6C6U
CryoEM structure of E.coli RNA polymerase elongation complex bound with NusG
6C6U の概要
エントリーDOI | 10.2210/pdb6c6u/pdb |
EMDBエントリー | 7350 7351 |
分子名称 | DNA (29-MER), ZINC ION, RNA (5'-R(*GP*CP*AP*UP*UP*CP*AP*AP*AP*GP*CP*CP*GP*AP*GP*AP*GP*GP*UP*A)-3'), ... (10 entities in total) |
機能のキーワード | rnap, elongation complex, anti-pausing, transcription, transcription-dna-rna complex, transcription/dna/rna |
由来する生物種 | Escherichia coli (strain K12) 詳細 |
タンパク質・核酸の鎖数 | 9 |
化学式量合計 | 414381.47 |
構造登録者 | Kang, J.Y.,Artsimovitch, I.,Landick, R.,Darst, S.A. (登録日: 2018-01-19, 公開日: 2018-07-25, 最終更新日: 2024-03-13) |
主引用文献 | Kang, J.Y.,Mooney, R.A.,Nedialkov, Y.,Saba, J.,Mishanina, T.V.,Artsimovitch, I.,Landick, R.,Darst, S.A. Structural Basis for Transcript Elongation Control by NusG Family Universal Regulators. Cell, 173:1650-1662.e14, 2018 Cited by PubMed Abstract: NusG/RfaH/Spt5 transcription elongation factors are the only transcription regulators conserved across all life. Bacterial NusG regulates RNA polymerase (RNAP) elongation complexes (ECs) across most genes, enhancing elongation by suppressing RNAP backtracking and coordinating ρ-dependent termination and translation. The NusG paralog RfaH engages the EC only at operon polarity suppressor (ops) sites and suppresses both backtrack and hairpin-stabilized pausing. We used single-particle cryoelectron microscopy (cryo-EM) to determine structures of ECs at ops with NusG or RfaH. Both factors chaperone base-pairing of the upstream duplex DNA to suppress backtracking, explaining stimulation of elongation genome-wide. The RfaH-opsEC structure reveals how RfaH confers operon specificity through specific recognition of an ops hairpin in the single-stranded nontemplate DNA and tighter binding to the EC to exclude NusG. Tight EC binding by RfaH sterically blocks the swiveled RNAP conformation necessary for hairpin-stabilized pausing. The universal conservation of NusG/RfaH/Spt5 suggests that the molecular mechanisms uncovered here are widespread. PubMed: 29887376DOI: 10.1016/j.cell.2018.05.017 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.7 Å) |
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