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Yorodumi- EMDB-38317: Structure of yeast replisome associated with FACT and histone hex... -
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| Title | Structure of yeast replisome associated with FACT and histone hexamer, Composite map | |||||||||
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Keywords | Replisome / FACT / histone hexamer / REPLICATION | |||||||||
| Function / homology | Function and homology informationRegulation of TP53 Activity through Phosphorylation / : / establishment of sister chromatid cohesion / regulation of sister chromatid cohesion / DNA-templated DNA replication maintenance of fidelity / gene conversion / Unwinding of DNA / maintenance of DNA repeat elements / FACT complex / regulation of nuclear cell cycle DNA replication ...Regulation of TP53 Activity through Phosphorylation / : / establishment of sister chromatid cohesion / regulation of sister chromatid cohesion / DNA-templated DNA replication maintenance of fidelity / gene conversion / Unwinding of DNA / maintenance of DNA repeat elements / FACT complex / regulation of nuclear cell cycle DNA replication / DNA replication initiation / replication fork protection complex / replication fork arrest / Cul8-RING ubiquitin ligase complex / meiotic chromosome segregation / HATs acetylate histones / RNA polymerase I upstream activating factor complex / Condensation of Prophase Chromosomes / epsilon DNA polymerase complex / : / : / MCM core complex / Assembly of the pre-replicative complex / Switching of origins to a post-replicative state / DNA strand elongation involved in mitotic DNA replication / GINS complex / MCM complex binding / mitotic DNA replication preinitiation complex assembly / nuclear DNA replication / : / premeiotic DNA replication / Assembly of the ORC complex at the origin of replication / regulation of chromatin organization / HDACs deacetylate histones / pre-replicative complex assembly involved in nuclear cell cycle DNA replication / anaphase-promoting complex binding / nucleotide-excision repair, DNA gap filling / Activation of the pre-replicative complex / SUMO binding / mitotic DNA replication / DNA replication checkpoint signaling / CMG complex / establishment of mitotic sister chromatid cohesion / nuclear pre-replicative complex / DNA replication proofreading / nucleosome organization / : / DNA replication preinitiation complex / Activation of ATR in response to replication stress / single-stranded DNA 3'-5' DNA exonuclease activity / mitotic DNA replication checkpoint signaling / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / MCM complex / Oxidative Stress Induced Senescence / double-strand break repair via break-induced replication / mitotic DNA replication initiation / RMTs methylate histone arginines / cellular response to osmotic stress / single-stranded DNA helicase activity / SUMOylation of chromatin organization proteins / mitotic intra-S DNA damage checkpoint signaling / silent mating-type cassette heterochromatin formation / regulation of DNA-templated DNA replication initiation / mitotic sister chromatid cohesion / Hydrolases; Acting on ester bonds; Exodeoxyribonucleases producing 5'-phosphomonoesters / TP53 Regulates Transcription of DNA Repair Genes / DNA strand elongation involved in DNA replication / RNA Polymerase II Pre-transcription Events / nuclear chromosome / leading strand elongation / RNA Polymerase I Promoter Escape / mitotic G2 DNA damage checkpoint signaling / positive regulation of transcription by RNA polymerase I / nucleolar large rRNA transcription by RNA polymerase I / Estrogen-dependent gene expression / nuclear replication fork / 3'-5' DNA helicase activity / rRNA transcription / replication fork processing / Dual incision in TC-NER / DNA replication origin binding / positive regulation of RNA polymerase II transcription preinitiation complex assembly / DNA replication initiation / error-prone translesion synthesis / positive regulation of transcription initiation by RNA polymerase II / Ub-specific processing proteases / subtelomeric heterochromatin formation / base-excision repair, gap-filling / nuclear periphery / telomere maintenance / DNA helicase activity / replication fork / helicase activity / meiotic cell cycle / transcription elongation by RNA polymerase II / base-excision repair / DNA-templated DNA replication / double-strand break repair via nonhomologous end joining / structural constituent of chromatin / peroxisome Similarity search - Function | |||||||||
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| Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | |||||||||
