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. Author manuscript; available in PMC: 2014 Dec 1.
Published in final edited form as: Mol Aspects Med. 2013 Apr 25;34(6):10.1016/j.mam.2013.04.001. doi: 10.1016/j.mam.2013.04.001

Figure 3. Model of PARP1 interaction with histone H2Av.

Figure 3

Nucleosome with H2Av works as a high affinity site (red) for PARP1 (blue) binding with specific chromatin domains. While in complex with H2Av-nucleosome, PARP1 is catalytically inactive. Phosphorylation of H2Av disrupts its interaction with PARP1 and stimulates PARP1 activity (poly(ADP-ribosylation)). PARP1 modifies histone H1 (Aubin et al., 1983) and facilitates local chromatin relaxation and remodeling.