INO80 and γ-H2AX Interaction Links ATP-Dependent Chromatin Remodeling to DNA Damage Repair
Copyright policy )INO80 and γ-H2AX Interaction Links ATP-Dependent Chromatin Remodeling to DNA Damage Repair
While the role of ATP-dependent chromatin remodeling in transcription is well established, a link between chromatin remodeling and DNA repair has remained elusive. We have found that the evolutionarily conserved INO80 chromatin remodeling complex directly participates in the repair of a double-strand break (DSB) in yeast. The INO80 complex is recruited to a HO endonuclease-induced DSB through a specific interaction with the DNA damage-induced phosphorylated histone H2A (gamma-H2AX). This interaction requires Nhp10, an HMG-like subunit of the INO80 complex. The loss of Nhp10 or gamma-H2AX results in reduced INO80 recruitment to the DSB. Finally, components of the INO80 complex show synthetic genetic interactions with the RAD52 DNA repair pathway, the main pathway for DSB repair in yeast. Our findings reveal a new role of ATP-dependent chromatin remodeling in nuclear processes and suggest that an ATP-dependent chromatin remodeling complex can read a DNA repair histone code.
- The University of Texas System United States
- Brandeis University United States
- University of Toronto Canada
- The University of Texas MD Anderson Cancer Center United States
Chromatin Immunoprecipitation, Saccharomyces cerevisiae Proteins, DNA Repair, Transcription, Genetic, Biochemistry, Genetics and Molecular Biology(all), Gene Expression Profiling, Saccharomyces cerevisiae, Chromatin Assembly and Disassembly, Rad52 DNA Repair and Recombination Protein, DNA-Binding Proteins, Histones, Adenosine Triphosphate, Mutation, Protein Binding
Chromatin Immunoprecipitation, Saccharomyces cerevisiae Proteins, DNA Repair, Transcription, Genetic, Biochemistry, Genetics and Molecular Biology(all), Gene Expression Profiling, Saccharomyces cerevisiae, Chromatin Assembly and Disassembly, Rad52 DNA Repair and Recombination Protein, DNA-Binding Proteins, Histones, Adenosine Triphosphate, Mutation, Protein Binding
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