ArticleNature2016
Structure of RNA polymerase I transcribing ribosomal DNA genes.
Article in Nature, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
What it found
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Who cites it
56 citing papers in PubMed, 94 citations in OpenAlex.
- Protein Secondary Structure Patterns in Short-Range Cross-Link Atlas.Angewandte Chemie (International ed. in English) · 2025Article
- Cryo-EM uncovers a sequential mechanism for RNA polymerase I pausing and stalling at abasic DNA lesions.Nature communications · 2025Article
- Coronin 2B deficiency induces nucleolar stress and neuronal apoptosis.Cell death & disease · 2024Article
- Structural basis of archaeal RNA polymerase transcription elongation and Spt4/5 recruitment.Nucleic acids research · 2024Article
- DNA-dependent RNA polymerases in plants.The Plant cell · 2023Article
- The A12.2 Subunit Plays an Integral Role in Pyrophosphate Release of RNA Polymerase I.Journal of molecular biology · 2023Article
- Regulation of ribosomal RNA gene copy number, transcription and nucleolus organization in eukaryotes.Nature reviews. Molecular cell biology · 2023Review
- Structure and mechanism of the plant RNA polymerase V.Science (New York, N.Y.) · 2023Article
- Archaea/eukaryote-specific ribosomal proteins - guardians of a complex structure.Computational and structural biotechnology journal · 2023Review
- 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
- How to Shut Down Transcription in Archaea during Virus Infection.Microorganisms · 2022Review
- Structural insights into nuclear transcription by eukaryotic DNA-dependent RNA polymerases.Nature reviews. Molecular cell biology · 2022Review
- RNA polymerase I (Pol I) lobe-binding subunit Rpa12.2 promotes RNA cleavage and proofreading.The Journal of biological chemistry · 2022Article
- A structural perspective of human RNA polymerase III.RNA biology · 2022Article
- Structural Studies of Eukaryotic RNA Polymerase I Using Cryo-Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Preparation of RNA Polymerase Complexes for Their Analysis by Single-Particle Cryo-Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Specialization of RNA Polymerase I in Comparison to Other Nuclear RNA Polymerases of Saccharomyces cerevisiae.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Establishment and Maintenance of Open Ribosomal RNA Gene Chromatin States in Eukaryotes.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Cryo-EM structures of human RNA polymerase I.Nature structural & molecular biology · 2021Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNA polymerase I (Pol I) is a highly processive enzyme that transcribes ribosomal DNA (rDNA) and regulates growth of eukaryotic cells. Crystal structures of free Pol I from the yeast Saccharomyces cerevisiae have revealed dimers of the enzyme stabilized by a 'connector' element and an expanded cleft containing the active centre in an inactive conformation. The central bridge helix was unfolded and a Pol-I-specific 'expander' element occupied the DNA-template-binding site. The structure of Pol I in its active transcribing conformation has yet to be determined, whereas structures of Pol II and Pol III have been solved with bound DNA template and RNA transcript. Here we report structures of active transcribing Pol I from yeast solved by two different cryo-electron microscopy approaches. A single-particle structure at 3.8 Å resolution reveals a contracted active centre cleft with bound DNA and RNA, and a narrowed pore beneath the active site that no longer holds the RNA-cleavage-stimulating domain of subunit A12.2. A structure at 29 Å resolution that was determined from cryo-electron tomograms of Pol I enzymes transcribing cellular rDNA confirms contraction of the cleft and reveals that incoming and exiting rDNA enclose an angle of around 150°. The structures suggest a model for the regulation of transcription elongation in which contracted and expanded polymerase conformations are associated with active and inactive states, respectively.
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Registered trials
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.