Structural Basis for the Histone Chaperone Activity of Asf1

@article{English2006StructuralBF,
  title={Structural Basis for the Histone Chaperone Activity of Asf1},
  author={Christine M. English and Melissa W. Adkins and J D Jeffrey D Carson and Mair E. A. Churchill and Jessica K Tyler},
  journal={Cell},
  year={2006},
  volume={127},
  pages={495-508}
}
Anti-silencing function 1 (Asf1) is a highly conserved chaperone of histones H3/H4 that assembles or disassembles chromatin during transcription, replication, and repair. The structure of the globular domain of Asf1 bound to H3/H4 determined by X-ray crystallography to a resolution of 1.7 Angstroms shows how Asf1 binds the H3/H4 heterodimer, enveloping the C terminus of histone H3 and physically blocking formation of the H3/H4 heterotetramer. Unexpectedly, the C terminus of histone H4 that… CONTINUE READING
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