登録情報 データベース : EMDB / ID : EMD-0128 構造の表示 ダウンロードとリンクタイトル Human nuclear RNA exosome EXO-10-MPP6 complex マップデータCryo-EM reconstruction of the human nuclear RNA exosome EXO-10-MPP6 complex 詳細 試料複合体 : Human nuclear RNA exosome EXO-14 complex複合体 : exosome complex複合体 : U44 ssRNA 詳細 キーワード nuclear exosome / RNA decay / cryoEM / hEXO-10 / hDIS3 / hMPP6 / RNA BINDING PROTEIN機能・相同性 機能・相同性情報分子機能 ドメイン・相同性 構成要素
DNA deamination / nucleolar exosome (RNase complex) / mRNA decay by 3' to 5' exoribonuclease / TRAMP-dependent tRNA surveillance pathway / CUT catabolic process / exosome (RNase complex) / nuclear polyadenylation-dependent rRNA catabolic process / U1 snRNA 3'-end processing / nuclear polyadenylation-dependent mRNA catabolic process / U5 snRNA 3'-end processing ... DNA deamination / nucleolar exosome (RNase complex) / mRNA decay by 3' to 5' exoribonuclease / TRAMP-dependent tRNA surveillance pathway / CUT catabolic process / exosome (RNase complex) / nuclear polyadenylation-dependent rRNA catabolic process / U1 snRNA 3'-end processing / nuclear polyadenylation-dependent mRNA catabolic process / U5 snRNA 3'-end processing / cytoplasmic exosome (RNase complex) / nuclear exosome (RNase complex) / poly(A)-dependent snoRNA 3'-end processing / U4 snRNA 3'-end processing / : / exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / : / Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / ATF4 activates genes in response to endoplasmic reticulum stress / Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA / histone mRNA catabolic process / nuclear mRNA surveillance / positive regulation of isotype switching / rRNA catabolic process / mRNA 3'-UTR AU-rich region binding / 7S RNA binding / isotype switching / 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リボヌクレアーゼ / RNA catabolic process / nuclear-transcribed mRNA catabolic process / KSRP (KHSRP) binds and destabilizes mRNA / nuclear chromosome / maturation of 5.8S rRNA / Major pathway of rRNA processing in the nucleolus and cytosol / RNA processing / guanyl-nucleotide exchange factor activity / euchromatin / fibrillar center / rRNA processing / chromosome / 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キソリボヌクレアーゼ / 3'-5'-RNA exonuclease activity / positive regulation of cell growth / endonuclease activity / defense response to virus / RNA polymerase II-specific DNA-binding transcription factor binding / immune response / intracellular membrane-bounded organelle / nucleolus / positive regulation of transcription by RNA polymerase II / DNA binding / RNA binding / extracellular exosome / nucleoplasm / identical protein binding / membrane / nucleus / cytoplasm / cytosol 類似検索 - 分子機能 Exosome complex component Rrp43 / : / Mammalian exosome complex component RRP40, N-terminal / M-phase phosphoprotein 6 / M-phase phosphoprotein 6 / Exosome complex exonuclease RRP44, S1 domain / S1 domain / RRP4, S1 domain / Exosome complex component RRP45 / Rrp40, S1 domain ... Exosome complex component Rrp43 / : / Mammalian exosome complex component RRP40, N-terminal / M-phase phosphoprotein 6 / M-phase phosphoprotein 6 / Exosome complex exonuclease RRP44, S1 domain / S1 domain / RRP4, S1 domain / Exosome complex component RRP45 / Rrp40, S1 domain / : / Exosome complex component RRP40, S1 domain / Exosome complex component CSL4, C-terminal / Exosome complex component, N-terminal domain / Exosome complex component Csl4 / Exosome component EXOSC1/CSL4 / PIN domain / Exosome complex exonuclease RRP4 N-terminal region / : / Rrp44-like cold shock domain / Rrp44-like cold shock domain / Exosome complex RNA-binding protein 1/RRP40/RRP4 / KH domain / Dis3-like cold-shock domain 2 / Dis3-like cold-shock domain 2 (CSD2) / Ribonuclease II/R, conserved site / Ribonuclease II family signature. / Ribonuclease II/R / RNB domain / RNB / Exoribonuclease, phosphorolytic domain 2 / 3' exoribonuclease family, domain 2 / Exoribonuclease, phosphorolytic domain 1 / PNPase/RNase PH domain superfamily / Exoribonuclease, PH domain 2 superfamily / 3' exoribonuclease family, domain 1 / Large family of predicted nucleotide-binding domains / PIN domain / K Homology domain, type 1 / K Homology domain, type 1 superfamily / PIN-like domain superfamily / Ribosomal protein S1-like RNA-binding domain / S1 domain / Ribosomal protein S5 domain 2-type fold / Nucleic acid-binding, OB-fold 類似検索 - ドメイン・相同性 Exosome complex component RRP45 / Exosome complex component RRP4 / Exosome complex component RRP42 / Exosome complex component MTR3 / Exosome complex component RRP43 / M-phase phosphoprotein 6 / Exosome complex component RRP41 / Exosome complex component RRP46 / Exosome complex component RRP40 / Exosome complex exonuclease RRP44 / Exosome complex component CSL4 類似検索 - 構成要素生物種 Homo sapiens (ヒト) / synthetic construct (人工物) 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 詳細 データ登録者Gerlach P / Schuller JM / Falk S / Basquin J / Conti E 資金援助 5件 詳細 詳細を隠すOrganization Grant number 国 European Molecular Biology Organization ALTF 1008-2015 European Commission ERC-2016-ADG 740329 EXORICO German Research Foundation SFB646, SFB1035, GRK1721 Louis-Jeantet Foundation Max Planck Society
引用ジャーナル : Elife / 年 : 2018タイトル : Distinct and evolutionary conserved structural features of the human nuclear exosome complex.著者 : Piotr Gerlach / Jan M Schuller / Fabien Bonneau / Jérôme Basquin / Peter Reichelt / Sebastian Falk / Elena Conti / 要旨 : The nuclear RNA exosome complex mediates the processing of structured RNAs and the decay of aberrant non-coding RNAs, an important function particularly in human cells. Most mechanistic studies to ... The nuclear RNA exosome complex mediates the processing of structured RNAs and the decay of aberrant non-coding RNAs, an important function particularly in human cells. Most mechanistic studies to date have focused on the yeast system. Here, we reconstituted and studied the properties of a recombinant 14-subunit human nuclear exosome complex. In biochemical assays, the human exosome embeds a longer RNA channel than its yeast counterpart. The 3.8 Å resolution cryo-EM structure of the core complex bound to a single-stranded RNA reveals that the RNA channel path is formed by two distinct features of the hDIS3 exoribonuclease: an open conformation and a domain organization more similar to bacterial RNase II than to yeast Rrp44. The cryo-EM structure of the holo-complex shows how obligate nuclear cofactors position the hMTR4 helicase at the entrance of the core complex, suggesting a striking structural conservation from lower to higher eukaryotes. 履歴 登録 2018年7月13日 - ヘッダ(付随情報) 公開 2018年8月1日 - マップ公開 2018年8月15日 - 更新 2024年5月15日 - 現状 2024年5月15日 処理サイト : PDBe / 状態 : 公開
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