Structural plasticity of histones H3-H4 facilitates their allosteric exchange between RbAp48 and ASF1

@inproceedings{Zhang2013StructuralPO,
  title={Structural plasticity of histones H3-H4 facilitates their allosteric exchange between RbAp48 and ASF1},
  author={Wei Zhang and Marek Tyl and Richard J. S. Ward and Frank Sobott and Joseph D. Maman and Andal S. Murthy and Aleksandra A. Watson and Oleg Fedorov and Andrew James Bowman and Tom Owen-Hughes and Hassane El-Mkami and Natalia V. Murzina and David G Norman and Ernest D. Laue},
  booktitle={Nature Structural &Molecular Biology},
  year={2013}
}
The mechanisms by which histones are disassembled and reassembled into nucleosomes and chromatin structure during DNA replication, repair and transcription are poorly understood. A better understanding of the processes involved is, however, crucial if we are to understand whether and how histone variants and post-translationally modified histones are inherited in an epigenetic manner. To this end we have studied the interaction of the histone H3–H4 complex with the human retinoblastoma… CONTINUE READING

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