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Related Concept Videos

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In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
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Related Experiment Video

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Quantification of γH2AX Foci in Response to Ionising Radiation
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Critical Function of γH2A in S-Phase.

Eva Mejia-Ramirez1, Oliver Limbo1, Petra Langerak1

  • 1Department of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, California, United States of America.

Plos Genetics
|September 15, 2015
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Summary

Phospho-H2AX (γH2AX) is crucial for DNA repair, particularly during replication stress. In fission yeast, γH2A is essential when Replication Factor C (RFC) is defective, stabilizing replication forks.

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Genetics

Background:

  • Phosphorylation of histone H2AX (γH2AX) by ATM and ATR is a key event in DNA damage response.
  • While extensively studied for DNA double-strand breaks, γH2AX's role in replication stress is emerging.
  • Replication stress also triggers γH2A formation in Schizosaccharomyces pombe.

Purpose of the Study:

  • Investigate the role of γH2A in DNA replication stress.
  • Identify factors essential for γH2A function when Replication Factor C (RFC) is defective.
  • Elucidate the mechanism by which γH2A stabilizes stalled replication forks.

Main Methods:

  • Focused genetic screen in fission yeast.
  • Immunoblot analysis.
  • Localization studies of proteins at replication forks.

Main Results:

  • γH2A is critical in RFC-defective cells, independent of canonical checkpoint proteins like Chk1, Cds1/Chk2, and Rad9-Hus1-Rad1.
  • Rad9-Hus1-Rad1 is not required for Rad3/ATR-mediated γH2A formation during S-phase.
  • Defects in DNA polymerase epsilon also necessitate γH2A.
  • γH2A interacts with Brc1, which localizes to stalled forks and prevents aberrant Replication Protein A (RPA) foci formation.
  • Brc1-bound chromatin stabilizes replisomes under limited PCNA or DNA polymerase availability.

Conclusions:

  • γH2A plays a vital, non-canonical role in maintaining genome stability during replication stress, particularly when RFC function is compromised.
  • The γH2A-Brc1 interaction is crucial for stabilizing stalled replication forks and preventing DNA damage.
  • This study highlights a novel pathway for replication fork stabilization mediated by γH2A and Brc1.