+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-38317 | |||||||||
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タイトル | Structure of yeast replisome associated with FACT and histone hexamer, Composite map | |||||||||
マップデータ | ||||||||||
試料 |
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キーワード | Replisome / FACT / histone hexamer / REPLICATION | |||||||||
機能・相同性 | 機能・相同性情報 Regulation of TP53 Activity through Phosphorylation / regulation of sister chromatid cohesion / establishment of sister chromatid cohesion / maintenance of DNA repeat elements / DNA-templated DNA replication maintenance of fidelity / gene conversion / HATs acetylate histones / FACT complex / Unwinding of DNA / replication fork arrest ...Regulation of TP53 Activity through Phosphorylation / regulation of sister chromatid cohesion / establishment of sister chromatid cohesion / maintenance of DNA repeat elements / DNA-templated DNA replication maintenance of fidelity / gene conversion / HATs acetylate histones / FACT complex / Unwinding of DNA / replication fork arrest / Cul8-RING ubiquitin ligase complex / regulation of nuclear cell cycle DNA replication / DNA replication initiation / meiotic chromosome segregation / Condensation of Prophase Chromosomes / SIRT1 negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / MCM core complex / Assembly of the pre-replicative complex / Switching of origins to a post-replicative state / epsilon DNA polymerase complex / DNA strand elongation involved in mitotic DNA replication / MCM complex binding / Assembly of the ORC complex at the origin of replication / GINS complex / nuclear DNA replication / regulation of chromatin organization / mitotic DNA replication preinitiation complex assembly / HDACs deacetylate histones / premeiotic DNA replication / pre-replicative complex assembly involved in nuclear cell cycle DNA replication / SUMO binding / nucleotide-excision repair, DNA gap filling / anaphase-promoting complex binding / mitotic DNA replication / Activation of the pre-replicative complex / nucleosome organization / DNA replication proofreading / CMG complex / nuclear pre-replicative complex / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / DNA replication checkpoint signaling / establishment of mitotic sister chromatid cohesion / single-stranded DNA 3'-5' DNA exonuclease activity / Activation of ATR in response to replication stress / DNA replication preinitiation complex / MCM complex / replication fork protection complex / Termination of translesion DNA synthesis / RMTs methylate histone arginines / Oxidative Stress Induced Senescence / mitotic DNA replication checkpoint signaling / double-strand break repair via break-induced replication / cellular response to osmotic stress / mitotic DNA replication initiation / single-stranded DNA helicase activity / regulation of DNA-templated DNA replication initiation / mitotic intra-S DNA damage checkpoint signaling / DNA strand elongation involved in DNA replication / silent mating-type cassette heterochromatin formation / prenyltransferase activity / 加水分解酵素; エステル加水分解酵素; 5'-リン酸モノエステル産生エンドデオキシリボヌクレアーゼ / mitotic sister chromatid cohesion / 3'-5' DNA helicase activity / nuclear chromosome / TP53 Regulates Transcription of DNA Repair Genes / isoprenoid biosynthetic process / leading strand elongation / RNA Polymerase II Pre-transcription Events / DNA unwinding involved in DNA replication / RNA Polymerase I Promoter Escape / replication fork processing / nuclear replication fork / mitotic G2 DNA damage checkpoint signaling / DNA replication origin binding / Estrogen-dependent gene expression / rRNA transcription / Dual incision in TC-NER / positive regulation of RNA polymerase II transcription preinitiation complex assembly / DNA replication initiation / subtelomeric heterochromatin formation / error-prone translesion synthesis / positive regulation of transcription initiation by RNA polymerase II / Ub-specific processing proteases / base-excision repair, gap-filling / nucleosomal DNA binding / DNA helicase activity / telomere maintenance / nuclear periphery / replication fork / meiotic cell cycle / helicase activity / transcription elongation by RNA polymerase II / base-excision repair / heterochromatin formation / DNA-templated DNA replication / double-strand break repair via nonhomologous end joining / structural constituent of chromatin / nucleosome / double-strand break repair 類似検索 - 分子機能 | |||||||||
