Eaf1 is the platform for NuA4 molecular assembly that evolutionarily links chromatin acetylation to ATP-dependent exchange of histone H2A variants.

@article{Auger2008Eaf1IT,
  title={Eaf1 is the platform for NuA4 molecular assembly that evolutionarily links chromatin acetylation to ATP-dependent exchange of histone H2A variants.},
  author={Anne Auger and Luc Galarneau and Mohammed Ibraheem Altaf and Amine Nourani and Yannick Doyon and Rhea T. Utley and Dominique Cronier and St{\'e}phane Allard and Jacques C{\^o}t{\'e}},
  journal={Molecular and cellular biology},
  year={2008},
  volume={28 7},
  pages={
          2257-70
        }
}
Eaf1 (for Esa1-associated factor 1) and Eaf2 have been identified as stable subunits of NuA4, a yeast histone H4/H2A acetyltransferase complex implicated in gene regulation and DNA repair. While both SWI3-ADA2-N-CoR-TF IIIB domain-containing proteins are required for normal cell cycle progression, their depletion does not affect the global Esa1-dependent acetylation of histones. In contrast to all other subunits, Eaf1 is found exclusively associated with the NuA4 complex in vivo. It serves as a… CONTINUE READING

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