recombination (HR) involves two chromatids that contain DNA sequences sharing a significant stretch of identity. One of these sequences uses a strand from another as a template to synthesize DNA in an enzyme-catalyzed reaction. The final product is a novel amalgamation of the two substrates. To ensure an accurate recombination of sequences, HR is restricted to the S and G2 phases of the cell cycle. At these stages, the DNA has been replicated already and the...
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Direct Restart of a Replication Fork Stalled by a Head-On RNA Polymerase
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Break-induced replication is enhanced by a phospho-activated RPA-binding module in Pol32.

David Jones1, Rowin Appanah1,2, Luke A Yates1

  • 1Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, Brighton, UK.

Nature Communications
|April 8, 2026
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Summary
This summary is machine-generated.

Phosphorylation of the Pol32 protein enhances its interaction with RPA, boosting break-induced replication (BIR) efficiency. This finding reveals a key regulatory mechanism in DNA double-strand break repair.

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Area of Science:

  • Molecular Biology
  • DNA Repair Mechanisms
  • Homologous Recombination

Background:

  • Break-induced replication (BIR) is crucial for repairing DNA double-strand breaks (DSBs) using homologous recombination.
  • The minimal replisome for BIR includes PCNA, DNA polymerase δ (Pol δ), and Pif1 helicase.

Purpose of the Study:

  • To identify and characterize the interaction between Pol δ and RPA during BIR.
  • To elucidate the role of Pol32 phosphorylation in regulating BIR efficiency.

Main Methods:

  • Protein interaction studies identifying an RPA-binding module (RBM) in Pol32.
  • Site-directed mutagenesis and phospho-mimetic substitutions in Pol32.
  • In vivo assessment of BIR efficiency.
  • Molecular modeling of protein interactions.

Main Results:

  • An RBM in Pol32 interacts with RPA subunit Rfa1.
  • Phosphorylation of Pol32 RBM at Thr256/Thr257 enhances Rfa1 binding.
  • Phospho-mimetic substitutions in Pol32 increase BIR efficiency in vivo.
  • Modeling suggests conserved RBM-RPA interactions across related helicases.

Conclusions:

  • Pol32 acts as a phosphorylation-dependent rheostat, modulating Pol δ affinity for RPA-bound BIR intermediates.
  • RPA plays a central role in orchestrating the enzymatic machinery of BIR.
  • Understanding these interactions provides insights into DNA repair pathway regulation.