Journal
MOLECULAR CELL
Volume 63, Issue 6, Pages 965-975Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2016.07.024
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Funding
- Chinese Ministry of Science and Technology [2014CB910100]
- National Natural Science Foundation of China [31270762, 31425007, 31230018, 31521002]
- Junior One Thousand Talents program
- National Basic Research Program of China [2015CB856200]
- Chinese Academy of Sciences [XDB08010100, KJZD-EW-L05]
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NuA4 catalyzes the acetylation of nucleosomes at histone H4, which is a well-established epigenetic event, controlling many genomic processes in Saccharomyces cerevisiae. Here we report the crystal structures of the NuA4 core complex and a cryoelectron microscopy structure with the nucleosome. The structures show that the histone-binding pocket of the enzyme is rearranged, suggesting its activation. The enzyme binds the histone tail mainly through the target lysine residue, with a preference for a small residue at the -1 position. The complex engages the nucleosome at the dish face and orients its catalytic pocket close to the H4 tail to achieve selective acetylation. The combined data reveal a space-sequence double recognition mechanism of the histone tails by amodifying enzyme in the context of the nucleosome.
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