登録情報 データベース : EMDB / ID : EMD-35041 ダウンロードとリンクタイトル Cryo-EM structure of the J-K-St region of EMCV IRES in complex with eIF4G-HEAT1 and eIF4A マップデータPost-process map 詳細 試料複合体 : Ternary complex of the J-K-St region of EMCV IRES with eIF4A and eIF4G-HEAT1タンパク質・ペプチド : Eukaryotic initiation factor 4A-Iタンパク質・ペプチド : Eukaryotic translation initiation factor 4 gamma 1RNA : IRES RNA (J-K-St)リガンド : MAGNESIUM IONリガンド : water 詳細 キーワード Translation initiation factors / Translation / 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
positive regulation of eukaryotic translation initiation factor 4F complex assembly / positive regulation of mRNA cap binding / positive regulation of translation in response to endoplasmic reticulum stress / cap-dependent translational initiation / macromolecule biosynthetic process / Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S / regulation of cellular response to stress / eukaryotic initiation factor 4E binding / RNA cap binding / eukaryotic translation initiation factor 4F complex ... positive regulation of eukaryotic translation initiation factor 4F complex assembly / positive regulation of mRNA cap binding / positive regulation of translation in response to endoplasmic reticulum stress / cap-dependent translational initiation / macromolecule biosynthetic process / Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S / regulation of cellular response to stress / eukaryotic initiation factor 4E binding / RNA cap binding / eukaryotic translation initiation factor 4F complex / cytoplasmic translational initiation / translation factor activity, RNA binding / Z-decay: degradation of maternal mRNAs by zygotically expressed factors / Deadenylation of mRNA / miRNA-mediated gene silencing by inhibition of translation / M-decay: degradation of maternal mRNAs by maternally stored factors / positive regulation of protein localization to cell periphery / regulation of translational initiation / Ribosomal scanning and start codon recognition / Translation initiation complex formation / negative regulation of peptidyl-threonine phosphorylation / mTORC1-mediated signalling / cellular response to nutrient levels / regulation of presynapse assembly / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / behavioral fear response / positive regulation of G1/S transition of mitotic cell cycle / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / energy homeostasis / translation initiation factor binding / translational initiation / positive regulation of protein metabolic process / translation initiation factor activity / positive regulation of neuron differentiation / negative regulation of autophagy / helicase activity / AUF1 (hnRNP D0) binds and destabilizes mRNA / lung development / neuron differentiation / ISG15 antiviral mechanism / Regulation of expression of SLITs and ROBOs / cytoplasmic stress granule / double-stranded RNA binding / positive regulation of peptidyl-serine phosphorylation / positive regulation of cell growth / postsynapse / response to ethanol / molecular adaptor activity / RNA helicase activity / ribosome / RNA helicase / translation / mRNA binding / ATP hydrolysis activity / RNA binding / extracellular exosome / ATP binding / identical protein binding / membrane / nucleus / cytoplasm / cytosol 類似検索 - 分子機能 ATP-dependent RNA helicase eIF4A, DEAD-box helicase domain / Initiation factor 4G / eIF4-gamma/eIF5/eIF2-epsilon / Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5 / W2 domain / W2 domain profile. / Initiation factor eIF-4 gamma, MA3 / MA3 domain / MI domain profile. / Domain in DAP-5, eIF4G, MA-3 and other proteins. ... ATP-dependent RNA helicase eIF4A, DEAD-box helicase domain / Initiation factor 4G / eIF4-gamma/eIF5/eIF2-epsilon / Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5 / W2 domain / W2 domain profile. / Initiation factor eIF-4 gamma, MA3 / MA3 domain / MI domain profile. / Domain in DAP-5, eIF4G, MA-3 and other proteins. / MIF4G domain / Middle domain of eukaryotic initiation factor 4G (eIF4G) / MIF4G-like, type 3 / DEAD-box subfamily ATP-dependent helicases signature. / ATP-dependent RNA helicase DEAD-box, conserved site / RNA helicase, DEAD-box type, Q motif / DEAD-box RNA helicase Q motif profile. / DEAD/DEAH box helicase / DEAD/DEAH box helicase domain / Helicase conserved C-terminal domain / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / Armadillo-type fold / P-loop containing nucleoside triphosphate hydrolase 類似検索 - ドメイン・相同性 Eukaryotic initiation factor 4A-I / Eukaryotic translation initiation factor 4 gamma 1 類似検索 - 構成要素生物種 Homo sapiens (ヒト) / Encephalomyocarditis virus (脳心筋炎ウイルス)手法 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度 : 3.76 Å 詳細 データ登録者Suzuki H / Fujiyoshi Y / Imai S / Shimada I 資金援助 日本, 2件 詳細 詳細を隠すOrganization Grant number 国 Japan Agency for Medical Research and Development (AMED) 21ae0121028h0001 日本 Japan Society for the Promotion of Science (JSPS) 20H00451 日本
引用ジャーナル : Nat Commun / 年 : 2023タイトル : Dynamically regulated two-site interaction of viral RNA to capture host translation initiation factor.著者 : Shunsuke Imai / Hiroshi Suzuki / Yoshinori Fujiyoshi / Ichio Shimada / 要旨 : Many RNA viruses employ internal ribosome entry sites (IRESs) in their genomic RNA to commandeer the host's translational machinery for replication. The IRES from encephalomyocarditis virus (EMCV) ... Many RNA viruses employ internal ribosome entry sites (IRESs) in their genomic RNA to commandeer the host's translational machinery for replication. The IRES from encephalomyocarditis virus (EMCV) interacts with eukaryotic translation initiation factor 4 G (eIF4G), recruiting the ribosomal subunit for translation. Here, we analyze the three-dimensional structure of the complex composed of EMCV IRES, the HEAT1 domain fragment of eIF4G, and eIF4A, by cryo-electron microscopy. Two distinct eIF4G-interacting domains on the IRES are identified, and complex formation changes the angle therebetween. Further, we explore the dynamics of these domains by using solution NMR spectroscopy, revealing conformational equilibria in the microsecond to millisecond timescale. In the lowly-populated conformations, the base-pairing register of one domain is shifted with the structural transition of the three-way junction, as in the complex structure. Our study provides insights into the viral RNA's sophisticated strategy for optimal docking to hijack the host protein. 履歴 登録 2022年12月24日 - ヘッダ(付随情報) 公開 2023年8月2日 - マップ公開 2023年8月2日 - 更新 2023年9月13日 - 現状 2023年9月13日 処理サイト : PDBj / 状態 : 公開
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