ArticleProceedings of the National Academy of Sciences of the United States of America2001
Kinetic trapping of DNA by transcription factor IIIB.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. 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.
- Cancer-associated TRF1 mutations alter PARP1 interaction dynamics: an in silico study.Mammalian genome : official journal of the International Mammalian Genome Society · 2026Article
- Structural basis of TFIIIC-dependent RNA polymerase III transcription initiation.Molecular cell · 2023Article
- 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
- Structure of the TFIIIC subcomplex τA provides insights into RNA polymerase III pre-initiation complex formation.Nature communications · 2020Article
- DNA origami-based single-molecule force spectroscopy elucidates RNA Polymerase III pre-initiation complex stability.Nature communications · 2020Article
- Determinants of Replication-Fork Pausing at tRNA Genes inGenetics · 2020Article
- Function of TFIIIC, RNA polymerase III initiation factor, in activation and repression of tRNA gene transcription.Nucleic acids research · 2018Article
- Article
- Differential Phosphorylation of RNA Polymerase III and the Initiation Factor TFIIIB in Saccharomyces cerevisiae.PloS one · 2015Article
- Intergenic transcriptional interference is blocked by RNA polymerase III transcription factor TFIIIB in Saccharomyces cerevisiae.Genetics · 2014Article
- Predicting expression: the complementary power of histone modification and transcription factor binding data.Epigenetics & chromatin · 2014Article
- Distinct promoter dynamics of the basal transcription factor TBP across the yeast genome.Nature structural & molecular biology · 2009Article
- Visual analysis of the yeast 5S rRNA gene transcriptome: regulation and role of La protein.Molecular and cellular biology · 2008Article
- Interactions of Brf1 peptides with the tetratricopeptide repeat-containing subunit of TFIIIC inhibit and promote preinitiation complex assembly.Molecular and cellular biology · 2006Article
- The Saccharomyces cerevisiae RNA polymerase III recruitment factor subunits Brf1 and Bdp1 impose a strict sequence preference for the downstream half of the TATA box.Nucleic acids research · 2006Article
- Global role of TATA box-binding protein recruitment to promoters in mediating gene expression profiles.Molecular and cellular biology · 2004Article
- A gain-of-function mutation in the second tetratricopeptide repeat of TFIIIC131 relieves autoinhibition of Brf1 binding.Molecular and cellular biology · 2002Article
- Regulation of pol III transcription by nutrient and stress signaling pathways.Biochimica et biophysica actaReview
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
High levels of RNA polymerase III gene transcription are achieved by facilitated recycling of the polymerase on transcription factor IIIB (TFIIIB)-DNA complexes that are stable through multiple rounds of initiation. TFIIIB-DNA complexes in yeast comprise the TATA-binding protein (TBP), the TFIIB-related factor TFIIIB70, and TFIIIB90. The high stability of the TFIIIB-DNA complex is conferred by TFIIIB90 binding to TFIIIB70-TBP-DNA complexes. This stability is thought to result from compound bends introduced in the DNA by TBP and TFIIIB90 and by protein-protein interactions that obstruct DNA dissociation. Here we present biochemical evidence that the high stability of TFIIIB-DNA complexes results from kinetic trapping of the DNA. Thermodynamic analysis shows that the free energies of formation of TFIIIB70-TBP-DNA (DeltaG degrees = -12.10 +/- 0.12 kcal/mol) and TFIIIB-DNA (DeltaG degrees = -11.90 +/- 0.14 kcal/mol) complexes are equivalent whereas a kinetic analysis shows that the half-lives of these complexes (46 +/- 3 min and 95 +/- 6 min, respectively) differ significantly. The differential stability of these isoenergetic complexes demonstrates that TFIIIB90 binding energy is used to drive conformational changes and increase the barrier to complex dissociation.
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