ATR and H2AX cooperate in maintaining genome stability under replication stress

J Biol Chem. 2009 Feb 27;284(9):5994-6003. doi: 10.1074/jbc.M806739200. Epub 2008 Dec 2.

Abstract

Chromosomal abnormalities are frequently caused by problems encountered during DNA replication. Although the ATR-Chk1 pathway has previously been implicated in preventing the collapse of stalled replication forks into double-strand breaks (DSB), the importance of the response to fork collapse in ATR-deficient cells has not been well characterized. Herein, we demonstrate that, upon stalled replication, ATR deficiency leads to the phosphorylation of H2AX by ATM and DNA-PKcs and to the focal accumulation of Rad51, a marker of homologous recombination and fork restart. Because H2AX has been shown to play a facilitative role in homologous recombination, we hypothesized that H2AX participates in Rad51-mediated suppression of DSBs generated in the absence of ATR. Consistent with this model, increased Rad51 focal accumulation in ATR-deficient cells is largely dependent on H2AX, and dual deficiencies in ATR and H2AX lead to synergistic increases in chromatid breaks and translocations. Importantly, the ATM and DNA-PK phosphorylation site on H2AX (Ser(139)) is required for genome stabilization in the absence of ATR; therefore, phosphorylation of H2AX by ATM and DNA-PKcs plays a pivotal role in suppressing DSBs during DNA synthesis in instances of ATR pathway failure. These results imply that ATR-dependent fork stabilization and H2AX/ATM/DNA-PKcs-dependent restart pathways cooperatively suppress double-strand breaks as a layered response network when replication stalls.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Ataxia Telangiectasia Mutated Proteins
  • Cell Cycle Proteins / antagonists & inhibitors
  • Cell Cycle Proteins / metabolism
  • Cell Cycle Proteins / physiology*
  • Cells, Cultured
  • DNA Breaks, Double-Stranded*
  • DNA Replication*
  • DNA-Activated Protein Kinase / metabolism
  • DNA-Binding Proteins / metabolism
  • Embryo, Mammalian / cytology
  • Embryo, Mammalian / metabolism
  • Embryo, Mammalian / radiation effects
  • Fibroblasts / cytology
  • Fibroblasts / metabolism
  • Fibroblasts / radiation effects
  • Genomic Instability*
  • Histones / physiology*
  • Metaphase
  • Mice
  • Mice, Knockout
  • Mitosis
  • Nuclear Proteins / metabolism
  • Phosphorylation
  • Protein Serine-Threonine Kinases / antagonists & inhibitors
  • Protein Serine-Threonine Kinases / metabolism
  • Protein Serine-Threonine Kinases / physiology*
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • RNA, Small Interfering / pharmacology
  • Rad51 Recombinase / metabolism
  • Radiation, Ionizing
  • Reverse Transcriptase Polymerase Chain Reaction
  • S Phase / physiology
  • Spectral Karyotyping
  • Tumor Suppressor Proteins / metabolism

Substances

  • Cell Cycle Proteins
  • DNA-Binding Proteins
  • H2AX protein, mouse
  • Histones
  • Nuclear Proteins
  • RNA, Messenger
  • RNA, Small Interfering
  • Tumor Suppressor Proteins
  • Atr protein, mouse
  • Ataxia Telangiectasia Mutated Proteins
  • Atm protein, mouse
  • DNA-Activated Protein Kinase
  • Prkdc protein, mouse
  • Protein Serine-Threonine Kinases
  • Rad51 Recombinase
  • Rad51 protein, mouse