Structure of the Drosophila nucleosome core particle highlights evolutionary constraints on the H2A-H2B histone dimer

@article{Clapier2008StructureOT,
  title={Structure of the Drosophila nucleosome core particle highlights evolutionary constraints on the H2A-H2B histone dimer},
  author={Cedric R. Clapier and S. Chakravarthy and Carlo Petosa and Carlos Fern{\'a}ndez-Tornero and Karolin Luger and Christoph W M{\"u}ller},
  journal={Proteins},
  year={2008},
  volume={71},
  pages={1 - 7}
}
We determined the 2.45 A crystal structure of the nucleosome core particle from Drosophila melanogaster and compared it to that of Xenopus laevis bound to the identical 147 base-pair DNA fragment derived from human alpha-satellite DNA. Differences between the two structures primarily reflect 16 amino acid substitutions between species, 15 of which are in histones H2A and H2B. Four of these involve histone tail residues, resulting in subtly altered protein-DNA interactions that exemplify the… CONTINUE READING

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