Zurück zu Ihrem Suchergebnis

Beschreibung

Histone H2A is one of four components of the core nucleosomal structure. Histones undergo a number of post-translational modifications (PTM) in response to various stimuli that may induce changes in the structure of the nucleosome and hide or expose DNA sequences. The degree of ubiquitylation at DNA damage sites is regulated at multiple levels in order to generate proper DNA damage response. Uncontrolled ubiquitylation of histones can lead to unscheduled transcriptional silencing and generate defects in DNA damage checkpoint activation and cell cycle arrest. The RNF168 E3 ligase ubiquitylates H2A at K13, K15, which in turn triggers the recruitment of DNA damage response proteins, such as 53BP1 and BRCA1 to DNA break sites. USP51, a deubiquitinating enzyme, removes H2AK13, 15ub following DNA repair. Depletion of USP51 can result in elevated levels of H2AK13, 15ub on chromatin and cause delays in disassembly of proteins at DNA damage foci.