9EI1
Cryo-EM structure of Human RNA polymerase II Elongation Complex bound to the RECQL5 helicase in the absence of nucleotide
9EI1 の概要
| エントリーDOI | 10.2210/pdb9ei1/pdb |
| EMDBエントリー | 48073 |
| 分子名称 | DNA-directed RNA polymerase II subunit RPB1, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerase II subunit RPB11-a, ... (18 entities in total) |
| 機能のキーワード | translocation, human rna polymerase ii, recql5 helicase, transcription, transferase-dna-rna complex, transferase/dna/rna |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| タンパク質・核酸の鎖数 | 16 |
| 化学式量合計 | 655202.09 |
| 構造登録者 | |
| 主引用文献 | Florez Ariza, A.J.,Lue, N.Z.,Grob, P.,Kaeser, B.,Fang, J.,Kassube, S.A.,Nogales, E. Structural insights into transcriptional regulation by the helicase RECQL5. Nat.Struct.Mol.Biol., 32:1721-1730, 2025 Cited by PubMed Abstract: Transcription poses a major challenge for genome stability. The RECQL5 helicase helps safeguard genome integrity and is the only member of the human RecQ helicase family that directly binds to RNA polymerase II (Pol II) and affects its progression. While RECQL5 mitigates transcription stress in cells, the molecular mechanism underlying this phenomenon is unclear. Here, we use cryo-electron microscopy to determine the structures of stalled human Pol II elongation complexes (ECs) bound to RECQL5. Our structures reveal the molecular interactions stabilizing RECQL5 binding to the Pol II EC and highlight its role as a transcriptional roadblock. Additionally, we find that, in its nucleotide-free state, RECQL5 twists the downstream DNA in the EC and, upon nucleotide binding, undergoes a conformational change that allosterically induces Pol II toward a post-translocation state. We propose that this mechanism may help restart Pol II elongation and, therefore, contribute to reducing transcription stress. PubMed: 40624164DOI: 10.1038/s41594-025-01611-8 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.2 Å) |
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