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Requirement of ATM-dependent monoubiquitylation of histone H2B for timely repair of DNA double-strand breaks.

Molecular cell | Mar 4, 2011

http://www.ncbi.nlm.nih.gov/pubmed/21362549

The cellular response to DNA double-strand breaks (DSBs) is mobilized by the protein kinase ATM, which phosphorylates key players in the DNA damage response (DDR) network. A major question is how ATM controls DSB repair. Optimal repair requires chromatin relaxation at damaged sites. Chromatin reorganization is coupled to dynamic alterations in histone posttranslational modifications. Here, we show that in human cells, DSBs induce monoubiquitylation of histone H2B, a modification that is associated in undamaged cells with transcription elongation. We find that this process relies on recruitment to DSB sites and ATM-dependent phosphorylation of the responsible E3 ubiquitin ligase: the RNF20-RNF40 heterodimer. H2B monoubiquitylation is required for timely recruitment of players in the two major DSB repair pathways-nonhomologous end-joining and homologous recombination repair-and optimal repair via both pathways. Our data and previous data suggest a two-stage model for chromatin decondensation that facilitates DSB repair.

Pubmed ID: 21362549 RIS Download

Mesh terms: Ataxia Telangiectasia Mutated Proteins | Cell Cycle Proteins | Chromatin | Comet Assay | DNA Damage | DNA Repair | DNA-Binding Proteins | HeLa Cells | Histones | Humans | Kinetics | Phosphorylation | Protein Processing, Post-Translational | Protein-Serine-Threonine Kinases | RNA Interference | Recombination, Genetic | Tumor Suppressor Proteins | Ubiquitin | Ubiquitin-Protein Ligases

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Associated grants

  • Agency: NCI NIH HHS, Id: CA50519
  • Agency: NCI NIH HHS, Id: P01 CA092584
  • Agency: NCI NIH HHS, Id: P01-CA92584
  • Agency: NCI NIH HHS, Id: R01 CA113859
  • Agency: NCI NIH HHS, Id: R37 CA050519
  • Agency: NCI NIH HHS, Id: R37 CA40099

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