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Yorodumi- PDB-8xgc: Structure of yeast replisome associated with FACT and histone hex... -
+Open data
-Basic information
Entry | Database: PDB / ID: 8xgc | ||||||
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Title | Structure of yeast replisome associated with FACT and histone hexamer, Composite map | ||||||
Components |
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Keywords | REPLICATION / Replisome / FACT / histone hexamer | ||||||
Function / homology | Function and homology information Regulation of TP53 Activity through Phosphorylation / regulation of sister chromatid cohesion / establishment of sister chromatid cohesion / DNA-templated DNA replication maintenance of fidelity / gene conversion / maintenance of DNA repeat elements / Unwinding of DNA / HDMs demethylate histones / HATs acetylate histones / FACT complex ...Regulation of TP53 Activity through Phosphorylation / regulation of sister chromatid cohesion / establishment of sister chromatid cohesion / DNA-templated DNA replication maintenance of fidelity / gene conversion / maintenance of DNA repeat elements / Unwinding of DNA / HDMs demethylate histones / HATs acetylate histones / FACT complex / replication fork arrest / regulation of nuclear cell cycle DNA replication / DNA replication initiation / Cul8-RING ubiquitin ligase complex / Condensation of Prophase Chromosomes / RNA polymerase I upstream activating factor complex / meiotic chromosome segregation / epsilon DNA polymerase complex / DNA strand elongation involved in mitotic DNA replication / MCM core complex / Assembly of the pre-replicative complex / Switching of origins to a post-replicative state / nuclear DNA replication / MCM complex binding / regulation of chromatin organization / GINS complex / mitotic DNA replication preinitiation complex assembly / premeiotic DNA replication / nucleosome organization / pre-replicative complex assembly involved in nuclear cell cycle DNA replication / nucleotide-excision repair, DNA gap filling / SUMO binding / mitotic DNA replication / DNA replication proofreading / Activation of the pre-replicative complex / anaphase-promoting complex binding / CMG complex / SUMOylation of chromatin organization proteins / single-stranded DNA 3'-5' DNA exonuclease activity / establishment of mitotic sister chromatid cohesion / DNA replication checkpoint signaling / nuclear pre-replicative complex / Activation of ATR in response to replication stress / MCM complex / DNA replication preinitiation complex / double-strand break repair via break-induced replication / mitotic DNA replication checkpoint signaling / replication fork protection complex / mitotic DNA replication initiation / single-stranded DNA helicase activity / RMTs methylate histone arginines / mitotic intra-S DNA damage checkpoint signaling / Hydrolases; Acting on ester bonds; Exodeoxyribonucleases producing 5'-phosphomonoesters / silent mating-type cassette heterochromatin formation / regulation of DNA-templated DNA replication initiation / DNA strand elongation involved in DNA replication / mitotic sister chromatid cohesion / leading strand elongation / nuclear chromosome / TP53 Regulates Transcription of DNA Repair Genes / DNA unwinding involved in DNA replication / replication fork processing / RNA Polymerase II Pre-transcription Events / positive regulation of transcription by RNA polymerase I / DNA replication origin binding / nuclear replication fork / nucleolar large rRNA transcription by RNA polymerase I / mitotic G2 DNA damage checkpoint signaling / subtelomeric heterochromatin formation / DNA replication initiation / positive regulation of transcription initiation by RNA polymerase II / positive regulation of RNA polymerase II transcription preinitiation complex assembly / error-prone translesion synthesis / heterochromatin formation / base-excision repair, gap-filling / DNA helicase activity / telomere maintenance / nuclear periphery / meiotic cell cycle / replication fork / helicase activity / transcription elongation by RNA polymerase II / base-excision repair / DNA-templated DNA replication / nucleosome assembly / double-strand break repair via nonhomologous end joining / structural constituent of chromatin / double-strand break repair / nucleosome / single-stranded DNA binding / mitotic cell cycle / chromatin organization / 4 iron, 4 sulfur cluster binding / double-stranded DNA binding / DNA helicase / DNA replication / chromosome, telomeric region / DNA-directed DNA polymerase / DNA-directed DNA polymerase activity / hydrolase activity Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.7 Å | ||||||
Authors | Li, N. / Gao, Y. / Yu, D. / Gao, N. / Zhai, Y. | ||||||
Funding support | China, 1items
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Citation | Journal: Nature / Year: 2024 Title: 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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8xgc.cif.gz | 1.9 MB | Display | PDBx/mmCIF format |
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PDB format | pdb8xgc.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 8xgc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xg/8xgc ftp://data.pdbj.org/pub/pdb/validation_reports/xg/8xgc | HTTPS FTP |
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-Related structure data
Related structure data | 38317MC C: citing same article (ref.) M: map data used to model this data |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-DNA replication licensing factor ... , 5 types, 5 molecules 23467
#1: Protein | Mass: 98911.539 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: A0A6A5Q1S9 |
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#2: Protein | Mass: 107653.508 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P24279, DNA helicase |
#3: Protein | Mass: 105138.375 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P30665, DNA helicase |
#5: Protein | Mass: 113110.211 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P53091, DNA helicase |
#6: Protein | Mass: 95049.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: A0A8H4BTB2 |
-Protein , 10 types, 14 molecules 5EFGHIJKNROSPQ
#4: Protein | Mass: 86505.734 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P29496, DNA helicase | ||||||||||||||
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#13: Protein | Mass: 74324.836 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: Q08032 | ||||||||||||||
#14: Protein | Mass: 104543.391 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: Q01454 #15: Protein | | Mass: 141296.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P53840 #16: Protein | | Mass: 36402.590 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: Q04659 #17: Protein | | Mass: 124516.375 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P25588 #20: Protein | Mass: 15391.007 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: A0A6A5Q536 #21: Protein | Mass: 11395.390 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P02309 #22: Protein | | Mass: 14013.177 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P04911 #23: Protein | | Mass: 14264.341 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P02294 |
-DNA polymerase epsilon ... , 2 types, 2 molecules 89
#7: Protein | Mass: 255992.484 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) References: UniProt: P21951, DNA-directed DNA polymerase, Hydrolases; Acting on ester bonds; Exodeoxyribonucleases producing 5'-phosphomonoesters |
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#8: Protein | Mass: 78425.852 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P24482 |
-DNA replication complex GINS protein ... , 4 types, 4 molecules ABCD
#9: Protein | Mass: 24230.576 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: Q12488 |
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#10: Protein | Mass: 29341.074 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) |
#11: Protein | Mass: 21977.135 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: Q12146 |
#12: Protein | Mass: 33983.617 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: Q03406 |
-FACT complex subunit ... , 2 types, 2 molecules LM
#18: Protein | Mass: 118776.984 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P32558 |
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#19: Protein | Mass: 63068.594 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: Q04636 |
-DNA chain , 2 types, 2 molecules XY
#24: DNA chain | Mass: 15689.072 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) |
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#25: DNA chain | Mass: 11935.764 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) |
-Non-polymers , 2 types, 12 molecules
#26: Chemical | ChemComp-ZN / #27: Chemical | ChemComp-ADP / |
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-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Endogenous replisomes / Type: COMPLEX / Entity ID: #1-#25 / Source: NATURAL |
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Source (natural) | Organism: Saccharomyces cerevisiae (brewer's yeast) |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2500 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
-Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction | Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 524000 / Symmetry type: POINT |