Authors | Li N / Gao Y / Yu D / Gao N / Zhai Y | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Nature / Year: 2024Title: Parental histone transfer caught at the replication fork. Authors: Ningning Li / Yuan Gao / Yujie Zhang / Daqi Yu / Jianwei Lin / Jianxun Feng / Jian Li / Zhichun Xu / Yingyi Zhang / Shangyu Dang / Keda Zhou / Yang Liu / Xiang David Li / Bik Kwoon Tye / ...Authors: Ningning Li / Yuan Gao / Yujie Zhang / Daqi Yu / Jianwei Lin / Jianxun Feng / Jian Li / Zhichun Xu / Yingyi Zhang / Shangyu Dang / Keda Zhou / Yang Liu / Xiang David Li / Bik Kwoon Tye / Qing Li / Ning Gao / Yuanliang Zhai / ![]() Abstract: In eukaryotes, DNA compacts into chromatin through nucleosomes. Replication of the eukaryotic genome must be coupled to the transmission of the epigenome encoded in the chromatin. Here we report cryo- ...In eukaryotes, DNA compacts into chromatin through nucleosomes. Replication of the eukaryotic genome must be coupled to the transmission of the epigenome encoded in the chromatin. Here we report cryo-electron microscopy structures of yeast (Saccharomyces cerevisiae) replisomes associated with the FACT (facilitates chromatin transactions) complex (comprising Spt16 and Pob3) and an evicted histone hexamer. In these structures, FACT is positioned at the front end of the replisome by engaging with the parental DNA duplex to capture the histones through the middle domain and the acidic carboxyl-terminal domain of Spt16. The H2A-H2B dimer chaperoned by the carboxyl-terminal domain of Spt16 is stably tethered to the H3-H4 tetramer, while the vacant H2A-H2B site is occupied by the histone-binding domain of Mcm2. The Mcm2 histone-binding domain wraps around the DNA-binding surface of one H3-H4 dimer and extends across the tetramerization interface of the H3-H4 tetramer to the binding site of Spt16 middle domain before becoming disordered. This arrangement leaves the remaining DNA-binding surface of the other H3-H4 dimer exposed to additional interactions for further processing. The Mcm2 histone-binding domain and its downstream linker region are nested on top of Tof1, relocating the parental histones to the replisome front for transfer to the newly synthesized lagging-strand DNA. Our findings offer crucial structural insights into the mechanism of replication-coupled histone recycling for maintaining epigenetic inheritance. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_38317.map.gz | 44.2 MB | EMDB map data format | |
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| Header (meta data) | emd-38317-v30.xml emd-38317.xml | 47.1 KB 47.1 KB | Display Display | EMDB header |
| Images | emd_38317.png | 117.7 KB | ||
| Filedesc metadata | emd-38317.cif.gz | 16.4 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-38317 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-38317 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8xgcMC C: citing same article ( M: atomic model generated by this map |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_38317.map.gz / Format: CCP4 / Size: 244.1 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: 1.06 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 : Endogenous replisomes
+Supramolecule #1: Endogenous replisomes
+Macromolecule #1: DNA replication licensing factor MCM2
+Macromolecule #2: DNA replication licensing factor MCM3
+Macromolecule #3: DNA replication licensing factor MCM4
+Macromolecule #4: Minichromosome maintenance protein 5
+Macromolecule #5: DNA replication licensing factor MCM6
+Macromolecule #6: DNA replication licensing factor MCM7
+Macromolecule #7: DNA polymerase epsilon catalytic subunit A
+Macromolecule #8: DNA polymerase epsilon subunit B
+Macromolecule #9: DNA replication complex GINS protein PSF1
+Macromolecule #10: DNA replication complex GINS protein PSF2
+Macromolecule #11: DNA replication complex GINS protein PSF3
+Macromolecule #12: DNA replication complex GINS protein SLD5
+Macromolecule #13: Cell division control protein 45
+Macromolecule #14: DNA polymerase alpha-binding protein
+Macromolecule #15: Topoisomerase 1-associated factor 1
+Macromolecule #16: Chromosome segregation in meiosis protein 3
+Macromolecule #17: Mediator of replication checkpoint protein 1
+Macromolecule #18: FACT complex subunit SPT16
+Macromolecule #19: FACT complex subunit POB3
+Macromolecule #20: Histone H3
+Macromolecule #21: Histone H4
+Macromolecule #22: Histone H2A.1
+Macromolecule #23: Histone H2B.2
+Macromolecule #24: DNA (51-MER)
+Macromolecule #25: DNA (39-MER)
+Macromolecule #26: ZINC ION
+Macromolecule #27: ADENOSINE-5'-DIPHOSPHATE
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (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: 2.5 µm / Nominal defocus min: 1.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Startup model | Type of model: NONE |
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| Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 524000 |
| Initial angle assignment | Type: PROJECTION MATCHING |
| Final angle assignment | Type: PROJECTION MATCHING |
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Keywords
Authors
China, 1 items
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FIELD EMISSION GUN
