登録情報 データベース : EMDB / ID : EMD-4886 構造の表示 ダウンロードとリンクタイトル Cryo-EM structure of E. coli RNA polymerase backtracked elongation complex in non-swiveled state マップデータ 詳細 試料複合体 : Cryo-EM structure of E. coli RNA polymerase backtracked elongation complex in non-swiveled state複合体 : RNA polymerase RNAポリメラーゼタンパク質・ペプチド : DNA-directed RNA polymerase subunit alpha ポリメラーゼタンパク質・ペプチド : DNA-directed RNA polymerase subunit beta ポリメラーゼタンパク質・ペプチド : DNA-directed RNA polymerase subunit beta' ポリメラーゼタンパク質・ペプチド : DNA-directed RNA polymerase subunit omega ポリメラーゼ複合体 : nucleic acids 核酸DNA : Non-template DNADNA : Template DNARNA : RNA リボ核酸リガンド : ZINC IONリガンド : MAGNESIUM ION 詳細 キーワード E. coli RNA polymerase / CTP / GreB / Elongation complex / TRANSCRIPTION (転写 (生物学))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
RNA polymerase complex / submerged biofilm formation / cellular response to cell envelope stress / cytosolic DNA-directed RNA polymerase complex / regulation of DNA-templated transcription initiation / bacterial-type flagellum assembly / bacterial-type flagellum-dependent cell motility / nitrate assimilation / transcription elongation factor complex / regulation of DNA-templated transcription elongation ... RNA polymerase complex / submerged biofilm formation / cellular response to cell envelope stress / cytosolic DNA-directed RNA polymerase complex / regulation of DNA-templated transcription initiation / bacterial-type flagellum assembly / bacterial-type flagellum-dependent cell motility / nitrate assimilation / transcription elongation factor complex / regulation of DNA-templated transcription elongation / transcription antitermination / DNA-templated transcription initiation / 運動性 / ribonucleoside binding / DNA-directed 5'-3' RNA polymerase activity / ポリメラーゼ / response to heat / protein-containing complex assembly / intracellular iron ion homeostasis / protein dimerization activity / response to antibiotic / magnesium ion binding / DNA binding / zinc ion binding / 生体膜 / 細胞質基質 / 細胞質 類似検索 - 分子機能 DNA-directed RNA polymerase, omega subunit / DNA-directed RNA polymerase, subunit beta-prime, bacterial type / DNA-directed RNA polymerase, beta subunit, external 1 domain superfamily / DNA-directed RNA polymerase, beta subunit, external 1 domain / RNA polymerase beta subunit external 1 domain / RNA polymerase, alpha subunit, C-terminal / Bacterial RNA polymerase, alpha chain C terminal domain / DNA-directed RNA polymerase, alpha subunit / DNA-directed RNA polymerase beta subunit, bacterial-type / RNA polymerase Rpb6 ... DNA-directed RNA polymerase, omega subunit / DNA-directed RNA polymerase, subunit beta-prime, bacterial type / DNA-directed RNA polymerase, beta subunit, external 1 domain superfamily / DNA-directed RNA polymerase, beta subunit, external 1 domain / RNA polymerase beta subunit external 1 domain / RNA polymerase, alpha subunit, C-terminal / Bacterial RNA polymerase, alpha chain C terminal domain / DNA-directed RNA polymerase, alpha subunit / DNA-directed RNA polymerase beta subunit, bacterial-type / RNA polymerase Rpb6 / RNA polymerase, subunit omega/Rpo6/RPB6 / RNA polymerase Rpb6 / RNA polymerase Rpb1, domain 3 superfamily / RNA polymerase Rpb1, clamp domain superfamily / RPB6/omega subunit-like superfamily / DNA-directed RNA polymerase, subunit beta-prime / RNA polymerase Rpb2, domain 2 superfamily / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 1 / RNA polymerase Rpb1, domain 1 / RNA polymerase, alpha subunit / RNA polymerase Rpb1, domain 4 / RNA polymerase Rpb1, domain 2 / RNA polymerase Rpb1, domain 4 / RNA polymerase, beta subunit, protrusion / RNA polymerase beta subunit / RNA polymerase, N-terminal / RNA polymerase Rpb1, funnel domain superfamily / RNA polymerase I subunit A N-terminus / RNA polymerase Rpb1, domain 5 / RNA polymerase Rpb1, domain 5 / DNA-directed RNA polymerase, insert domain / DNA-directed RNA polymerase, RpoA/D/Rpb3-type / RNA polymerase Rpb3/RpoA insert domain / RNA polymerase Rpb3/Rpb11 dimerisation domain / RNA polymerases D / DNA-directed RNA polymerase, insert domain superfamily / RNA polymerase, RBP11-like subunit / RNA polymerase Rpb2, domain 2 / RNA polymerase Rpb2, domain 2 / RNA polymerase, beta subunit, conserved site / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerase Rpb2, OB-fold / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerases beta chain signature. / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain / DNA-directed RNA polymerase, subunit 2 / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain superfamily / RNA polymerase Rpb2, domain 6 類似検索 - ドメイン・相同性 DNA-directed RNA polymerase subunit alpha / DNA-directed RNA polymerase subunit omega / DNA-directed RNA polymerase subunit beta' / DNA-directed RNA polymerase subunit beta 類似検索 - 構成要素生物種 Escherichia coli K-12 (大腸菌) / Escherichia coli (大腸菌) / Escherichia coli (strain K12) (大腸菌)手法 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度 : 3.7 Å 詳細 データ登録者Abdelkareem M / Saint-Andre C 資金援助 フランス, 1件 詳細 詳細を隠すOrganization Grant number 国 European Research Council 679734 フランス
引用ジャーナル : Mol Cell / 年 : 2019タイトル : Structural Basis of Transcription: RNA Polymerase Backtracking and Its Reactivation.著者 : Mo'men Abdelkareem / Charlotte Saint-André / Maria Takacs / Gabor Papai / Corinne Crucifix / Xieyang Guo / Julio Ortiz / Albert Weixlbaumer / 要旨 : Regulatory sequences or erroneous incorporations during DNA transcription cause RNA polymerase backtracking and inactivation in all kingdoms of life. Reactivation requires RNA transcript cleavage. ... Regulatory sequences or erroneous incorporations during DNA transcription cause RNA polymerase backtracking and inactivation in all kingdoms of life. Reactivation requires RNA transcript cleavage. Essential transcription factors (GreA and GreB, or TFIIS) accelerate this reaction. We report four cryo-EM reconstructions of Escherichia coli RNA polymerase representing the entire reaction pathway: (1) a backtracked complex; a backtracked complex with GreB (2) before and (3) after RNA cleavage; and (4) a reactivated, substrate-bound complex with GreB before RNA extension. Compared with eukaryotes, the backtracked RNA adopts a different conformation. RNA polymerase conformational changes cause distinct GreB states: a fully engaged GreB before cleavage; a disengaged GreB after cleavage; and a dislodged, loosely bound GreB removed from the active site to allow RNA extension. These reconstructions provide insight into the catalytic mechanism and dynamics of RNA cleavage and extension and suggest how GreB targets backtracked complexes without interfering with canonical transcription. 履歴 登録 2019年4月23日 - ヘッダ(付随情報) 公開 2019年7月3日 - マップ公開 2019年7月3日 - 更新 2024年5月22日 - 現状 2024年5月22日 処理サイト : PDBe / 状態 : 公開
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