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RNF 4 interacts with both SUMO and nucleosomes to promote the DNA damage response
Author(s) -
Groocock Lynda M,
Nie Minghua,
Prudden John,
Moiani Davide,
Wang Tao,
Cheltsov Anton,
Rambo Robert P,
Arvai Andrew S,
Hitomi Chiharu,
Tainer John A,
Luger Karolin,
Perry J Jefferson P,
LazzeriniDenchi Eros,
Boddy Michael N
Publication year - 2014
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1002/embr.201338369
Subject(s) - dna damage , dna , microbiology and biotechnology , nucleosome , chemistry , histone , biology , biochemistry
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 RNF 4 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 RNF 4, in addition to interaction with SUMO . We identify a nucleosome‐targeting motif within the RNF 4 RING domain that can bind DNA and thereby enables RNF 4 to selectively ubiquitinate nucleosomal histones. Furthermore, RNF 4 nucleosome‐targeting is crucially required for the repair of TRF 2‐depleted dysfunctional telomeres by 53 BP 1‐mediated non‐homologous end joining.