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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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Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51
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RADX interacts with single-stranded DNA to promote replication fork stability.

Lisa Schubert1, Teresa Ho1,2, Saskia Hoffmann1

  • 1Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, Copenhagen, Denmark.

EMBO Reports
|October 13, 2017
PubMed
Summary

RADX is a newly identified protein that binds single-stranded DNA (ssDNA) and is crucial for maintaining genome integrity. Its balanced interaction with Replication Protein A (RPA) prevents DNA replication fork defects.

Keywords:
DNA replicationgenome integrityreplication protein Areplication stresssingle‐stranded DNA

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Area of Science:

  • Molecular Biology
  • Genetics
  • Cell Biology

Background:

  • Single-stranded DNA (ssDNA) intermediates are crucial in DNA transactions.
  • Oligonucleotide/oligosaccharide-binding (OB) fold domains mediate protein interactions with ssDNA.
  • Replication Protein A (RPA) is a key heterotrimeric complex essential for genome maintenance, protecting ssDNA and aiding in DNA damage response.

Purpose of the Study:

  • To identify and characterize novel ssDNA-binding proteins involved in genome maintenance.
  • To investigate the role of the uncharacterized protein RADX in DNA replication and stress response.
  • To elucidate the interplay between RADX and RPA in maintaining DNA replication integrity.

Main Methods:

  • Identification of ssDNA-binding proteins using biochemical assays.
  • Characterization of RADX's OB fold domains and their role in ssDNA binding.
  • Analysis of RADX's recruitment to replication stress sites.
  • Assessment of replication fork dynamics and DNA degradation upon RADX deregulation.
  • Investigation of the functional relationship between RADX and RPA.

Main Results:

  • The uncharacterized protein RADX was identified as an ssDNA-binding factor in human cells.
  • RADX possesses an N-terminal cluster of OB folds responsible for ssDNA binding and recruitment to replication stress sites.
  • Dysregulation of RADX leads to increased replication fork stalling and degradation.
  • A balanced interplay between RADX and RPA is critical for preventing these replication defects.

Conclusions:

  • RADX is an essential component of cellular pathways safeguarding DNA replication integrity.
  • RADX functions alongside RPA to manage ssDNA during both normal and stressful conditions.
  • Understanding RADX-RPA interactions provides insights into maintaining genome stability.