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Open data
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Basic information
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Title | NuA4 bound to the nucleosome | |||||||||
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![]() | NuA4 nucleosome / DNA BINDING PROTEIN / DNA BINDING PROTEIN-DNA complex | |||||||||
Function / homology | ![]() PI5P Regulates TP53 Acetylation / NuA3b histone acetyltransferase complex / NuA3a histone acetyltransferase complex / NuA3 histone acetyltransferase complex / RHOB GTPase cycle / DNA Damage/Telomere Stress Induced Senescence / Sensing of DNA Double Strand Breaks / RHOA GTPase cycle / cellular bud neck contractile ring / mitotic actomyosin contractile ring contraction ...PI5P Regulates TP53 Acetylation / NuA3b histone acetyltransferase complex / NuA3a histone acetyltransferase complex / NuA3 histone acetyltransferase complex / RHOB GTPase cycle / DNA Damage/Telomere Stress Induced Senescence / Sensing of DNA Double Strand Breaks / RHOA GTPase cycle / cellular bud neck contractile ring / mitotic actomyosin contractile ring contraction / piccolo histone acetyltransferase complex / vacuole inheritance / ascospore wall assembly / TTT Hsp90 cochaperone complex / peptide 2-hydroxyisobutyryltransferase activity / histone crotonyltransferase activity / SUMOylation of transcription cofactors / positive regulation of triglyceride biosynthetic process / actin cortical patch / DNA-templated transcription elongation / SLIK (SAGA-like) complex / histone H4 acetyltransferase activity / Swr1 complex / kinetochore assembly / rDNA heterochromatin formation / Ino80 complex / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / histone H3K4me3 reader activity / SAGA complex / SWI/SNF complex / protein-lysine-acetyltransferase activity / DNA repair-dependent chromatin remodeling / establishment of cell polarity / NuA4 histone acetyltransferase complex / actin filament bundle / histone acetyltransferase activity / Estrogen-dependent gene expression / positive regulation of macroautophagy / protein secretion / : / Ub-specific processing proteases / chromosome organization / histone acetyltransferase / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / meiotic cell cycle / actin filament / transcription coregulator activity / positive regulation of transcription elongation by RNA polymerase II / structural constituent of cytoskeleton / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / endocytosis / transcription corepressor activity / structural constituent of chromatin / nucleosome / heterochromatin formation / actin cytoskeleton / chromatin organization / protein-containing complex assembly / histone binding / regulation of cell cycle / chromatin remodeling / protein heterodimerization activity / DNA repair / DNA-templated transcription / chromatin binding / regulation of transcription by RNA polymerase II / regulation of DNA-templated transcription / chromatin / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / DNA binding / zinc ion binding / ATP binding / identical protein binding / nucleus / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 8.8 Å | |||||||||
![]() | Qu K / Chen Z | |||||||||
Funding support | 1 items
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![]() | ![]() 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. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
Map data | ![]() | 2.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 34.6 KB 34.6 KB | Display Display | ![]() |
Images | ![]() | 28.7 KB | ||
Filedesc metadata | ![]() | 11.8 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 420.2 KB | Display | ![]() |
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Full document | ![]() | 419.8 KB | Display | |
Data in XML | ![]() | 5 KB | Display | |
Data in CIF | ![]() | 5.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7vvzMC ![]() 7vvuC ![]() 7vvyC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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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
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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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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.6 |
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Vitrification | Cryogen name: NITROGEN |
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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: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.3 µm |
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Image processing
Startup model | Type of model: OTHER |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 8.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 474949 |
Initial angle assignment | Type: ANGULAR RECONSTITUTION |
Final angle assignment | Type: ANGULAR RECONSTITUTION |