生物種 | Saccharomyces cerevisiae (パン酵母) | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 3.7 Å | |||||||||
データ登録者 | Li N / Gao Y / Yu D / Gao N / Zhai Y | |||||||||
資金援助 | 中国, 1件
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引用 | ジャーナル: Nature / 年: 2024 タイトル: Parental histone transfer caught at the replication fork. 著者: 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 ...著者: 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 / 要旨: 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. | |||||||||
履歴 |
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-構造の表示
添付画像 |
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-ダウンロードとリンク
-EMDBアーカイブ
マップデータ | emd_38317.map.gz | 44.2 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-38317-v30.xml emd-38317.xml | 47.1 KB 47.1 KB | 表示 表示 | EMDBヘッダ |
画像 | emd_38317.png | 117.7 KB | ||
Filedesc metadata | emd-38317.cif.gz | 16.4 KB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-38317 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-38317 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_38317_validation.pdf.gz | 419.1 KB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_38317_full_validation.pdf.gz | 418.6 KB | 表示 | |
XML形式データ | emd_38317_validation.xml.gz | 7.5 KB | 表示 | |
CIF形式データ | emd_38317_validation.cif.gz | 8.7 KB | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-38317 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-38317 | HTTPS FTP |
-関連構造データ
-リンク
EMDBのページ | EMDB (EBI/PDBe) / EMDataResource |
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「今月の分子」の関連する項目 |
-マップ
ファイル | ダウンロード / ファイル: emd_38317.map.gz / 形式: CCP4 / 大きさ: 244.1 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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投影像・断面図 | 画像のコントロール
画像は Spider により作成 | ||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 1.06 Å | ||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
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-添付データ
-試料の構成要素
+全体 : Endogenous replisomes
+超分子 #1: Endogenous replisomes
+分子 #1: DNA replication licensing factor MCM2
+分子 #2: DNA replication licensing factor MCM3
+分子 #3: DNA replication licensing factor MCM4
+分子 #4: Minichromosome maintenance protein 5
+分子 #5: DNA replication licensing factor MCM6
+分子 #6: DNA replication licensing factor MCM7
+分子 #7: DNA polymerase epsilon catalytic subunit A
+分子 #8: DNA polymerase epsilon subunit B
+分子 #9: DNA replication complex GINS protein PSF1
+分子 #10: DNA replication complex GINS protein PSF2
+分子 #11: DNA replication complex GINS protein PSF3
+分子 #12: DNA replication complex GINS protein SLD5
+分子 #13: Cell division control protein 45
+分子 #14: DNA polymerase alpha-binding protein
+分子 #15: Topoisomerase 1-associated factor 1
+分子 #16: Chromosome segregation in meiosis protein 3
+分子 #17: Mediator of replication checkpoint protein 1
+分子 #18: FACT complex subunit SPT16
+分子 #19: FACT complex subunit POB3
+分子 #20: Histone H3
+分子 #21: Histone H4
+分子 #22: Histone H2A.1
+分子 #23: Histone H2B.2
+分子 #24: DNA (51-MER)
+分子 #25: DNA (39-MER)
+分子 #26: ZINC ION
+分子 #27: ADENOSINE-5'-DIPHOSPHATE
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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解析 | 単粒子再構成法 |
試料の集合状態 | particle |
-試料調製
緩衝液 | pH: 7.5 |
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凍結 | 凍結剤: ETHANE |
-電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
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撮影 | フィルム・検出器のモデル: GATAN K3 BIOQUANTUM (6k x 4k) 平均電子線量: 50.0 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: FIELD EMISSION GUN |
電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 2.5 µm / 最小 デフォーカス(公称値): 1.0 µm |
実験機器 | モデル: Titan Krios / 画像提供: FEI Company |
-画像解析
初期モデル | モデルのタイプ: NONE |
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最終 再構成 | 解像度のタイプ: BY AUTHOR / 解像度: 3.7 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 524000 |
初期 角度割当 | タイプ: PROJECTION MATCHING |
最終 角度割当 | タイプ: PROJECTION MATCHING |