sNASP and ASF1A function through both competitive and compatible modes of histone binding

@inproceedings{Bowman2017sNASPAA,
  title={sNASP and ASF1A function through both competitive and compatible modes of histone binding},
  author={Andrew Bowman and Akiko Koide and Jay S. Goodman and Meaghan E. Colling and Daria Zinne and Shohei Koide and Andreas G Ladurner},
  booktitle={Nucleic acids research},
  year={2017}
}
Histone chaperones are proteins that interact with histones to regulate the thermodynamic process of nucleosome assembly. sNASP and ASF1 are conserved histone chaperones that interact with histones H3 and H4 and are found in a multi-chaperoning complex in vivo Previously we identified a short peptide motif within H3 that binds to the TPR domain of sNASP with nanomolar affinity. Interestingly, this peptide motif is sequestered within the known ASF1-H3-H4 interface, raising the question of how… CONTINUE READING

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Proceedings of the National Academy of Sciences of the United States of America • 2005
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