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<scp>RNF</scp> 4 interacts with both <scp>SUMO</scp> and nucleosomes to promote the <scp>DNA</scp> damage response
- Source :
- EMBO reports. 15:601-608
- Publication Year :
- 2014
- Publisher :
- EMBO, 2014.
-
Abstract
- 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.
- Subjects :
- DNA Repair
Chromosomal Proteins, Non-Histone
DNA damage
DNA repair
Ubiquitin-Protein Ligases
Amino Acid Motifs
SUMO protein
SUMO enzymes
Crystallography, X-Ray
Biochemistry
Cell Line
Gene Knockout Techniques
Mice
Ubiquitin
Genetics
Animals
Telomeric Repeat Binding Protein 2
Molecular Biology
chemistry.chemical_classification
DNA ligase
biology
Scientific Reports
Ubiquitination
Nuclear Proteins
Telomere
Nucleosomes
Protein Structure, Tertiary
Ubiquitin ligase
Cell biology
DNA-Binding Proteins
Tamoxifen
Histone
chemistry
Small Ubiquitin-Related Modifier Proteins
biology.protein
Tumor Suppressor p53-Binding Protein 1
Protein Processing, Post-Translational
DNA Damage
Transcription Factors
Subjects
Details
- ISSN :
- 14693178 and 1469221X
- Volume :
- 15
- Database :
- OpenAIRE
- Journal :
- EMBO reports
- Accession number :
- edsair.doi.dedup.....a27bdb4f20ff031c36d9198d1ce0a2f0