ArticleProceedings of the National Academy of Sciences of the United States of America2005
Reconfiguring the connectivity of a multiprotein complex: fusions of yeast TATA-binding protein with Brf1, and the function of transcription factor IIIB.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 36 citations in OpenAlex.
- Elucidating the molecular properties and anti-mycobacterial activity of cysteine peptidase domain of D29 mycobacteriophage endolysin.Journal of virology · 2024Article
- Structural basis of TFIIIC-dependent RNA polymerase III transcription initiation.Molecular cell · 2023Article
- Structure of the TFIIIC subcomplex τA provides insights into RNA polymerase III pre-initiation complex formation.Nature communications · 2020Article
- Determinants of Replication-Fork Pausing at tRNA Genes inGenetics · 2020Article
- The Structures of Eukaryotic Transcription Pre-initiation Complexes and Their Functional Implications.Sub-cellular biochemistry · 2019Review
- Article
- Structural visualization of RNA polymerase III transcription machineries.Cell discovery · 2018Article
- Retrotransposon targeting to RNA polymerase III-transcribed genes.Mobile DNA · 2018Review
- Molecular mechanisms of Bdp1 in TFIIIB assembly and RNA polymerase III transcription initiation.Nature communications · 2017Article
- Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly.Nature communications · 2015Article
- Article
- In vitro targeting of strand transfer by the Ty3 retroelement integrase.The Journal of biological chemistry · 2012Article
- The C53/C37 subcomplex of RNA polymerase III lies near the active site and participates in promoter opening.The Journal of biological chemistry · 2010Article
- Requirement of Nhp6 proteins for transcription of a subset of tRNA genes and heterochromatin barrier function in Saccharomyces cerevisiae.Molecular and cellular biology · 2007Article
- Interactions of Brf1 peptides with the tetratricopeptide repeat-containing subunit of TFIIIC inhibit and promote preinitiation complex assembly.Molecular and cellular biology · 2006Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transcription factor (TF) IIIB, the central transcription initiation factor of RNA polymerase III (pol III), is composed of three subunits, Bdp1, Brf1 and TATA-binding protein (TBP), all essential for normal function in vivo and in vitro. Brf1 is a modular protein: Its N-proximal half is related to TFIIB and binds similarly to the C-terminal stirrup of TBP; its C-proximal one-third provides most of the affinity for TBP by binding along the entire length of the convex surface and N-terminal lateral face of TBP. A structure-informed triple fusion protein, with TBP core placed between the N- and C-proximal domains of Brf1, has been constructed. The Brf1-TBP triple fusion protein effectively replaces both Brf1 and TBP in TFIIIC-dependent and -independent transcription in vitro, and forms extremely stable TFIIIB-DNA complexes that are indistinguishable from wild-type TFIIIB-DNA complexes by chemical nuclease footprinting. Unlike Brf1 and TBP, the triple fusion protein is able to recruit pol III for TATA box-directed transcription of linear and supercoiled DNA in the absence of Bdp1. The Brf1-TBP triple fusion protein also effectively replaces Brf1 function in vivo as the intact protein, creating a TBP paralogue in yeast that is privatized for pol III transcription.
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