ArticleNucleic acids research2013
RNA polymerase III-specific general transcription factor IIIC contains a heterodimer resembling TFIIF Rap30/Rap74.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 28 citations in OpenAlex.
- Mechanism of interaction between the transactivation domain of N-myc and the DNA-binding surface of TFIIIC5.Nucleic acids research · 2026Article
- Should I stay or should I go: TFIIIC as assembly factor and barrier in RNA polymerase III transcription.Biochemical Society transactions · 2025Review
- Structural and kinetic insights into tRNA promoter engagement by yeast general transcription factor TFIIIC.Nucleic acids research · 2025Article
- Characterization of Tau95 led to the identification of a four-subunit TFIIIC complex in trypanosomatid parasites.Applied microbiology and biotechnology · 2024Article
- Biallelic variants in GTF3C5, a regulator of RNA polymerase III-mediated transcription, cause a multisystem developmental disorder.Human genetics · 2024Article
- Unveiling the role of GAS41 in cancer progression.Cancer cell international · 2023Review
- Structural insights into human TFIIIC promoter recognition.Science advances · 2023Article
- Structure of the TFIIIC subcomplex τA provides insights into RNA polymerase III pre-initiation complex formation.Nature communications · 2020Article
- Nucleotide Loading Modes of Human RNA Polymerase II as Deciphered by Molecular Simulations.Biomolecules · 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 studies of RFCEMBO reports · 2017Article
- Specialization versus conservation: How Pol I and Pol III use the conserved architecture of the pre-initiation complex for specialized transcription.Transcription · 2016Review
- Super elongation complex contains a TFIIF-related subcomplex.Transcription · 2016Article
- Zooming in on Transcription Preinitiation.Journal of molecular biology · 2016Review
- Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly.Nature communications · 2015Article
- Crystal structure of a TAF1-TAF7 complex in human transcription factor IID reveals a promoter binding module.Cell research · 2014Article
- Structural and functional insight into TAF1-TAF7, a subcomplex of transcription factor II D.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Comparative overview of RNA polymerase II and III transcription cycles, with focus on RNA polymerase III termination and reinitiation.Transcription · 2014Review
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transcription of tRNA-encoding genes by RNA polymerase (Pol) III requires the six-subunit general transcription factor IIIC that uses subcomplexes τA and τB to recognize two gene-internal promoter elements named A- and B-box. The Schizosaccharomyces pombe τA subcomplex comprises subunits Sfc1, Sfc4 and Sfc7. The crystal structure of the Sfc1/Sfc7 heterodimer reveals similar domains and overall domain architecture to the Pol II-specific general transcription factor TFIIF Rap30/Rap74. The N-terminal Sfc1/Sfc7 dimerization module consists of a triple β-barrel similar to the N-terminal TFIIF Rap30/Rap74 dimerization module, whereas the C-terminal Sfc1 DNA-binding domain contains a winged-helix domain most similar to the TFIIF Rap30 C-terminal winged-helix domain. Sfc1 DNA-binding domain recognizes single and double-stranded DNA by an unknown mechanism. Several features observed for A-box recognition by τA resemble the recognition of promoters by bacterial RNA polymerase, where σ factor unfolds double-stranded DNA and stabilizes the non-coding DNA strand in an open conformation. Such a function has also been proposed for TFIIF, suggesting that the observed structural similarity between Sfc1/Sfc7 and TFIIF Rap30/Rap74 might also reflect similar functions.
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