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基本情報
登録情報 | ![]() | |||||||||||||||||||||||||||
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タイトル | RNA polymerase II elongation complex bound with Rad26 and Elf1, stalled at SHL(-3.5) of the nucleosome | |||||||||||||||||||||||||||
![]() | RNA polymerase II elongation complex bound with Elf1 and Rad26, stalled at SHL(-3.5) of the nucleosome | |||||||||||||||||||||||||||
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![]() | Transcription / RNA / DNA / Repair | |||||||||||||||||||||||||||
機能・相同性 | ![]() regulation of septum digestion after cytokinesis / siRNA-mediated pericentric heterochromatin formation / RPB4-RPB7 complex / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / ATP-dependent chromatin remodeler activity / termination of RNA polymerase II transcription / termination of RNA polymerase III transcription / : / : / termination of RNA polymerase I transcription ...regulation of septum digestion after cytokinesis / siRNA-mediated pericentric heterochromatin formation / RPB4-RPB7 complex / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / ATP-dependent chromatin remodeler activity / termination of RNA polymerase II transcription / termination of RNA polymerase III transcription / : / : / termination of RNA polymerase I transcription / RNA polymerase II complex binding / transcription initiation at RNA polymerase III promoter / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / transcription initiation at RNA polymerase I promoter / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / negative regulation of tumor necrosis factor-mediated signaling pathway / transcription elongation by RNA polymerase I / negative regulation of megakaryocyte differentiation / positive regulation of translational initiation / heterochromatin organization / RNA polymerase I complex / RNA polymerase III complex / protein localization to CENP-A containing chromatin / transcription-coupled nucleotide-excision repair / RNA polymerase III activity / RNA polymerase II, core complex / pericentric heterochromatin / tRNA transcription by RNA polymerase III / Replacement of protamines by nucleosomes in the male pronucleus / RNA polymerase I activity / CENP-A containing nucleosome / Packaging Of Telomere Ends / RNA polymerase II activity / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / Deposition of new CENPA-containing nucleosomes at the centromere / nucleosomal DNA binding / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / translation initiation factor binding / Inhibition of DNA recombination at telomere / Meiotic synapsis / telomere organization / RNA Polymerase I Promoter Opening / Assembly of the ORC complex at the origin of replication / SUMOylation of chromatin organization proteins / DNA methylation / Condensation of Prophase Chromosomes / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / SIRT1 negatively regulates rRNA expression / Chromatin modifications during the maternal to zygotic transition (MZT) / HCMV Late Events / innate immune response in mucosa / transcription elongation factor complex / PRC2 methylates histones and DNA / Defective pyroptosis / HDACs deacetylate histones / transcription elongation by RNA polymerase II / RNA Polymerase I Promoter Escape / lipopolysaccharide binding / transcription initiation at RNA polymerase II promoter / Nonhomologous End-Joining (NHEJ) / Transcriptional regulation by small RNAs / Formation of the beta-catenin:TCF transactivating complex / P-body / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / NoRC negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / B-WICH complex positively regulates rRNA expression / G2/M DNA damage checkpoint / HDMs demethylate histones / DNA Damage/Telomere Stress Induced Senescence / Metalloprotease DUBs / ribonucleoside binding / PKMTs methylate histone lysines / Meiotic recombination / RMTs methylate histone arginines / Pre-NOTCH Transcription and Translation / DNA-directed 5'-3' RNA polymerase activity / Activation of anterior HOX genes in hindbrain development during early embryogenesis / DNA-directed RNA polymerase / HCMV Early Events / Transcriptional regulation of granulopoiesis / structural constituent of chromatin / antimicrobial humoral immune response mediated by antimicrobial peptide / UCH proteinases / nucleosome / nucleosome assembly / E3 ubiquitin ligases ubiquitinate target proteins / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / chromatin organization / RUNX1 regulates transcription of genes involved in differentiation of HSCs / single-stranded DNA binding / HATs acetylate histones / Processing of DNA double-strand break ends / antibacterial humoral response / Senescence-Associated Secretory Phenotype (SASP) / Oxidative Stress Induced Senescence / defense response to Gram-negative bacterium / Estrogen-dependent gene expression 類似検索 - 分子機能 | |||||||||||||||||||||||||||
生物種 | ![]() ![]() | |||||||||||||||||||||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 6.95 Å | |||||||||||||||||||||||||||
