+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-30779 | |||||||||
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タイトル | Structure of Human RNA Polymerase III elongation complex | |||||||||
マップデータ | Insert Funnel conformation (RPC10 inserts in Funnel) | |||||||||
試料 |
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キーワード | RNA Polymerase III / transcription | |||||||||
機能・相同性 | 機能・相同性情報 snRNA transcription by RNA polymerase III / RNA Polymerase III Chain Elongation / RNA Polymerase III Transcription Termination / calcitonin gene-related peptide receptor activity / DNA/RNA hybrid binding / regulation of transcription by RNA polymerase I / regulation of transcription by RNA polymerase III / RPAP3/R2TP/prefoldin-like complex / DNA polymerase III complex / Cytosolic sensors of pathogen-associated DNA ...snRNA transcription by RNA polymerase III / RNA Polymerase III Chain Elongation / RNA Polymerase III Transcription Termination / calcitonin gene-related peptide receptor activity / DNA/RNA hybrid binding / regulation of transcription by RNA polymerase I / regulation of transcription by RNA polymerase III / RPAP3/R2TP/prefoldin-like complex / DNA polymerase III complex / Cytosolic sensors of pathogen-associated DNA / RNA Polymerase III Transcription Initiation From Type 1 Promoter / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Polymerase III Transcription Initiation From Type 3 Promoter / RNA Polymerase III Abortive And Retractive Initiation / positive regulation of innate immune response / Abortive elongation of HIV-1 transcript in the absence of Tat / nucleobase-containing compound metabolic process / RNA Polymerase I Transcription Termination / FGFR2 alternative splicing / MicroRNA (miRNA) biogenesis / Signaling by FGFR2 IIIa TM / Viral Messenger RNA Synthesis / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / mRNA Capping / PIWI-interacting RNA (piRNA) biogenesis / termination of RNA polymerase III transcription / HIV Transcription Initiation / RNA Polymerase II HIV Promoter Escape / Transcription of the HIV genome / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Initiation And Promoter Clearance / RNA polymerase III activity / transcription initiation at RNA polymerase III promoter / mRNA Splicing - Minor Pathway / RNA Polymerase I Transcription Initiation / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / transcription by RNA polymerase I / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / Processing of Capped Intron-Containing Pre-mRNA / transcription by RNA polymerase III / RNA polymerase II transcribes snRNA genes / neuropeptide signaling pathway / Tat-mediated elongation of the HIV-1 transcript / transcription elongation by RNA polymerase I / Formation of HIV-1 elongation complex containing HIV-1 Tat / tRNA transcription by RNA polymerase III / RNA polymerase I activity / RNA polymerase I complex / RNA polymerase III complex / Formation of HIV elongation complex in the absence of HIV Tat / RNA polymerase II, core complex / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / RNA Polymerase II Pre-transcription Events / Inhibition of DNA recombination at telomere / positive regulation of interferon-beta production / mRNA Splicing - Major Pathway / acrosomal vesicle / protein-DNA complex / TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase I Promoter Escape / Transcriptional regulation by small RNAs / NoRC negatively regulates rRNA expression / B-WICH complex positively regulates rRNA expression / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / Formation of TC-NER Pre-Incision Complex / ribonucleoside binding / fibrillar center / DNA-directed 5'-3' RNA polymerase activity / Activation of anterior HOX genes in hindbrain development during early embryogenesis / DNA-directed RNA polymerase / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / single-stranded DNA binding / 4 iron, 4 sulfur cluster binding / double-stranded DNA binding / defense response to virus / Estrogen-dependent gene expression / transcription by RNA polymerase II / cell population proliferation / nucleic acid binding / nuclear body / protein dimerization activity / protein stabilization / intracellular membrane-bounded organelle / innate immune response / nucleotide binding / centrosome / DNA-templated transcription / chromatin binding / magnesium ion binding / DNA binding / zinc ion binding 類似検索 - 分子機能 | |||||||||
生物種 | Homo sapiens (ヒト) | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 3.5 Å | |||||||||
データ登録者 | Li L / Yu Z | |||||||||
