+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-20077 | ||||||||||||
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タイトル | Subunit joining exposes nascent pre-40S rRNA for processing and quality control | ||||||||||||
マップデータ | |||||||||||||
試料 |
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キーワード | 80S-like complex / 60S / RIBOSOME | ||||||||||||
機能・相同性 | 機能・相同性情報 hexon binding / pre-mRNA 5'-splice site binding / cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / response to cycloheximide / SRP-dependent cotranslational protein targeting to membrane / GTP hydrolysis and joining of the 60S ribosomal subunit / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Formation of a pool of free 40S subunits / negative regulation of mRNA splicing, via spliceosome ...hexon binding / pre-mRNA 5'-splice site binding / cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / response to cycloheximide / SRP-dependent cotranslational protein targeting to membrane / GTP hydrolysis and joining of the 60S ribosomal subunit / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Formation of a pool of free 40S subunits / negative regulation of mRNA splicing, via spliceosome / preribosome, large subunit precursor / L13a-mediated translational silencing of Ceruloplasmin expression / translational elongation / ribosomal large subunit export from nucleus / 90S preribosome / regulation of translational fidelity / protein-RNA complex assembly / translational termination / maturation of LSU-rRNA / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit biogenesis / translational initiation / macroautophagy / maintenance of translational fidelity / modification-dependent protein catabolic process / protein tag activity / rRNA processing / ribosome biogenesis / viral capsid / 5S rRNA binding / large ribosomal subunit rRNA binding / ribosomal large subunit assembly / cytoplasmic translation / cytosolic large ribosomal subunit / negative regulation of translation / rRNA binding / ribosome / protein ubiquitination / structural constituent of ribosome / translation / response to antibiotic / mRNA binding / ubiquitin protein ligase binding / host cell nucleus / nucleolus / RNA binding / nucleus / metal ion binding / cytosol / cytoplasm 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: 3.8 Å | ||||||||||||
データ登録者 | Rai J / Parker MD | ||||||||||||
資金援助 | 米国, 3件
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引用 | ジャーナル: RNA / 年: 2021 タイトル: An open interface in the pre-80S ribosome coordinated by ribosome assembly factors Tsr1 and Dim1 enables temporal regulation of Fap7. 著者: Jay Rai / Melissa D Parker / Haina Huang / Stefan Choy / Homa Ghalei / Matthew C Johnson / Katrin Karbstein / M Elizabeth Stroupe / 要旨: During their maturation, nascent 40S subunits enter a translation-like quality control cycle, where they are joined by mature 60S subunits to form 80S-like ribosomes. While these assembly ...During their maturation, nascent 40S subunits enter a translation-like quality control cycle, where they are joined by mature 60S subunits to form 80S-like ribosomes. While these assembly intermediates are essential for maturation and quality control, how they form, and how their structure promotes quality control, remains unknown. To address these questions, we determined the structure of an 80S-like ribosome assembly intermediate to an overall resolution of 3.4 Å. The structure, validated by biochemical data, resolves a large body of previously paradoxical data and illustrates how assembly and translation factors cooperate to promote the formation of an interface that lacks many mature subunit contacts but is stabilized by the universally conserved methyltransferase Dim1. We also show how Tsr1 enables this interface by blocking the canonical binding of eIF5B to 40S subunits, while maintaining its binding to 60S. The structure also shows how this interface leads to unfolding of the platform, which allows for temporal regulation of the ATPase Fap7, thus linking 40S maturation to quality control during ribosome assembly. | ||||||||||||
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_20077.map.gz | 121.5 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-20077-v30.xml emd-20077.xml | 68.8 KB 68.8 KB | 表示 表示 | EMDBヘッダ |
画像 | emd_20077.png | 146.6 KB | ||
Filedesc metadata | emd-20077.cif.gz | 13.8 KB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-20077 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-20077 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_20077_validation.pdf.gz | 466.2 KB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_20077_full_validation.pdf.gz | 465.8 KB | 表示 | |
XML形式データ | emd_20077_validation.xml.gz | 7.1 KB | 表示 | |
CIF形式データ | emd_20077_validation.cif.gz | 8.1 KB | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-20077 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-20077 | 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_20077.map.gz / 形式: CCP4 / 大きさ: 216 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: 1.24 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
-試料の構成要素
+全体 : 60S subunit of 80S-like ribosome
+超分子 #1: 60S subunit of 80S-like ribosome
+分子 #1: 60S ribosomal protein L1-A
+分子 #2: 60S ribosomal protein L2-A
+分子 #3: 60S ribosomal protein L3
+分子 #4: 60S ribosomal protein L4-A
+分子 #5: 60S ribosomal protein L5
+分子 #6: 60S ribosomal protein L6-A
+分子 #7: 60S ribosomal protein L7-A
+分子 #8: 60S ribosomal protein L8-A
+分子 #9: 60S ribosomal protein L9-A
+分子 #10: 60S ribosomal protein L10
+分子 #11: 60S ribosomal protein L11-B
+分子 #12: 60S ribosomal protein L12-A
+分子 #13: 60S ribosomal protein L13-A
+分子 #14: 60S ribosomal protein L14-A
+分子 #15: 60S ribosomal protein L15-A
+分子 #16: 60S ribosomal protein L16-A
+分子 #17: 60S ribosomal protein L17-A
+分子 #18: 60S ribosomal protein L18-A
+分子 #19: 60S ribosomal protein L19-A
+分子 #20: 60S ribosomal protein L20-A
+分子 #21: 60S ribosomal protein L21-A
+分子 #22: 60S ribosomal protein L22-A
+分子 #23: 60S ribosomal protein L23-A
+分子 #24: 60S ribosomal protein L24-A
+分子 #25: 60S ribosomal protein L25
+分子 #26: 60S ribosomal protein L26-A
+分子 #27: 60S ribosomal protein L27-A
+分子 #28: 60S ribosomal protein L28
+分子 #29: 60S ribosomal protein L29
+分子 #30: 60S ribosomal protein L30
+分子 #31: 60S ribosomal protein L31-A
+分子 #32: 60S ribosomal protein L32
+分子 #33: 60S ribosomal protein L33-A
+分子 #34: 60S ribosomal protein L34-A
+分子 #35: 60S ribosomal protein L35-A
+分子 #36: 60S ribosomal protein L36-A
+分子 #37: 60S ribosomal protein L37-A
+分子 #38: 60S ribosomal protein L38
+分子 #39: 60S ribosomal protein L39
+分子 #40: Ubiquitin-60S ribosomal protein L40
+分子 #41: 60S ribosomal protein L42-A
+分子 #42: 60S ribosomal protein L43-A
+分子 #43: 60S acidic ribosomal protein P0,60S acidic ribosomal protein P0,A...
+分子 #47: P1
+分子 #48: P2
+分子 #44: 25S ribosomal RNA
+分子 #45: 5.8S ribosomal RNA
+分子 #46: 5S ribosomal RNA
-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: 6.8 |
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グリッド | 詳細: unspecified |
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: DIRECT ELECTRON DE-64 (8k x 8k) 検出モード: COUNTING / 平均電子線量: 25.0 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: EMDB MAP |
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最終 再構成 | 解像度のタイプ: BY AUTHOR / 解像度: 3.8 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 83558 |
初期 角度割当 | タイプ: NOT APPLICABLE |
最終 角度割当 | タイプ: MAXIMUM LIKELIHOOD |