Histone core phosphorylation regulates DNA accessibility.

@article{Brehove2015HistoneCP,
  title={Histone core phosphorylation regulates DNA accessibility.},
  author={Matthew Brehove and Tao T. Wang and Justin A. North and Yi Luo and Sarah J. Dreher and John C. Shimko and Jennifer J. Ottesen and Karolin Luger and Michael Guy Poirier},
  journal={The Journal of biological chemistry},
  year={2015},
  volume={290 37},
  pages={22612-21}
}
Nucleosome unwrapping dynamics provide transient access to the complexes involved in DNA transcription, repair, and replication, whereas regulation of nucleosome unwrapping modulates occupancy of these complexes. Histone H3 is phosphorylated at tyrosine 41 (H3Y41ph) and threonine 45 (H3T45ph). H3Y41ph is implicated in regulating transcription, whereas H3T45ph is involved in DNA replication and apoptosis. These modifications are located in the DNA-histone interface near where the DNA exits the… CONTINUE READING
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