引用 | ジャーナル: Cell Res / 年: 2021 タイトル: Structure of human RNA polymerase III elongation complex. 著者: Liang Li / Zishuo Yu / Dan Zhao / Yulei Ren / Haifeng Hou / Yanhui Xu / 要旨: RNA polymerase III (Pol III) transcribes essential structured small RNAs, such as tRNAs, 5S rRNA and U6 snRNA. The transcriptional activity of Pol III is tightly controlled and its dysregulation is ...RNA polymerase III (Pol III) transcribes essential structured small RNAs, such as tRNAs, 5S rRNA and U6 snRNA. The transcriptional activity of Pol III is tightly controlled and its dysregulation is associated with human diseases, such as cancer. Human Pol III has two isoforms with difference only in one of its subunits RPC7 (α and β). Despite structural studies of yeast Pol III, structure of human Pol III remains unsolved. Here, we determined the structures of 17-subunit human Pol IIIα complex in the backtracked and post-translocation states, respectively. Human Pol III contains a generally conserved catalytic core, similar to that of yeast counterpart, and structurally unique RPC3-RPC6-RPC7 heterotrimer and RPC10. The N-ribbon of TFIIS-like RPC10 docks on the RPC4-RPC5 heterodimer and the C-ribbon inserts into the funnel of Pol III in the backtracked state but is more flexible in the post-translocation state. RPC7 threads through the heterotrimer and bridges the stalk and Pol III core module. The winged helix 1 domain of RPC6 and the N-terminal region of RPC7α stabilize each other and may prevent Maf1-mediated repression of Pol III activity. The C-terminal FeS cluster of RPC6 coordinates a network of interactions that mediate core-heterotrimer contacts and stabilize Pol III. Our structural analysis sheds new light on the molecular mechanism of human Pol IIIα-specific transcriptional regulation and provides explanations for upregulated Pol III activity in RPC7α-dominant cancer cells. | |||||||||
履歴 |
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-構造の表示
ムービー |
ムービービューア |
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構造ビューア | EMマップ: SurfViewMolmilJmol/JSmol |
添付画像 |
-ダウンロードとリンク
-EMDBアーカイブ
マップデータ | emd_30779.map.gz | 62.5 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-30779-v30.xml emd-30779.xml | 42.9 KB 42.9 KB | 表示 表示 | EMDBヘッダ |
画像 | emd_30779.png | 72.7 KB | ||
Filedesc metadata | emd-30779.cif.gz | 10.5 KB | ||
その他 | emd_30779_additional_1.map.gz emd_30779_additional_2.map.gz | 97.9 MB 118.1 MB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-30779 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-30779 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_30779_validation.pdf.gz | 551.6 KB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_30779_full_validation.pdf.gz | 551.2 KB | 表示 | |
XML形式データ | emd_30779_validation.xml.gz | 6.4 KB | 表示 | |
CIF形式データ | emd_30779_validation.cif.gz | 7.4 KB | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-30779 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-30779 | 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_30779.map.gz / 形式: CCP4 / 大きさ: 125 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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注釈 | Insert Funnel conformation (RPC10 inserts in Funnel) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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:
CCP4マップ ヘッダ情報:
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-添付データ
-追加マップ: Masked RPC6 WH domain
ファイル | emd_30779_additional_1.map | ||||||||||||
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注釈 | Masked RPC6 WH domain | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-追加マップ: the best resolved map of hPol3 in backtracked state
ファイル | emd_30779_additional_2.map | ||||||||||||
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注釈 | the best resolved map of hPol3 in backtracked state | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-試料の構成要素
+全体 : Structure of Human RNA Polymerase III elongation complex
+超分子 #1: Structure of Human RNA Polymerase III elongation complex
+超分子 #2: RNA Polymerase III elongation
+超分子 #3: DNA
+超分子 #4: RNA
+分子 #1: DNA-directed RNA polymerase III subunit RPC1
+分子 #2: DNA-directed RNA polymerase III subunit RPC2
+分子 #3: DNA-directed RNA polymerases I and III subunit RPAC1
+分子 #4: DNA-directed RNA polymerase III subunit RPC8
+分子 #5: DNA-directed RNA polymerase III subunit RPC10
+分子 #6: DNA-directed RNA polymerases I and III subunit RPAC2
+分子 #7: DNA-directed RNA polymerases I, II, and III subunit RPABC4
+分子 #8: DNA-directed RNA polymerase III subunit RPC6
+分子 #9: DNA-directed RNA polymerases I, II, and III subunit RPABC1
+分子 #10: DNA-directed RNA polymerases I, II, and III subunit RPABC2
+分子 #11: DNA-directed RNA polymerases I, II, and III subunit RPABC3
+分子 #12: DNA-directed RNA polymerases I, II, and III subunit RPABC5
+分子 #13: DNA-directed RNA polymerase III subunit RPC3
+分子 #14: DNA-directed RNA polymerase III subunit RPC7
+分子 #15: DNA-directed RNA polymerase III subunit RPC9
+分子 #16: DNA-directed RNA polymerase III subunit RPC5
+分子 #17: DNA-directed RNA polymerase III subunit RPC4
+分子 #18: DNA (5'-D(P*TP*CP*GP*TP*CP*TP*GP*AP*TP*CP*TP*CP*GP*GP*AP*A)-3')
+分子 #19: DNA (5'-D(P*TP*TP*CP*CP*GP*AP*GP*AP*TP*CP*AP*GP*AP*CP*GP*AP*GP*AP...
+分子 #20: RNA (5'-R(P*CP*CP*CP*GP*AP*U)-3')
+分子 #21: MAGNESIUM ION
+分子 #22: ZINC ION
+分子 #23: IRON/SULFUR CLUSTER
-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: 8 |
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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 (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 |
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: OTHER |
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最終 再構成 | 解像度のタイプ: BY AUTHOR / 解像度: 3.5 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 98293 |
初期 角度割当 | タイプ: OTHER |
最終 角度割当 | タイプ: MAXIMUM LIKELIHOOD |