Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
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Journal
IF	>30 >20 >10 >5 all

Title	Structure of the NuA4 acetyltransferase complex bound to the nucleosome.
Journal, issue, pages	Nature, Vol. 610, Issue 7932, Page 569-574, Year 2022
Publish date	Oct 5, 2022
Authors	Keke Qu / Kangjing Chen / Hao Wang / Xueming Li / Zhucheng Chen /
PubMed Abstract	Deoxyribonucleic acid in eukaryotes wraps around the histone octamer to form nucleosomes, the fundamental unit of chromatin. The N termini of histone H4 interact with nearby nucleosomes and play an ...Deoxyribonucleic acid in eukaryotes wraps around the histone octamer to form nucleosomes, the fundamental unit of chromatin. The N termini of histone H4 interact with nearby nucleosomes and play an important role in the formation of high-order chromatin structure and heterochromatin silencing. NuA4 in yeast and its homologue Tip60 complex in mammalian cells are the key enzymes that catalyse H4 acetylation, which in turn regulates chromatin packaging and function in transcription activation and DNA repair. Here we report the cryo-electron microscopy structure of NuA4 from Saccharomyces cerevisiae bound to the nucleosome. NuA4 comprises two major modules: the catalytic histone acetyltransferase (HAT) module and the transcription activator-binding (TRA) module. The nucleosome is mainly bound by the HAT module and is positioned close to a polybasic surface of the TRA module, which is important for the optimal activity of NuA4. The nucleosomal linker DNA carrying the upstream activation sequence is oriented towards the conserved, transcription activator-binding surface of the Tra1 subunit, which suggests a potential mechanism of NuA4 to act as a transcription co-activator. The HAT module recognizes the disk face of the nucleosome through the H2A-H2B acidic patch and nucleosomal DNA, projecting the catalytic pocket of Esa1 to the N-terminal tail of H4 and supporting its function in selective acetylation of H4. Together, our findings illustrate how NuA4 is assembled and provide mechanistic insights into nucleosome recognition and transcription co-activation by a HAT.
External links	Nature / PubMed:36198799
Methods	EM (single particle)
Resolution	2.7 - 8.8 Å
Structure data	32148 7vvu EMDB-32148, PDB-7vvu: NuA4 HAT module bound to the nucleosome Method: EM (single particle) / Resolution: 3.4 Å 32149 7vvy EMDB-32149, PDB-7vvy: TRA module of NuA4 Method: EM (single particle) / Resolution: 3.1 Å 32150 7vvz EMDB-32150, PDB-7vvz: NuA4 bound to the nucleosome Method: EM (single particle) / Resolution: 8.8 Å EMDB-32156: ARP submodule of NuA4 Method: EM (single particle) / Resolution: 2.7 Å EMDB-32157: Tra1-head part of NuA4 Method: EM (single particle) / Resolution: 2.8 Å EMDB-32158: NCP-RA of NuA4 bound to the nucleosome Method: EM (single particle) / Resolution: 2.8 Å EMDB-33224: NCP-HAT module with long linker DNA Method: EM (single particle) / Resolution: 6.7 Å
Chemicals	ChemComp-CMC: CARBOXYMETHYL COENZYME A ChemComp-MG: Unknown entry ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM
Source	saccharomyces cerevisiae (brewer's yeast) baker's yeast (brewer's yeast) xenopus laevis (African clawed frog) saccharomyces cerevisiae s288c (yeast)
Keywords	DNA BINDING PROTEIN/DNA / NuA4 nucleosome / DNA BINDING PROTEIN / DNA BINDING PROTEIN-DNA complex / NuA4 Tra1