Crosslinking RNF168(1-113) to Nucleosome core particels
Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q Exactive
ORGANISM(S): Homo Sapiens (human)
SUBMITTER: 
Michael Uckelmann
LAB HEAD: Chen Davidovich
PROVIDER: PXD012723 | Pride | 2019-04-02
REPOSITORIES: Pride
Publications
Structural basis of specific H2A K13/K15 ubiquitination by RNF168.
Horn Velten V Uckelmann Michael M Zhang Heyi H Eerland Jelmer J Aarsman Ivette I le Paige Ulric B UB Davidovich Chen C Sixma Titia K TK van Ingen Hugo H
Nature communications 20190415 1
Ubiquitination of chromatin by modification of histone H2A is a critical step in both regulation of DNA repair and regulation of cell fate. These very different outcomes depend on the selective modification of distinct lysine residues in H2A, each by a specific E3 ligase. While polycomb PRC1 complexes modify K119, resulting in gene silencing, the E3 ligase RNF168 modifies K13/15, which is a key event in the response to DNA double-strand breaks. The molecular origin of ubiquitination site specifi ...[more]
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