Nucleolin mediates nucleosome disruption critical for DNA double-strand break repair
Copyright policy )Nucleolin mediates nucleosome disruption critical for DNA double-strand break repair
Significance Recognition and repair of DNA lesions are critical for maintaining genomic stability and reducing the generation of mutations that lead to cancer development. A mechanism of chromatin alteration is described here that is essential for repair of DNA double-strand breaks. The histone chaperone, nucleolin, is recruited to sites of DNA breaks via binding to RAD50 of the MRE11-NBS1-RAD50 complex, where it removes histone proteins H2A and H2B from the nucleosome at the break site. This nucleosome disruption allows DNA repair proteins to access the DNA lesion and facilitate repair of the DNA break. Clinical implications of these findings include the identification of new targets, such as nucleolin, that could be modulated to enhance sensitivity of tumor cells to radiation therapy.
- Duke University United States
- St. Jude Children's Research Hospital United States
Nucleolin, MRE11 Homologue Protein, Nuclear Proteins, RNA-Binding Proteins, Recombinational DNA Repair, Cell Cycle Proteins, Phosphoproteins, G1 Phase Cell Cycle Checkpoints, Acid Anhydride Hydrolases, Nucleosomes, DNA-Binding Proteins, Histones, DNA Repair Enzymes, Cell Line, Tumor, Replication Protein A, Humans, DNA Breaks, Double-Stranded, Protein Multimerization
Nucleolin, MRE11 Homologue Protein, Nuclear Proteins, RNA-Binding Proteins, Recombinational DNA Repair, Cell Cycle Proteins, Phosphoproteins, G1 Phase Cell Cycle Checkpoints, Acid Anhydride Hydrolases, Nucleosomes, DNA-Binding Proteins, Histones, DNA Repair Enzymes, Cell Line, Tumor, Replication Protein A, Humans, DNA Breaks, Double-Stranded, Protein Multimerization
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