Dataset Information

Crosslinking RNF168(1-113) to Nucleosome core particels

ABSTRACT: The project aimed to identify interaction sites of RNF168 with the Nucleosomes. RNF168 interaction with the Nucleosome was probed by BS3 crosslinking to support structure modeling based on NMR and mutagenesis experiments

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Michael Uckelmann

LAB HEAD: Chen Davidovich

PROVIDER: PXD012723 | Pride | 2019-04-02

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	P2CH20181009_MU10.raw	Raw
	P2CH20181009_MU10_HCDFT.cross-linked.BS3.plabel	Other
	P2CH20181009_MU8.raw	Raw
	P2CH20181009_MU8_HCDFT.cross-linked.BS3.plabel	Other
	P2CH20181009_MU9.raw	Raw

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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]

PMID: 30988309

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