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Tudor-interacting repair regulator (TIRR) is an RNA-binding protein and a negative regulator of the DNA-repair factor p53-binding protein 1 (53BP1). In non-damage conditions, TIRR is bound to 53BP1. After DNA damage, TIRR and 53BP1 dissociate, and 53BP1 binds the chromatin at the double-strand break (DSB) to promote non-homologous end joining (NHEJ)-mediated repair. However, the exact mechanistic details of this dissociation after damage are unknown. Increasing evidence has implicated RNA as a crucial factor in the DNA damage response (DDR). Here, we show that RNA can separate TIRR/53BP1. Specifically, RNA with a hairpin secondary structure, transcribed at the DSB by RNA polymerase II (RNAPII), promotes TIRR/53BP1 complex separation. This hairpin RNA binds to the same residues on TIRR as 53BP1. Our results uncover a role of DNA-damage-derived RNA in modulating a protein-protein interaction and contribute to our understanding of DSB repair.

Original publication




Journal article


Cell reports

Publication Date





Sir William Dunn School of Pathology, South Parks Road, Oxford OX1 3RE, UK.


Chromatin, RNA Polymerase II, RNA-Binding Proteins, DNA, RNA, DNA Repair, Protein Binding, Tumor Suppressor Protein p53, DNA Breaks, Double-Stranded, DNA End-Joining Repair, Tumor Suppressor p53-Binding Protein 1