登録情報 データベース : EMDB / ID : EMD-11104 構造の表示 ダウンロードとリンクタイトル Bacillus subtilis RNA polymerase HelD complex 1 マップデータ 詳細 試料複合体 : Recycling complex of Bacillus subitilis RNAP with HelD 詳細機能・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 helicase complex / nucleoid / recombinational repair / 3'-5' DNA helicase activity / DNA-directed RNA polymerase complex / DNA helicase activity / ribonucleoside binding / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / DNA helicase ... DNA helicase complex / nucleoid / recombinational repair / 3'-5' DNA helicase activity / DNA-directed RNA polymerase complex / DNA helicase activity / ribonucleoside binding / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / DNA helicase / protein dimerization activity / hydrolase activity / response to antibiotic / DNA-templated transcription / regulation of DNA-templated transcription / magnesium ion binding / ATP hydrolysis activity / DNA binding / zinc ion binding / ATP binding / cytoplasm / cytosol 類似検索 - 分子機能 : / RNA polymerase epsilon subunit / RNA polymerase epsilon subunit / DNA-directed RNA polymerase subunit delta / DNA-directed RNA polymerase subunit delta, N-terminal domain superfamily / ASXL, HARE-HTH domain / HB1, ASXL, restriction endonuclease HTH domain / HARE-type HTH domain profile. / UvrD-like helicase C-terminal domain / UvrD-like helicase C-terminal domain ... : / RNA polymerase epsilon subunit / RNA polymerase epsilon subunit / DNA-directed RNA polymerase subunit delta / DNA-directed RNA polymerase subunit delta, N-terminal domain superfamily / ASXL, HARE-HTH domain / HB1, ASXL, restriction endonuclease HTH domain / HARE-type HTH domain profile. / UvrD-like helicase C-terminal domain / UvrD-like helicase C-terminal domain / UvrD/REP helicase N-terminal domain / UvrD-like helicase, ATP-binding domain / UvrD-like DNA helicase ATP-binding domain profile. / DNA helicase, UvrD/REP type / DNA-directed RNA polymerase, subunit beta-prime, bacterial type / 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 Rpb1, domain 3 superfamily / RNA polymerase Rpb1, clamp domain 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 5 / RNA polymerase Rpb1, domain 4 / RNA polymerase Rpb1, domain 2 / RNA polymerase Rpb1, domain 5 / 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 / 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 / P-loop containing nucleoside triphosphate hydrolase 類似検索 - ドメイン・相同性 DNA-directed RNA polymerase subunit beta' / DNA-directed RNA polymerase subunit alpha / Probable DNA-directed RNA polymerase subunit delta / ATP-dependent DNA helicase rep / DNA-directed RNA polymerase subunit beta / DNA-directed RNA polymerase subunit epsilon / DNA-directed RNA polymerase subunit epsilon / DNA helicase IV / DNA-directed RNA polymerase subunit delta / DNA-directed RNA polymerase subunit alpha ... DNA-directed RNA polymerase subunit beta' / DNA-directed RNA polymerase subunit alpha / Probable DNA-directed RNA polymerase subunit delta / ATP-dependent DNA helicase rep / DNA-directed RNA polymerase subunit beta / DNA-directed RNA polymerase subunit epsilon / DNA-directed RNA polymerase subunit epsilon / DNA helicase IV / DNA-directed RNA polymerase subunit delta / DNA-directed RNA polymerase subunit alpha / DNA-directed RNA polymerase subunit beta / DNA-directed RNA polymerase subunit beta' 類似検索 - 構成要素生物種 Bacillus subtilis (枯草菌)手法 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度 : 4.23 Å 詳細 データ登録者Pei H / Hilal T / Huang Y / Said N / Loll B / Wahl MC 資金援助 ドイツ, 米国, 4件 詳細 詳細を隠すOrganization Grant number 国 German Research Foundation (DFG) HA 2549/15-2 ドイツ German Research Foundation (DFG) RTG 2473-1 ドイツ German Research Foundation (DFG) WA 1126/11-1 ドイツ National Institutes of Health/National Center for Complementary and Integrative Health (NIH/NCCIH) GM067153 米国
引用ジャーナル : Nat Commun / 年 : 2020タイトル : The δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling.著者 : Hao-Hong Pei / Tarek Hilal / Zhuo A Chen / Yong-Heng Huang / Yuan Gao / Nelly Said / Bernhard Loll / Juri Rappsilber / Georgiy A Belogurov / Irina Artsimovitch / Markus C Wahl / 要旨 : Cellular RNA polymerases (RNAPs) can become trapped on DNA or RNA, threatening genome stability and limiting free enzyme pools, but how RNAP recycling into active states is achieved remains elusive. ... Cellular RNA polymerases (RNAPs) can become trapped on DNA or RNA, threatening genome stability and limiting free enzyme pools, but how RNAP recycling into active states is achieved remains elusive. In Bacillus subtilis, the RNAP δ subunit and NTPase HelD have been implicated in RNAP recycling. We structurally analyzed Bacillus subtilis RNAP-δ-HelD complexes. HelD has two long arms: a Gre cleavage factor-like coiled-coil inserts deep into the RNAP secondary channel, dismantling the active site and displacing RNA, while a unique helical protrusion inserts into the main channel, prying the β and β' subunits apart and, aided by δ, dislodging DNA. RNAP is recycled when, after releasing trapped nucleic acids, HelD dissociates from the enzyme in an ATP-dependent manner. HelD abundance during slow growth and a dimeric (RNAP-δ-HelD) structure that resembles hibernating eukaryotic RNAP I suggest that HelD might also modulate active enzyme pools in response to cellular cues. 履歴 登録 2020年5月29日 - ヘッダ(付随情報) 公開 2020年10月14日 - マップ公開 2020年10月14日 - 更新 2021年4月28日 - 現状 2021年4月28日 処理サイト : PDBe / 状態 : 公開
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