ArticleLife science alliance2022
The human RNA polymerase I structure reveals an HMG-like docking domain specific to metazoans.
Article in Life science alliance, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- RiboScreenBiomedicines · 2026Review
- 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
- Article
- Crossing boundaries of light microscopy resolution discerns novel assemblies in the nucleolus.Histochemistry and cell biology · 2024Article
- Structural basis of archaeal RNA polymerase transcription elongation and Spt4/5 recruitment.Nucleic acids research · 2024Article
- Polymerase I as a Target for Treating Neurodegenerative Disorders.Biomedicines · 2024Review
- Regulation of ribosomal RNA gene copy number, transcription and nucleolus organization in eukaryotes.Nature reviews. Molecular cell biology · 2023Review
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Authors and funding
19 authors.
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Abstract
Transcription of the ribosomal RNA precursor by RNA polymerase (Pol) I is a major determinant of cellular growth, and dysregulation is observed in many cancer types. Here, we present the purification of human Pol I from cells carrying a genomic GFP fusion on the largest subunit allowing the structural and functional analysis of the enzyme across species. In contrast to yeast, human Pol I carries a single-subunit stalk, and in vitro transcription indicates a reduced proofreading activity. Determination of the human Pol I cryo-EM reconstruction in a close-to-native state rationalizes the effects of disease-associated mutations and uncovers an additional domain that is built into the sequence of Pol I subunit RPA1. This "dock II" domain resembles a truncated HMG box incapable of DNA binding which may serve as a downstream transcription factor-binding platform in metazoans. Biochemical analysis, in situ modelling, and ChIP data indicate that Topoisomerase 2a can be recruited to Pol I via the domain and cooperates with the HMG box domain-containing factor UBF. These adaptations of the metazoan Pol I transcription system may allow efficient release of positive DNA supercoils accumulating downstream of the transcription bubble.
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