ArticleNature communications2017
Molecular mechanisms of Bdp1 in TFIIIB assembly and RNA polymerase III transcription initiation.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 59 citations in OpenAlex.
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- Two distinct SWI/SNF complexes direct chromatin-linked transcriptional programs in Toxoplasma.Nature communications · 2026Article
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- Aspergillus fumigatus dsRNA virus promotes fungal fitness and pathogenicity in the mammalian host.Nature microbiology · 2025Article
- Should I stay or should I go: TFIIIC as assembly factor and barrier in RNA polymerase III transcription.Biochemical Society transactions · 2025Review
- The Central FacilitaTOR: Coordinating Transcription and Translation in Eukaryotes.International journal of molecular sciences · 2025Review
- Structural insights into distinct mechanisms of RNA polymerase II and III recruitment to snRNA promoters.Nature communications · 2025Article
- Distinctive physical properties of DNA shared by RNA polymerase II gene promoters and 5'-flanking regions of tRNA genes.Journal of biochemistry · 2024Article
- Structure of the SNAPc-bound RNA polymerase III preinitiation complex.Cell research · 2023Article
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- BDP1 as a biomarker in serous ovarian cancer.Cancer medicine · 2023Article
- Structural basis of human SNAPc recognizing proximal sequence element of snRNA promoter.Nature communications · 2022Article
- Transcriptional factor III A promotes colorectal cancer progression by upregulating cystatin A.World journal of gastrointestinal oncology · 2022Article
- Structural insights into nuclear transcription by eukaryotic DNA-dependent RNA polymerases.Nature reviews. Molecular cell biology · 2022Review
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- Reply to Schramm, L. Comment on "Li et al.Diagnostics (Basel, Switzerland) · 2022Article
- A structural perspective of human RNA polymerase III.RNA biology · 2022Article
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
Abstract
Initiation of gene transcription by RNA polymerase (Pol) III requires the activity of TFIIIB, a complex formed by Brf1 (or Brf2), TBP (TATA-binding protein), and Bdp1. TFIIIB is required for recruitment of Pol III and to promote the transition from a closed to an open Pol III pre-initiation complex, a process dependent on the activity of the Bdp1 subunit. Here, we present a crystal structure of a Brf2-TBP-Bdp1 complex bound to DNA at 2.7 Å resolution, integrated with single-molecule FRET analysis and in vitro biochemical assays. Our study provides a structural insight on how Bdp1 is assembled into TFIIIB complexes, reveals structural and functional similarities between Bdp1 and Pol II factors TFIIA and TFIIF, and unravels essential interactions with DNA and with the upstream factor SNAPc. Furthermore, our data support the idea of a concerted mechanism involving TFIIIB and RNA polymerase III subunits for the closed to open pre-initiation complex transition.Transcription initiation by RNA polymerase III requires TFIIIB, a complex formed by Brf1/Brf2, TBP and Bdp1. Here, the authors describe the crystal structure of a Brf2-TBP-Bdp1 complex bound to a DNA promoter and characterize the role of Bdp1 in TFIIIB assembly and pre-initiation complex formation.
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