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基本情報
登録情報 | ![]() | ||||||||||||||||||
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タイトル | human 40S ribosome bound by a SKI238-exosome complex | ||||||||||||||||||
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![]() | RNA-binding / RNA-degradation / cytoplasm / helicase / RIBOSOME | ||||||||||||||||||
機能・相同性 | ![]() DNA deamination / nucleolar exosome (RNase complex) / exoribonuclease II activity / exoribonuclease II / Dom34-Hbs1 complex / nuclear-transcribed mRNA catabolic process, no-go decay / U1 snRNA 3'-end processing / U5 snRNA 3'-end processing / TRAMP-dependent tRNA surveillance pathway / Ski complex ...DNA deamination / nucleolar exosome (RNase complex) / exoribonuclease II activity / exoribonuclease II / Dom34-Hbs1 complex / nuclear-transcribed mRNA catabolic process, no-go decay / U1 snRNA 3'-end processing / U5 snRNA 3'-end processing / TRAMP-dependent tRNA surveillance pathway / Ski complex / exosome (RNase complex) / CUT catabolic process / U4 snRNA 3'-end processing / cytoplasmic exosome (RNase complex) / mRNA decay by 3' to 5' exoribonuclease / nuclear polyadenylation-dependent rRNA catabolic process / poly(A)-dependent snoRNA 3'-end processing / Cdc73/Paf1 complex / nuclear exosome (RNase complex) / nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay / exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / negative regulation of myeloid cell differentiation / Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / ATF4 activates genes in response to endoplasmic reticulum stress / histone mRNA catabolic process / Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA / positive regulation of isotype switching / 3'-5' RNA helicase activity / nuclear mRNA surveillance / rRNA catabolic process / 7S RNA binding / mRNA 3'-UTR AU-rich region binding / isotype switching / negative regulation of endoplasmic reticulum unfolded protein response / oxidized pyrimidine DNA binding / response to TNF agonist / positive regulation of base-excision repair / positive regulation of respiratory burst involved in inflammatory response / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / positive regulation of gastrulation / nucleolus organization / regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway / protein tyrosine kinase inhibitor activity / IRE1-RACK1-PP2A complex / positive regulation of endodeoxyribonuclease activity / positive regulation of Golgi to plasma membrane protein transport / translation at postsynapse / TNFR1-mediated ceramide production / ribosome disassembly / RNA catabolic process / negative regulation of DNA repair / negative regulation of RNA splicing / mammalian oogenesis stage / supercoiled DNA binding / activation-induced cell death of T cells / neural crest cell differentiation / NF-kappaB complex / oxidized purine DNA binding / negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide / cysteine-type endopeptidase activator activity involved in apoptotic process / negative regulation of peptidyl-serine phosphorylation / ubiquitin-like protein conjugating enzyme binding / regulation of establishment of cell polarity / translation at presynapse / positive regulation of ubiquitin-protein transferase activity / rRNA modification in the nucleus and cytosol / negative regulation of phagocytosis / Formation of the ternary complex, and subsequently, the 43S complex / erythrocyte homeostasis / cytoplasmic side of rough endoplasmic reticulum membrane / KSRP (KHSRP) binds and destabilizes mRNA / laminin receptor activity / protein kinase A binding / maturation of 5.8S rRNA / negative regulation of ubiquitin protein ligase activity / pigmentation / nuclear chromosome / Ribosomal scanning and start codon recognition / ion channel inhibitor activity / Translation initiation complex formation / positive regulation of mitochondrial depolarization / positive regulation of T cell receptor signaling pathway / mRNA catabolic process / positive regulation of activated T cell proliferation / fibroblast growth factor binding / negative regulation of Wnt signaling pathway / Association of TriC/CCT with target proteins during biosynthesis / monocyte chemotaxis / negative regulation of translational frameshifting / Protein hydroxylation / BH3 domain binding / TOR signaling / SARS-CoV-1 modulates host translation machinery / regulation of cell division / mTORC1-mediated signalling / T cell proliferation involved in immune response / Peptide chain elongation / iron-sulfur cluster binding / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / nuclear-transcribed mRNA catabolic process 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: 3.4 Å | ||||||||||||||||||
![]() | Koegel A / Keidel A / Loukeri MJ / Kuhn CC / Langer LM / Schaefer IB / Conti E | ||||||||||||||||||
資金援助 | ![]() ![]()
