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RSF1, chromatin remodeling protein, facilitates DNA damage checkpoints and homologous recombination repair

Authors
Min, Sunwoo; Jo, Sujin; Ji, Jae-Hoon; Cho, Hyeseong
Department
Department of Biochemistry & Molecular Biology
Abstract
In eukaryotes, the high level of chromatin compaction is the mechanical barrier to repair DNA double strand breaks (DSBs) upon DNA damage. In order to repair DNA damage and relieve the complexity of chromatin structure at DSBs, it has been reported that the nucleosome is destabilized in the presence of DNA damage to allow the DNA damage machinery to access the DSBs. Furthermore, the global chromatin relaxation around DSB sites is highly regulated by ATM activity, and its substrate, KAP-1, induces chromatin relaxation by dispersing the remodeling factor from chromatin. Previously, we proposed that RSF1, as a subunit of RSF (Remodeling and Spacing Factor) chromatin remodeler, is required to propagate γH2A.X signals and promote homologous recombination repair. However, it is still unclear how RSF1 modifies chromatin structure in response to DNA damage. Here, we selected proteins that tightly bind to RSF1 by mass spectrometry analysis and aimed to identify epigenetic modifying enzymes that are recruited to DSB sites by RSF1.
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