![]() | Osumi K / Kujirai T / Ehara H / Kinoshita C / Saotome M / Kagawa W / Sekine S / Takizawa Y / Kurumizaka H | |||||||||||||||||||||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Structural Basis of Damaged Nucleotide Recognition by Transcribing RNA Polymerase II in the Nucleosome. 著者: Ken Osumi / Tomoya Kujirai / Haruhiko Ehara / Mitsuo Ogasawara / Chiaki Kinoshita / Mika Saotome / Wataru Kagawa / Shun-Ichi Sekine / Yoshimasa Takizawa / Hitoshi Kurumizaka / ![]() 要旨: In transcription-coupled repair (TCR), transcribing RNA polymerase II (RNAPII) stalls at a DNA lesion and recruits TCR proteins to the damaged site. However, the mechanism by which RNAPII recognizes ...In transcription-coupled repair (TCR), transcribing RNA polymerase II (RNAPII) stalls at a DNA lesion and recruits TCR proteins to the damaged site. However, the mechanism by which RNAPII recognizes a DNA lesion in the nucleosome remains enigmatic. In the present study, we inserted an apurinic/apyrimidinic DNA lesion analogue, tetrahydrofuran (THF), in the nucleosomal DNA, where RNAPII stalls at the SHL(-4), SHL(-3.5), and SHL(-3) positions, and determined the structures of these complexes by cryo-electron microscopy. In the RNAPII-nucleosome complex stalled at SHL(-3.5), the nucleosome orientation relative to RNAPII is quite different from those in the SHL(-4) and SHL(-3) complexes, which have nucleosome orientations similar to naturally paused RNAPII-nucleosome complexes. Furthermore, we found that an essential TCR protein, Rad26 (CSB), enhances the RNAPII processivity, and consequently augments the DNA damage recognition efficiency of RNAPII in the nucleosome. The cryo-EM structure of the Rad26-RNAPII-nucleosome complex revealed that Rad26 binds to the stalled RNAPII through a novel interface, which is completely different from those previously reported. These structures may provide important information to understand the mechanism by which RNAPII recognizes the nucleosomal DNA lesion and recruits TCR proteins to the stalled RNAPII on the nucleosome. | |||||||||||||||||||||||||||
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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 | ![]() | 228.5 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 61.3 KB 61.3 KB | 表示 表示 | ![]() |
FSC (解像度算出) | ![]() | 14.3 KB | 表示 | ![]() |
画像 | ![]() | 90.8 KB | ||
マスクデータ | ![]() ![]() ![]() | 244.1 MB 244.1 MB 244.1 MB | ![]() | |
Filedesc metadata | ![]() | 12 KB | ||
その他 | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() | 193.9 MB 194.2 MB 194.2 MB 193.8 MB 208.4 MB 228.8 MB 228.8 MB 194.7 MB 194.5 MB | ||
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-検証レポート
文書・要旨 | ![]() | 1.1 MB | 表示 | ![]() |
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文書・詳細版 | ![]() | 1.1 MB | 表示 | |
XML形式データ | ![]() | 21.6 KB | 表示 | |
CIF形式データ | ![]() | 28.6 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
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リンク
EMDBのページ | ![]() ![]() |
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「今月の分子」の関連する項目 |
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マップ
ファイル | ![]() | ||||||||||||||||||||
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注釈 | RNA polymerase II elongation complex bound with Elf1 and Rad26, stalled at SHL(-3.5) of the nucleosome | ||||||||||||||||||||
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
+マスク #1
+マスク #2
+マスク #3
+追加マップ: Half map 1 of the Rad26-RNAPII interface map
+追加マップ: Half map 2 of the Rad26-RNAPII interface map
+追加マップ: Half map 1 of the Rad26 map
+追加マップ: Half map 2 of the Rad26 map
+追加マップ: Postprocessed map of the Rad26-RNAPII interface map
+追加マップ: Postprocessed map of the Rad26 map
+追加マップ: Postprocessed map of the Rad26 map
+ハーフマップ: Half map 2 of the main map
+ハーフマップ: Half map 1 of the main map
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試料の構成要素
+全体 : RNA polymerase II elongation complex bound with Rad26 and Elf1, s...
+超分子 #1: RNA polymerase II elongation complex bound with Rad26 and Elf1, s...
+超分子 #2: RNA polymerase II elongation complex
+超分子 #3: Histone
+超分子 #4: DNA, RNA
+超分子 #5: Rad26
+超分子 #6: Transcription elongation factor Elf1
+分子 #1: DNA-directed RNA polymerase subunit
+分子 #2: DNA-directed RNA polymerase subunit beta
+分子 #3: RNA polymerase II third largest subunit B44, part of central core
+分子 #4: RNA polymerase II subunit B32
+分子 #5: DNA-directed RNA polymerases I, II, and III subunit RPABC1
+分子 #6: RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III
+分子 #7: RNA polymerase II subunit
+分子 #8: DNA-directed RNA polymerases I, II, and III subunit RPABC3
+分子 #9: DNA-directed RNA polymerase subunit
+分子 #10: RNA polymerase subunit ABC10-beta, common to RNA polymerases I, I...
+分子 #11: RNA polymerase II subunit B12.5
+分子 #12: RNA polymerase subunit ABC10-alpha
+分子 #13: Transcription elongation factor 1 homolog
+分子 #15: DNA repair protein
+分子 #18: Histone H3.1
+分子 #19: Histone H4
+分子 #20: Histone H2A type 1-B/E
+分子 #21: Histone H2B type 1-J
+分子 #14: DNA (198-MER)
+分子 #17: DNA (198-MER)
+分子 #16: RNA (5'-R(P*GP*UP*UP*UP*UP*CP*GP*UP*UP*GP*UP*UP*UP*UP*UP*U)-3')
+分子 #22: ZINC ION
+分子 #23: MAGNESIUM ION
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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![]() | 単粒子再構成法 |
試料の集合状態 | particle |
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試料調製
緩衝液 | pH: 7.5 |
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凍結 | 凍結剤: ETHANE |
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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: 57.6 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: ![]() |
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 |