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RNF4 interacts with both SUMO and nucleosomes to promote the DNA damage response.

Authors: Lynda M LM. Groocock, Minghua M. Nie, John J. Prudden, Davide D. Moiani, Tao T. Wang, Anton A. Cheltsov, Robert P RP. Rambo, Andrew S AS. Arvai, Chiharu C. Hitomi, John A JA. Tainer, Karolin K. Luger, J Jefferson P JJ. Perry, Eros E. Lazzerini-Denchi, Michael N MN. Boddy
Published: 04/08/2014, EMBO reports


The post-translational modification of DNA repair and checkpoint proteins by ubiquitin and small ubiquitin-like modifier (SUMO) critically orchestrates the DNA damage response (DDR). The ubiquitin ligase RNF4 integrates signaling by SUMO and ubiquitin, through its selective recognition and ubiquitination of SUMO-modified proteins. Here, we define a key new determinant for target discrimination by RNF4, in addition to interaction with SUMO. We identify a nucleosome-targeting motif within the RNF4 RING domain that can bind DNA and thereby enables RNF4 to selectively ubiquitinate nucleosomal histones. Furthermore, RNF4 nucleosome-targeting is crucially required for the repair of TRF2-depleted dysfunctional telomeres by 53BP1-mediated non-homologous end joining.

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