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Updated: Jun 24, 2026

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution
Published on: January 16, 2017
Dual roles of the DHX9 RGG domain in hybrid-dependent recruitment and suppression of 53BP1
Yuina Tsuchiya1, Yudai Hiwatashi1, Hayaki Ikegame1
1Graduate School of Bionics, Tokyo University of Technology, Hachioji, Tokyo, 192-0982, Japan.
Abstract:
DNA double-strand breaks (DSBs) are repaired mainly by non-homologous end-joining (NHEJ) and homologous recombination repair (HR) in mammalian cells. Recent studies highlight the importance of RNA in regulating these pathways and influencing pathway choice, particularly through the formation and resolution of DNA-RNA hybrids. Here, we show that DNA-RNA hybrids are formed at DSB sites in a PARP1- and poly (ADP-ribosyl)ation-dependent manner and are resolved by DHX9 dependent manner. The carboxyl-terminal RGG domain of DHX9 is necessary and sufficient for its recruitment and is required for efficient DNA end-resection. We further identify methylated arginine residues within this domain that are required for suppressing loading of the NHEJ-promoting factor 53BP1 to the DSB sites. Our findings highlight a central role of the RGG domain of DHX9 in DNA-RNA hybrid regulation and DSB repair pathway choice.
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