Poly(ADP-ribose) polymerase 1 is inhibited by a histone H2A variant, MacroH2A, and contributes to silencing of the inactive X chromosome.

@article{Nusinow2007PolyADPriboseP1,
  title={Poly(ADP-ribose) polymerase 1 is inhibited by a histone H2A variant, MacroH2A, and contributes to silencing of the inactive X chromosome.},
  author={Dmitri A Nusinow and Inmaculada Hern{\'a}ndez-Mu{\~n}oz and Thomas G Fazzio and Girish M Shah and W Lee Kraus and Barbara Panning},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 17},
  pages={12851-9}
}
Poly(ADP-ribose) polymerase 1 (PARP-1) is a nuclear enzyme that is involved in modulating chromatin structure, regulation of gene expression, and sensing DNA damage. Here, we report that PARP-1 enzymatic activity is inhibited by macroH2A, a vertebrate histone H2A variant that is enriched on facultative heterochromatin. MacroH2A family members have a large C-terminal non-histone domain (NHD) and H2A-like histone domain. MacroH2A1.2 and PARP-1 interact in vivo and in vitro via the NHD. The NHD of… CONTINUE READING

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