ArticleMolecular and cellular biology2011
The TFIIF-like Rpc37/53 dimer lies at the center of a protein network to connect TFIIIC, Bdp1, and the RNA polymerase III active center.
Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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52 citing papers in PubMed, 69 citations in OpenAlex.
- Mutational and biophysical analyses reveal a TFIIIC binding region in the TFIIF-related Rpc53 subunit of RNA polymerase III.The Journal of biological chemistry · 2023Article
- Site-directed biochemical analyses reveal that the switchable C-terminus of Rpc31 contributes to RNA polymerase III transcription initiation.Nucleic acids research · 2023Article
- Structural basis of Ty1 integrase tethering to RNA polymerase III for targeted retrotransposon integration.Nature communications · 2023Article
- Structural insights into nuclear transcription by eukaryotic DNA-dependent RNA polymerases.Nature reviews. Molecular cell biology · 2022Review
- The nuclear and cytoplasmic activities of RNA polymerase III, and an evolving transcriptome for surveillance.Nucleic acids research · 2021Article
- Mechanism of RNA polymerase III termination-associated reinitiation-recycling conferred by the essential function of the N terminal-and-linker domain of the C11 subunit.Nature communications · 2021Article
- Light and shadow on the mechanisms of integration site selection in yeast Ty retrotransposon families.Current genetics · 2021Review
- A mutation in POLR3E impairs antiviral immune response and RNA polymerase III.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Nucleotide Loading Modes of Human RNA Polymerase II as Deciphered by Molecular Simulations.Biomolecules · 2020Article
- Loss of Function of an RNA Polymerase III Subunit Leads to Impaired Maize Kernel Development.Plant physiology · 2020Article
- Desumoylation of RNA polymerase III lies at the core of the Sumo stress response in yeast.The Journal of biological chemistry · 2019Article
- Electron-deficient p-benzoyl-l-phenylalanine derivatives increase covalent chemical capture yields for protein-protein interactions.Protein science : a publication of the Protein Society · 2019Article
- Genetic analyses led to the discovery of a super-active mutant of the RNA polymerase I.PLoS genetics · 2019Article
- RNA polymerase III subunits C37/53 modulate rU:dA hybrid 3' end dynamics during transcription termination.Nucleic acids research · 2019Article
- The Structures of Eukaryotic Transcription Pre-initiation Complexes and Their Functional Implications.Sub-cellular biochemistry · 2019Review
- Signaling to and from the RNA Polymerase III Transcription and Processing Machinery.Annual review of biochemistry · 2018Review
- The TFIIE-related Rpc82 subunit of RNA polymerase III interacts with the TFIIB-related transcription factor Brf1 and the polymerase cleft for transcription initiation.Nucleic acids research · 2018Article
- Functions of the TFIIE-Related Tandem Winged-Helix Domain of Rpc34 in RNA Polymerase III Initiation and Elongation.Molecular and cellular biology · 2018Article
- Article
- Structural visualization of RNA polymerase III transcription machineries.Cell discovery · 2018Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic RNA polymerase III (Pol III) relies on a transcription factor TFIIF-like Rpc37/53 subcomplex for promoter opening, elongation, termination, and reinitiation. By incorporating the photoreactive amino acid p-benzoyl-L-phenylalanine (BPA) into Rpc37, Rpc53, and the Rpc2 subunit of Pol III, we mapped protein-protein interactions, revealing the position of Rpc37/53 within the Pol III preinitiation complex (PIC). BPA photo-cross-linking was combined with site-directed hydroxyl radical probing to localize the Rpc37/53 dimerization module on the lobe/external 2 domains of Rpc2, in similarity to the binding of TFIIF on Pol II. N terminal to the dimerization domain, Rpc53 binds the Pol III-specific subunits Rpc82 and Rpc34, the Pol III stalk, and the assembly factor TFIIIC, essential for PIC formation. The C-terminal domain of Rpc37 interacts extensively with Rpc2 and Rpc34 and contains binding sites for initiation factor Bdp1. We also located the C-terminal domain of Rpc37 within the Pol III active center in the ternary elongation complex, where it likely functions in accurate termination. Our work explains how the Rpc37/53 dimer is anchored on the Pol III core and acts as a hub to integrate a protein network for initiation and termination.
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