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![]() | ![]() タイトル: Structural basis of mRNA decay by the human exosome-ribosome supercomplex. 著者: Alexander Kögel / Achim Keidel / Matina-Jasemi Loukeri / Christopher C Kuhn / Lukas M Langer / Ingmar B Schäfer / Elena Conti / ![]() 要旨: The interplay between translation and mRNA decay is widespread in human cells. In quality-control pathways, exonucleolytic degradation of mRNA associated with translating ribosomes is mediated ...The interplay between translation and mRNA decay is widespread in human cells. In quality-control pathways, exonucleolytic degradation of mRNA associated with translating ribosomes is mediated largely by the cytoplasmic exosome, which includes the exoribonuclease complex EXO10 and the helicase complex SKI238 (refs. ). The helicase can extract mRNA from the ribosome and is expected to transfer it to the exoribonuclease core through a bridging factor, HBS1L3 (also known as SKI7), but the mechanisms of this molecular handover remain unclear. Here we reveal how human EXO10 is recruited by HBS1L3 (SKI7) to an active ribosome-bound SKI238 complex. We show that rather than a sequential handover, a direct physical coupling mechanism takes place, which culminates in the formation of a cytoplasmic exosome-ribosome supercomplex. Capturing the structure during active decay reveals a continuous path in which an RNA substrate threads from the 80S ribosome through the SKI2 helicase into the exoribonuclease active site of the cytoplasmic exosome complex. The SKI3 subunit of the complex directly binds to HBS1L3 (SKI7) and also engages a surface of the 40S subunit, establishing a recognition platform in collided disomes. Exosome and ribosome thus work together as a single structural and functional unit in co-translational mRNA decay, coordinating their activities in a transient supercomplex. | ||||||||||||||||||
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構造の表示
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ダウンロードとリンク
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マップデータ | ![]() | 71.4 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 74.7 KB 74.7 KB | 表示 表示 | ![]() |
FSC (解像度算出) | ![]() | 29.4 KB | 表示 | ![]() |
画像 | ![]() | 35.4 KB | ||
マスクデータ | ![]() | 2.1 GB | ![]() | |
Filedesc metadata | ![]() | 17.3 KB | ||
その他 | ![]() ![]() ![]() | 66.4 MB 1.5 GB 1.5 GB | ||
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-検証レポート
文書・要旨 | ![]() | 750.4 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 750 KB | 表示 | |
XML形式データ | ![]() | 37.5 KB | 表示 | |
CIF形式データ | ![]() | 51.1 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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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: 0.8512 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
ファイル | ![]() | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
-追加マップ: composite map human 40S ribosome bound to the...
ファイル | emd_51134_additional_1.map | ||||||||||||
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注釈 | composite map human 40S ribosome bound to the SKI238 complex and the exosome | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: #2
ファイル | emd_51134_half_map_1.map | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: #1
ファイル | emd_51134_half_map_2.map | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
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試料の構成要素
+全体 : human 40S ribosome bound by a SKI238-exosome complex
+超分子 #1: human 40S ribosome bound by a SKI238-exosome complex
+分子 #1: Superkiller complex protein 3
+分子 #2: WD repeat-containing protein 61
+分子 #3: Exosome complex component RRP42
+分子 #4: Exosome complex component CSL4
+分子 #5: Exosome complex component RRP45
+分子 #6: Exosome complex component RRP43
+分子 #7: Exosome complex component RRP41
+分子 #8: Exosome complex component RRP46
+分子 #9: Helicase SKI2W
+分子 #10: Isoform 2 of HBS1-like protein
+分子 #11: Exosome complex component MTR3
+分子 #12: Exosome complex component RRP40
+分子 #13: Exosome complex component RRP4
+分子 #15: 60S ribosomal protein L41
+分子 #16: DIS3-like exonuclease 1
+分子 #18: 40S ribosomal protein SA
+分子 #19: 40S ribosomal protein S3a
+分子 #20: 40S ribosomal protein S2
+分子 #21: 40S ribosomal protein S3
+分子 #22: 40S ribosomal protein S4, X isoform
+分子 #23: 40S ribosomal protein S5
+分子 #24: 40S ribosomal protein S6
+分子 #25: 40S ribosomal protein S7
+分子 #26: 40S ribosomal protein S8
+分子 #27: 40S ribosomal protein S9
+分子 #28: 40S ribosomal protein S10
+分子 #29: 40S ribosomal protein S11
+分子 #30: 40S ribosomal protein S12
+分子 #31: 40S ribosomal protein S13
+分子 #32: 40S ribosomal protein S14
+分子 #33: 40S ribosomal protein S15
+分子 #34: 40S ribosomal protein S16
+分子 #35: 40S ribosomal protein S17
+分子 #36: 40S ribosomal protein S18
+分子 #37: 40S ribosomal protein S19
+分子 #38: 40S ribosomal protein S20
+分子 #39: 40S ribosomal protein S21
+分子 #40: 40S ribosomal protein S15a
+分子 #41: 40S ribosomal protein S23
+分子 #42: 40S ribosomal protein S24
+分子 #43: 40S ribosomal protein S25
+分子 #44: 40S ribosomal protein S26
+分子 #45: 40S ribosomal protein S27
+分子 #46: 40S ribosomal protein S28
+分子 #47: 40S ribosomal protein S29
+分子 #48: 40S ribosomal protein S30
+分子 #49: Ubiquitin
+分子 #50: Receptor of activated protein C kinase 1
+分子 #14: CrPV-IRES RNA
+分子 #17: 18S 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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![]() | 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: 7.4 |
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グリッド | モデル: Quantifoil R2/1 / メッシュ: 200 / 支持フィルム - 材質: CARBON / 支持フィルム - トポロジー: CONTINUOUS / 前処理 - タイプ: GLOW DISCHARGE |
凍結 | 凍結剤: ETHANE-PROPANE |
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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: 64.2 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): 2.4 µm / 最小 デフォーカス(公称値): 0.6 µm |
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |