Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation.

@article{Haenni2008IdentificationOL,
  title={Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation.},
  author={Sandra S Haenni and Paul O. Hassa and Matthias Altmeyer and Monika Fey and Ralph Imhof and Michael O Hottiger},
  journal={The international journal of biochemistry & cell biology},
  year={2008},
  volume={40 10},
  pages={2274-83}
}
Poly-ADP-ribose polymerase-2 (PARP-2) was described to regulate cellular functions comprising DNA surveillance, inflammation and cell differentiation by co-regulating different transcription factors. Using an in vitro and in vivo approach, we identified PARP-2 as a new substrate for the histone acetyltransferases PCAF and GCN5L. Site directed mutagenesis indicated that lysines 36 and 37, located in the nuclear localization signal of PARP-2, are the main targets for PCAF and GCN5L activity in… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 29 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 39 references

Acetyla - tion of poly ( ADP - ribose ) polymerase - 1 by p 300 / CREB - binding protein regulates coactivation of NF - kappaB - dependent transcription

  • PO Hassa, ElserM Haenni SS, HottigerMO
  • J Biol Chem
  • 2005
Highly Influential
10 Excerpts

Poly ( ADP - ribose ) : novel functions for an old molecule

  • DE Sterner, SL Berger
  • Nat Rev Mol Cell Biol
  • 2006

A role for the Tip 60 histone acetyltransferase in the acetylation and activation of ATM

  • Y Sun, Y Xu, K Roy, BD Price
  • Proc Natl Acad Sci U S A
  • 2005
1 Excerpt

Molecular evolution of the histone deacetylase family : functional implications of phylogenetic analysis

  • S asan, N El-Andaloussi, U Hardeland, PO Hassa, C Burki, R Imhof
  • J Mol Biol
  • 2004

Similar Papers

Loading similar papers…