The molecular basis for histone H4- and H2A-specific amino-terminal acetylation by NatD.

@article{Magin2015TheMB,
  title={The molecular basis for histone H4- and H2A-specific amino-terminal acetylation by NatD.},
  author={Robert S Magin and Glen P. Liszczak and Ronen Marmorstein},
  journal={Structure},
  year={2015},
  volume={23 2},
  pages={332-41}
}
N-terminal acetylation is among the most common protein modifications in eukaryotes and is mediated by evolutionarily conserved N-terminal acetyltransferases (NATs). NatD is among the most selective NATs; its only known substrates are histones H4 and H2A, containing the N-terminal sequence SGRGK in humans. Here we characterize the molecular basis for substrate-specific acetylation by NatD by reporting its crystal structure bound to cognate substrates and performing related biochemical studies… CONTINUE READING

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