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Yorodumi- EMDB-38407: Structural basis for the linker histone H5-nucleosome binding and... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-38407 | |||||||||||||||||||||||||||||||||
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Title | Structural basis for the linker histone H5-nucleosome binding and chromatin compaction | |||||||||||||||||||||||||||||||||
Map data | ||||||||||||||||||||||||||||||||||
Sample |
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Keywords | Chromatin Fiber / Histone / DNA / Linker Histone / Nucleosome / Epigenetics / Genome Folding / Interaction / GENE REGULATION | |||||||||||||||||||||||||||||||||
Function / homology | Function and homology information negative regulation of DNA recombination / chromosome condensation / nucleosomal DNA binding / structural constituent of chromatin / nucleosome / nucleosome assembly / chromatin organization / double-stranded DNA binding / protein heterodimerization activity / DNA binding / nucleus Similarity search - Function | |||||||||||||||||||||||||||||||||
Biological species | synthetic construct (others) / Xenopus laevis (African clawed frog) / Gallus gallus (chicken) | |||||||||||||||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.6 Å | |||||||||||||||||||||||||||||||||
Authors | Li WY / Song F / Zhu P | |||||||||||||||||||||||||||||||||
Funding support | China, United States, 10 items
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Citation | Journal: Cell Res / Year: 2024 Title: Structural basis for linker histone H5-nucleosome binding and chromatin fiber compaction. Authors: Wenyan Li / Jie Hu / Feng Song / Juan Yu / Xin Peng / Shuming Zhang / Lin Wang / Mingli Hu / Jia-Cheng Liu / Yu Wei / Xue Xiao / Yan Li / Dongyu Li / Hui Wang / Bing-Rui Zhou / Linchang Dai ...Authors: Wenyan Li / Jie Hu / Feng Song / Juan Yu / Xin Peng / Shuming Zhang / Lin Wang / Mingli Hu / Jia-Cheng Liu / Yu Wei / Xue Xiao / Yan Li / Dongyu Li / Hui Wang / Bing-Rui Zhou / Linchang Dai / Zongjun Mou / Min Zhou / Haonan Zhang / Zheng Zhou / Huidong Zhang / Yawen Bai / Jin-Qiu Zhou / Wei Li / Guohong Li / Ping Zhu / Abstract: The hierarchical packaging of chromatin fibers plays a critical role in gene regulation. The 30-nm chromatin fibers, a central-level structure bridging nucleosomal arrays to higher-order ...The hierarchical packaging of chromatin fibers plays a critical role in gene regulation. The 30-nm chromatin fibers, a central-level structure bridging nucleosomal arrays to higher-order organizations, function as the first level of transcriptional dormant chromatin. The dynamics of 30-nm chromatin fiber play a crucial role in biological processes related to DNA. Here, we report a 3.6-angstrom resolution cryogenic electron microscopy structure of H5-bound dodecanucleosome, i.e., the chromatin fiber reconstituted in the presence of linker histone H5, which shows a two-start left-handed double helical structure twisted by tetranucleosomal units. An atomic structural model of the H5-bound chromatin fiber, including an intact chromatosome, is built, which provides structural details of the full-length linker histone H5, including its N-terminal domain and an HMG-motif-like C-terminal domain. The chromatosome structure shows that H5 binds the nucleosome off-dyad through a three-contact mode in the chromatin fiber. More importantly, the H5-chromatin structure provides a fine molecular basis for the intra-tetranucleosomal and inter-tetranucleosomal interactions. In addition, we systematically validated the physiological functions and structural characteristics of the tetranucleosomal unit through a series of genetic and genomic studies in Saccharomyces cerevisiae and in vitro biophysical experiments. Furthermore, our structure reveals that multiple structural asymmetries of histone tails confer a polarity to the chromatin fiber. These findings provide structural and mechanistic insights into how a nucleosomal array folds into a higher-order chromatin fiber with a polarity in vitro and in vivo. | |||||||||||||||||||||||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_38407.map.gz | 12.7 MB | EMDB map data format | |
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Header (meta data) | emd-38407-v30.xml emd-38407.xml | 44.4 KB 44.4 KB | Display Display | EMDB header |
Images | emd_38407.png | 126.7 KB | ||
Filedesc metadata | emd-38407.cif.gz | 8.3 KB | ||
Others | emd_38407_half_map_1.map.gz emd_38407_half_map_2.map.gz | 71.3 MB 71.3 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-38407 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-38407 | HTTPS FTP |
-Validation report
Summary document | emd_38407_validation.pdf.gz | 886.3 KB | Display | EMDB validaton report |
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Full document | emd_38407_full_validation.pdf.gz | 885.9 KB | Display | |
Data in XML | emd_38407_validation.xml.gz | 12.8 KB | Display | |
Data in CIF | emd_38407_validation.cif.gz | 15.3 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-38407 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-38407 | HTTPS FTP |
-Related structure data
Related structure data | 8xjvMC C: citing same article (ref.) M: atomic model generated by this map |
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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_38407.map.gz / Format: CCP4 / Size: 91.1 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: 1.76 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_38407_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_38407_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
+Entire : 12x177bp-H5 chromatin
+Supramolecule #1: 12x177bp-H5 chromatin
+Supramolecule #2: Widom 601 DNA
+Supramolecule #3: Histone H2A
+Supramolecule #4: Histone H2B
+Supramolecule #5: Histone H3.1
+Supramolecule #6: Histone H4
+Supramolecule #7: Linker histone H5
+Macromolecule #1: DNA
+Macromolecule #2: DNA
+Macromolecule #3: Histone H2A
+Macromolecule #4: Histone H2B 1.1
+Macromolecule #5: Histone H3
+Macromolecule #6: Histone H4
+Macromolecule #7: Histone H5
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
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Grid | Model: Quantifoil R2/1 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: NITROGEN |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Detector mode: COUNTING / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 2.0 µm / Nominal magnification: 47000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: EMDB MAP EMDB ID: |
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Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0) / Number images used: 13670 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
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Output model | PDB-8xjv: |