9EHZ
Cryo-EM structure of Human RNA polymerase II Elongation Complex in an Intermediate Translocation State
Summary for 9EHZ
| Entry DOI | 10.2210/pdb9ehz/pdb |
| EMDB information | 48071 |
| Descriptor | DNA-directed RNA polymerase II subunit RPB4, Non-template DNA, nucleic acid scaffold, RNA, nucleic acid scaffold, ... (17 entities in total) |
| Functional Keywords | translocation, human rna polymerase ii, transcription, transferase-dna-rna complex, transferase/dna/rna |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 15 |
| Total formula weight | 546221.25 |
| Authors | |
| Primary citation | Ariza, A.J.F.,Lue, N.Z.,Grob, P.,Kaeser, B.,Fang, J.,Kassube, S.A.,Nogales, E. Structural insights into transcriptional regulation by the helicase RECQL5. Biorxiv, 2025 Cited by PubMed Abstract: Transcription and its regulation pose a major challenge for genome stability. The helicase RECQL5 has been proposed as an important factor to help safeguard the genome, and is the only member of the human RecQ helicase family that directly binds to RNA Polymerase II (Pol II) and affects its progression. RECQL5 mitigates transcription stress and genome instability in cells, yet the molecular mechanism underlying this phenomenon is unclear. Here, we employ cryo-electron microscopy (cryo-EM) to determine the structures of stalled 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 RECQL5 can modulate the Pol II translocation state. In its nucleotide-free state, RECQL5 mechanically twists the downstream DNA in the EC, and upon nucleotide binding, it undergoes a conformational change that allosterically induces Pol II towards a post-translocation state. We propose this mechanism may help restart Pol II elongation and therefore contribute to reduction of transcription stress. PubMed: 39975028DOI: 10.1101/2025.01.29.634372 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.6 Å) |
Structure validation
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