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Title | The NuA4 Core Complex Acetylates Nucleosomal Histone H4 through a Double Recognition Mechanism. |
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Journal, issue, pages | Mol Cell, Vol. 63, Issue 6, Page 965-975, Year 2016 |
Publish date | Sep 15, 2016 |
Authors | Peng Xu / Chengmin Li / Zhihong Chen / Shuanying Jiang / Shilong Fan / Jiawei Wang / Junbiao Dai / Ping Zhu / Zhucheng Chen / |
PubMed Abstract | 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 ...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 a modifying enzyme in the context of the nucleosome. |
External links | Mol Cell / PubMed:27594449 |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 2.7 - 7.9 Å |
Structure data | EMDB-9536: PDB-5j9q: PDB-5j9t: PDB-5j9u: PDB-5j9w: |
Chemicals | ChemComp-HOH: ChemComp-ACO: |
Source |
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Keywords | TRANSFERASE / NuA4 / nucleosome / histone / acetylation |