ArticleNature communications2019
Molecular insight into RNA polymerase I promoter recognition and promoter melting.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 55 citations in OpenAlex.
- Dynamic positioning of Rpc34 winged helix in RNA polymerase III elongation complex for its stability with implications for reinitiation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Dynamic landscape of transcription initiation by yeast RNA polymerase I.Nucleic acids research · 2026Article
- Ribosomal RNA synthesis by RNA polymerase I is subject to premature termination of transcription.eLife · 2026Article
- Clinical significance and functional characterization of RRN3 in gastric cancer: insights from pan-cancer analysis and experimental validation.Frontiers in oncology · 2026Article
- The ribosomal RNA transcription landscapes of Plasmodium falciparum and related apicomplexan parasites.Nucleic acids research · 2025Review
- Cryo-EM uncovers a sequential mechanism for RNA polymerase I pausing and stalling at abasic DNA lesions.Nature communications · 2025Article
- The Nucleolus: A Central Hub for Ribosome Biogenesis and Cellular Regulatory Signals.International journal of molecular sciences · 2025Review
- Remote homology identification of themicroPublication biology · 2024Article
- RNA polymerase I mutant affects ribosomal RNA processing and ribosomal DNA stability.RNA biology · 2024Article
- DNA-dependent RNA polymerases in plants.The Plant cell · 2023Article
- Regulation of ribosomal RNA gene copy number, transcription and nucleolus organization in eukaryotes.Nature reviews. Molecular cell biology · 2023Review
- Ribosome biogenesis factors-from names to functions.The EMBO journal · 2023Review
- Roles of ribosomal RNA in health and disease.Frontiers in RNA research · 2023Article
- Regulation of RNA Polymerase I Stability and Function.Cancers · 2022Review
- The human RNA polymerase I structure reveals an HMG-like docking domain specific to metazoans.Life science alliance · 2022Article
- Structural insights into nuclear transcription by eukaryotic DNA-dependent RNA polymerases.Nature reviews. Molecular cell biology · 2022Review
- Mechanism of RNA polymerase I selection by transcription factor UAF.Science advances · 2022Article
- Structural Studies of Eukaryotic RNA Polymerase I Using Cryo-Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Structure of the human RNA polymerase I elongation complex.Cell discovery · 2021Article
- Structural basis of RNA polymerase inhibition by viral and host factors.Nature communications · 2021Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNA polymerase I (Pol I) assembles with core factor (CF) and Rrn3 on the rDNA core promoter for transcription initiation. Here, we report cryo-EM structures of closed, intermediate and open Pol I initiation complexes from 2.7 to 3.7 Å resolution to visualize Pol I promoter melting and to structurally and biochemically characterize the recognition mechanism of Pol I promoter DNA. In the closed complex, double-stranded DNA runs outside the DNA-binding cleft. Rotation of CF and upstream DNA with respect to Pol I and Rrn3 results in the spontaneous loading and opening of the promoter followed by cleft closure and positioning of the Pol I A49 tandem winged helix domain (tWH) onto DNA. Conformational rearrangement of A49 tWH leads to a clash with Rrn3 to initiate complex disassembly and promoter escape. Comprehensive insight into the Pol I transcription initiation cycle allows comparisons with promoter opening by Pol II and Pol III.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.