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Restarting Stalled Replication Forks

Restarting Stalled Replication Forks

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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Related Experiment Video

Updated: Jan 14, 2026

Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51

Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51

Published on: February 13, 2019

Dissecting the RAD51-BRC4 Interaction Landscape through Integrative Molecular Simulations and Experimental

Veronica Bresciani^1,2, Francesco Rinaldi¹, Pedro Franco^3,4

¹Computational and Chemical Biology, Istituto Italiano di Tecnologia, Genova 16163, Italy.

Journal of Chemical Information and Modeling

|October 22, 2025

Summary

This summary is machine-generated.

Researchers elucidated the dynamic interaction between RAD51 and BRCA2

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Last Updated: Jan 14, 2026

Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51

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Identifying the Effects of BRCA1 Mutations on Homologous Recombination using Cells that Express Endogenous Wild-type BRCA1

Identifying the Effects of BRCA1 Mutations on Homologous Recombination using Cells that Express Endogenous Wild-type BRCA1

Published on: February 17, 2011

Area of Science:

Molecular Biology
Biochemistry
Structural Biology

Background:

Homologous recombination (HR) relies on RAD51 and BRCA2 protein interaction for DNA repair.
BRCA2's BRC repeats mediate RAD51 recruitment, a key step in HR.
Structural data for full-length RAD51 complexed with BRC repeats is lacking.

Purpose of the Study:

To characterize the solution structure of the full-length RAD51-BRC4 complex.
To understand the conformational dynamics governing RAD51 recruitment by BRCA2.
To identify key interaction sites for potential therapeutic targeting.

Main Methods:

Integrative approach combining AlphaFold2 predictions, cross-linking mass spectrometry, and small-angle X-ray scattering.
Molecular dynamics simulations to analyze conformational ensembles.
Atomic-level structural analysis of the RAD51-BRC4 interface.

Main Results:

The full-length RAD51-BRC4 complex exists as a mixture of compact and elongated conformations.
Identified key residues at the RAD51 N-terminus and BRC4 interface that drive conformational dynamics.
Provided atomic-level insights into the RAD51-BRC4 recognition mechanism.

Conclusions:

The study reveals the dynamic nature of the RAD51-BRC4 complex in solution.
Uncovered critical interaction hotspots for RAD51-BRC4 binding.
Findings offer potential targets for developing novel anticancer agents targeting HR.