ArticleeLife2019
The cryo-EM structure of a 12-subunit variant of RNA polymerase I reveals dissociation of the A49-A34.5 heterodimer and rearrangement of subunit A12.2.
Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 45 citations in OpenAlex.
- Dynamic landscape of transcription initiation by yeast RNA polymerase I.Nucleic acids research · 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
- Embracing Heterogeneity: Challenging the Paradigm of Replisomes as Deterministic Machines.Chemical reviews · 2023Review
- The A12.2 Subunit Plays an Integral Role in Pyrophosphate Release of RNA Polymerase I.Journal of molecular biology · 2023Article
- 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
- A structural perspective of human RNA polymerase III.RNA biology · 2022Article
- Specialization of RNA Polymerase I in Comparison to Other Nuclear RNA Polymerases of Saccharomyces cerevisiae.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Structural Studies of Eukaryotic RNA Polymerase I Using Cryo-Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Evolution of the RNA Cleavage Subunit C11/RPC10, and Recycling by RNA Polymerase III.Journal of cellular immunology · 2022Article
- Structural insights into RNA polymerase III-mediated transcription termination through trapping poly-deoxythymidine.Nature communications · 2021Article
- Structure of the human RNA polymerase I elongation complex.Cell discovery · 2021Article
- The N-terminal domain of the A12.2 subunit stimulates RNA polymerase I transcription elongation.Biophysical journal · 2021Article
- Review
- Conserved strategies of RNA polymerase I hibernation and activation.Nature communications · 2021Article
- Structural insights into transcriptional regulation of human RNA polymerase III.Nature structural & molecular biology · 2021Article
- Coupling Between Production of Ribosomal RNA and Maturation: Just at the Beginning.Frontiers in molecular biosciences · 2021Review
- Article
- Dynamics of the RNA polymerase I TFIIF/TFIIE-like subcomplex: a mini-review.Biochemical Society transactions · 2020Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
RNA polymerase (Pol) I is a 14-subunit enzyme that solely transcribes pre-ribosomal RNA. Cryo-electron microscopy (EM) structures of Pol I initiation and elongation complexes have given first insights into the molecular mechanisms of Pol I transcription. Here, we present cryo-EM structures of yeast Pol I elongation complexes (ECs) bound to the nucleotide analog GMPCPP at 3.2 to 3.4 Å resolution that provide additional insight into the functional interplay between the Pol I-specific transcription-like factors A49-A34.5 and A12.2. Strikingly, most of the nucleotide-bound ECs lack the A49-A34.5 heterodimer and adopt a Pol II-like conformation, in which the A12.2 C-terminal domain is bound in a previously unobserved position at the A135 surface. Our structural and biochemical data suggest a mechanism where reversible binding of the A49-A34.5 heterodimer could contribute to the regulation of Pol I transcription initiation and elongation.
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