+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-32150 | |||||||||
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Title | NuA4 bound to the nucleosome | |||||||||
Map data | ||||||||||
Sample |
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Function / homology | Function and homology information PI5P Regulates TP53 Acetylation / NuA3b histone acetyltransferase complex / RHOB GTPase cycle / NuA3a histone acetyltransferase complex / DNA Damage/Telomere Stress Induced Senescence / Sensing of DNA Double Strand Breaks / NuA3 histone acetyltransferase complex / RHOA GTPase cycle / cellular bud neck contractile ring / mitotic actomyosin contractile ring contraction ...PI5P Regulates TP53 Acetylation / NuA3b histone acetyltransferase complex / RHOB GTPase cycle / NuA3a histone acetyltransferase complex / DNA Damage/Telomere Stress Induced Senescence / Sensing of DNA Double Strand Breaks / NuA3 histone acetyltransferase complex / RHOA GTPase cycle / cellular bud neck contractile ring / mitotic actomyosin contractile ring contraction / piccolo histone acetyltransferase complex / ascospore wall assembly / vacuole inheritance / histone H4K16 acetyltransferase activity / peptide 2-hydroxyisobutyryltransferase activity / histone crotonyltransferase activity / SUMOylation of transcription cofactors / DNA-templated transcription elongation / positive regulation of triglyceride biosynthetic process / actin cortical patch / Swr1 complex / SLIK (SAGA-like) complex / histone H4 acetyltransferase activity / rDNA heterochromatin formation / kinetochore assembly / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / peptide N-acetyltransferase activity / Ino80 complex / SWI/SNF complex / SAGA complex / peptide-lysine-N-acetyltransferase activity / establishment of cell polarity / NuA4 histone acetyltransferase complex / actin filament bundle / Estrogen-dependent gene expression / positive regulation of macroautophagy / protein secretion / chromosome organization / Ub-specific processing proteases / histone acetyltransferase activity / histone acetyltransferase / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / methylated histone binding / meiotic cell cycle / actin filament / positive regulation of transcription elongation by RNA polymerase II / transcription coregulator activity / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / structural constituent of cytoskeleton / endocytosis / structural constituent of chromatin / transcription corepressor activity / nucleosome / chromatin organization / histone binding / protein-containing complex assembly / regulation of cell cycle / chromatin remodeling / protein heterodimerization activity / DNA repair / DNA-templated transcription / chromatin binding / regulation of DNA-templated transcription / chromatin / regulation of transcription by RNA polymerase II / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / DNA binding / ATP binding / identical protein binding / nucleus / metal ion binding / cytosol Similarity search - Function | |||||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) / Saccharomyces cerevisiae S288C (yeast) / Xenopus laevis (African clawed frog) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 8.8 Å | |||||||||
Authors | Qu K / Chen Z | |||||||||
Funding support | 1 items
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Citation | Journal: Nature / Year: 2022 Title: Structure of the NuA4 acetyltransferase complex bound to the nucleosome. Authors: Keke Qu / Kangjing Chen / Hao Wang / Xueming Li / Zhucheng Chen / 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. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_32150.map.gz | 2.2 MB | EMDB map data format | |
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Header (meta data) | emd-32150-v30.xml emd-32150.xml | 33.7 KB 33.7 KB | Display Display | EMDB header |
Images | emd_32150.png | 28.7 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-32150 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-32150 | HTTPS FTP |
-Validation report
Summary document | emd_32150_validation.pdf.gz | 366.3 KB | Display | EMDB validaton report |
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Full document | emd_32150_full_validation.pdf.gz | 365.9 KB | Display | |
Data in XML | emd_32150_validation.xml.gz | 5 KB | Display | |
Data in CIF | emd_32150_validation.cif.gz | 5.6 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-32150 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-32150 | HTTPS FTP |
-Related structure data
Related structure data | 7vvzMC 7vvuC 7vvyC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_32150.map.gz / Format: CCP4 / Size: 3.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 4.33 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Sample components
+Entire : NuA4 bound to the nucleosome
+Supramolecule #1: NuA4 bound to the nucleosome
+Macromolecule #1: Chromatin modification-related protein EAF6
+Macromolecule #2: Chromatin modification-related protein YNG2
+Macromolecule #3: Enhancer of polycomb-like protein 1
+Macromolecule #4: Histone H3
+Macromolecule #5: Histone H4
+Macromolecule #6: Histone H2A
+Macromolecule #7: Histone H2B 1.1
+Macromolecule #8: Histone acetyltransferase ESA1
+Macromolecule #11: Epl1 arginine anchor
+Macromolecule #12: Chromatin modification-related protein EAF1
+Macromolecule #13: Actin-related protein 4
+Macromolecule #14: Actin
+Macromolecule #15: SWR1-complex protein 4
+Macromolecule #16: Transcription-associated protein 1
+Macromolecule #9: DNA (207-mer)
+Macromolecule #10: DNA (207-mer)
+Macromolecule #17: CARBOXYMETHYL COENZYME *A
+Macromolecule #18: MAGNESIUM ION
+Macromolecule #19: ADENOSINE-5'-TRIPHOSPHATE
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.6 |
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Vitrification | Cryogen name: NITROGEN |
-Electron microscopy
Microscope | FEI TITAN |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.3 µm |
-Image processing
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 8.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 474949 |
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Initial angle assignment | Type: ANGULAR RECONSTITUTION |
Final angle assignment | Type: ANGULAR RECONSTITUTION |