登録情報 データベース : EMDB / ID : EMD-34849 ダウンロードとリンクタイトル Cryo-EM structure of E. coli RNAP sigma32 complex マップデータ 詳細 試料複合体 : Cryo-EM structure of E. coli RNAP sigma32 complexタンパク質・ペプチド : DNA-directed RNA polymerase subunit alphaタンパク質・ペプチド : DNA-directed RNA polymerase subunit betaタンパク質・ペプチド : RNA polymerase sigma factor RpoHタンパク質・ペプチド : DNA-directed RNA polymerase subunit beta'DNA : DNA (54-MER)DNA : DNA (54-MER) 残り2件を表示 表示を減らすリガンド : ZINC IONリガンド : MAGNESIUM ION 詳細 キーワード transcription / RNA polymerase / sigma factor / heat shock response / TRANSCRIPTION-DNA complex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
site-specific recombinase activity / invertasome / DNA-binding transcription activator activity / submerged biofilm formation / cellular response to cell envelope stress / regulation of DNA-templated transcription initiation / sigma factor activity / bacterial-type flagellum assembly / bacterial-type RNA polymerase core enzyme binding / cytosolic DNA-directed RNA polymerase complex ... site-specific recombinase activity / invertasome / DNA-binding transcription activator activity / submerged biofilm formation / cellular response to cell envelope stress / regulation of DNA-templated transcription initiation / sigma factor activity / bacterial-type flagellum assembly / bacterial-type RNA polymerase core enzyme binding / cytosolic DNA-directed RNA polymerase complex / bacterial-type flagellum-dependent cell motility / nitrate assimilation / core promoter sequence-specific DNA binding / transcription elongation factor complex / regulation of DNA-templated transcription elongation / transcription antitermination / DNA-templated transcription initiation / cell motility / ribonucleoside binding / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / regulation of gene expression / response to heat / DNA recombination / intracellular iron ion homeostasis / protein dimerization activity / response to antibiotic / DNA-templated transcription / regulation of DNA-templated transcription / magnesium ion binding / DNA binding / zinc ion binding / membrane / plasma membrane / cytosol / cytoplasm 類似検索 - 分子機能 RNA polymerase sigma factor RpoH, proteobacteria / : / Sigma-70 factors family signature 1. / Sigma-70 factors family signature 2. / RNA polymerase sigma-70 / RNA polymerase sigma-70 region 4 / Sigma-70, region 4 / RNA polymerase sigma-70 region 2 / RNA polymerase sigma-70 like domain / Sigma-70 region 2 ... RNA polymerase sigma factor RpoH, proteobacteria / : / Sigma-70 factors family signature 1. / Sigma-70 factors family signature 2. / RNA polymerase sigma-70 / RNA polymerase sigma-70 region 4 / Sigma-70, region 4 / RNA polymerase sigma-70 region 2 / RNA polymerase sigma-70 like domain / Sigma-70 region 2 / RNA polymerase sigma factor, region 2 / RNA polymerase sigma factor, region 3/4-like / 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 / DNA-directed RNA polymerase, subunit beta-prime / RNA polymerase Rpb2, domain 2 superfamily / RNA polymerase Rpb1, domain 3 superfamily / 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 / RNA polymerase Rpb1, clamp domain superfamily / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 1 / RNA polymerase, beta subunit, protrusion / RNA polymerase beta subunit / RNA polymerase Rpb1, domain 1 / RNA polymerase, alpha subunit / RNA polymerase Rpb1, domain 5 / RNA polymerase Rpb1, domain 4 / DNA-directed RNA polymerase, insert domain superfamily / RNA polymerase Rpb1, domain 2 / RNA polymerase Rpb1, domain 5 / RNA polymerase Rpb1, domain 4 / RNA polymerase Rpb2, domain 2 / RNA polymerase Rpb2, domain 2 / RNA polymerase, RBP11-like subunit / RNA polymerase, N-terminal / RNA polymerase Rpb1, funnel domain superfamily / RNA polymerase I subunit A N-terminus / 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 beta' / DNA-directed RNA polymerase subunit beta / RNA polymerase sigma factor RpoH 類似検索 - 構成要素生物種 Escherichia coli K-12 (大腸菌) / Escherichia coli (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 : 2.49 Å 詳細 データ登録者Wu S / Ma LX 資金援助 1件 詳細 詳細を隠すOrganization Grant number 国 Not funded
引用ジャーナル : Biomolecules / 年 : 2023タイトル : Structural Insight into the Mechanism of σ32-Mediated Transcription Initiation of Bacterial RNA Polymerase.著者 : Qiang Lu / Taiyu Chen / Jiening Wang / Feng Wang / Wenlong Ye / Lixin Ma / Shan Wu / 要旨 : Bacterial RNA polymerases (RNAP) form distinct holoenzymes with different σ factors to initiate diverse gene expression programs. In this study, we report a cryo-EM structure at 2.49 Å of RNA ... Bacterial RNA polymerases (RNAP) form distinct holoenzymes with different σ factors to initiate diverse gene expression programs. In this study, we report a cryo-EM structure at 2.49 Å of RNA polymerase transcription complex containing a temperature-sensitive bacterial σ factor, σ (σ-RPo). The structure of σ-RPo reveals key interactions essential for the assembly of σ-RNAP holoenzyme and for promoter recognition and unwinding by σ. Specifically, a weak interaction between σ and -35/-10 spacer is mediated by T128 and K130 in σ. A histidine in σ, rather than a tryptophan in σ, acts as a wedge to separate the base pair at the upstream junction of the transcription bubble, highlighting the differential promoter-melting capability of different residue combinations. Structure superimposition revealed relatively different orientations between βFTH and σ from other σ-engaged RNAPs and biochemical data suggest that a biased σ-βFTH configuration may be adopted to modulate binding affinity to promoter so as to orchestrate the recognition and regulation of different promoters. Collectively, these unique structural features advance our understanding of the mechanism of transcription initiation mediated by different σ factors. 履歴 登録 2022年11月25日 - ヘッダ(付随情報) 公開 2023年5月31日 - マップ公開 2023年5月31日 - 更新 2024年7月3日 - 現状 2024年7月3日 処理サイト : PDBj / 状態 : 公開
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