ArticleNucleic acids research2012
Crosslinking-MS analysis reveals RNA polymerase I domain architecture and basis of rRNA cleavage.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 69 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
- Altering the ligand specificity of DectiSomes.The Journal of biological chemistry · 2025Article
- Regulation of ribosomal RNA gene copy number, transcription and nucleolus organization in eukaryotes.Nature reviews. Molecular cell biology · 2023Review
- RNA polymerase I (Pol I) lobe-binding subunit Rpa12.2 promotes RNA cleavage and proofreading.The Journal of biological chemistry · 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
- Targeted Cross-Linking Mass Spectrometry on Single-Step Affinity Purified Molecular Complexes in the Yeast Saccharomyces cerevisiae.Methods in molecular biology (Clifton, N.J.) · 2022Article
- The N-terminal domain of the A12.2 subunit stimulates RNA polymerase I transcription elongation.Biophysical journal · 2021Article
- Dynamics of the RNA polymerase I TFIIF/TFIIE-like subcomplex: a mini-review.Biochemical Society transactions · 2020Review
- RNA polymerase I (Pol I) passage through nucleosomes depends on Pol I subunits binding its lobe structure.The Journal of biological chemistry · 2020Article
- Conditional depletion of the RNA polymerase I subunit PAF53 reveals that it is essential for mitosis and enables identification of functional domains.The Journal of biological chemistry · 2019Article
- Structural and biochemical analyses of the nuclear pore complex component ELYS identify residues responsible for nucleosome binding.Communications biology · 2019Article
- The Vaccinia virion: Filling the gap between atomic and ultrastructure.PLoS pathogens · 2019Article
- An AP-MS- and BioID-compatible MAC-tag enables comprehensive mapping of protein interactions and subcellular localizations.Nature communications · 2018Article
- Functions of the TFIIE-Related Tandem Winged-Helix Domain of Rpc34 in RNA Polymerase III Initiation and Elongation.Molecular and cellular biology · 2018Article
- Cross-Linking Mass Spectrometry: An Emerging Technology for Interactomics and Structural Biology.Analytical chemistry · 2018Review
- Modeling Protein Excited-state Structures from "Over-length" Chemical Cross-links.The Journal of biological chemistry · 2017Article
- Article
- Molecular Structures of Transcribing RNA Polymerase I.Molecular cell · 2016Article
- The diverse and expanding role of mass spectrometry in structural and molecular biology.The EMBO journal · 2016Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
RNA polymerase (Pol) I contains a 10-subunit catalytic core that is related to the core of Pol II and includes subunit A12.2. In addition, Pol I contains the heterodimeric subcomplexes A14/43 and A49/34.5, which are related to the Pol II subcomplex Rpb4/7 and the Pol II initiation factor TFIIF, respectively. Here we used lysine-lysine crosslinking, mass spectrometry (MS) and modeling based on five crystal structures, to extend the previous homology model of the Pol I core, to confirm the location of A14/43 and to position A12.2 and A49/34.5 on the core. In the resulting model of Pol I, the C-terminal ribbon (C-ribbon) domain of A12.2 reaches the active site via the polymerase pore, like the C-ribbon of the Pol II cleavage factor TFIIS, explaining why the intrinsic RNA cleavage activity of Pol I is strong, in contrast to the weak cleavage activity of Pol II. The A49/34.5 dimerization module resides on the polymerase lobe, like TFIIF, whereas the A49 tWH domain resides above the cleft, resembling parts of TFIIE. This indicates that Pol I and also Pol III are distantly related to a Pol II-TFIIS-TFIIF-TFIIE complex.
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