ArticleGenes & development2016
Rapid dynamics of general transcription factor TFIIB binding during preinitiation complex assembly revealed by single-molecule analysis.
Article in Genes & development, 2016. 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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Who cites it
52 citing papers in PubMed, 78 citations in OpenAlex.
- Cleavage of the RNA polymerase II general transcription factor TFIIB tunes transcription during stress.Genes & development · 2026Article
- Live-cell single-molecule dynamics of eukaryotic RNA polymerase machineries.Science (New York, N.Y.) · 2026Article
- RNA polymerase II initiation factors show different dynamic behaviour upon induced transcription in live cells.bioRxiv : the preprint server for biology · 2025Article
- Single-molecule Microscopy Reveals That TFIIE Subunits Dynamically Interact With Preinitiation Complexes in a Manner Impacted by TFIIH.Journal of molecular biology · 2025Article
- Short activation domains control chromatin association of transcription factors.bioRxiv : the preprint server for biology · 2025Article
- Single-molecule imaging for investigating the transcriptional control.Molecules and cells · 2025Review
- Quantifying Transcription Factor Enrichment at Target Loci in Live Embryos.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Embryo Development in a Stochastic Universe.Bioelectricity · 2024Article
- Genome-scale chromatin binding dynamics of RNA Polymerase II general transcription machinery components.The EMBO journal · 2024Article
- Real-time single-molecule imaging of transcriptional regulatory networks in living cells.Nature reviews. Genetics · 2024Review
- Mechanisms and Functions of the RNA Polymerase II General Transcription Machinery during the Transcription Cycle.Biomolecules · 2024Review
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- TBP facilitates RNA Polymerase I transcription following mitosis.RNA biology · 2024Article
- Protein interaction network revealed by quantitative proteomic analysis links TFIIB to multiple aspects of the transcription cycle.Biochimica et biophysica acta. Proteins and proteomics · 2024Article
- Regulation of the RNA polymerase II pre-initiation complex by its associated coactivators.Nature reviews. Genetics · 2023Review
- Single-molecule tracking (SMT): a window into live-cell transcription biochemistry.Biochemical Society transactions · 2023Article
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- Regulatory Mechanisms for Transcriptional Bursting Revealed by an Event-Based Model.Research (Washington, D.C.) · 2023Article
- Activation domains can decouple the mean and noise of gene expression.Cell reports · 2022Article
Corrections and comments
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Authors and funding
13 authors at 6 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transcription of protein-encoding genes in eukaryotic cells requires the coordinated action of multiple general transcription factors (GTFs) and RNA polymerase II (Pol II). A "step-wise" preinitiation complex (PIC) assembly model has been suggested based on conventional ensemble biochemical measurements, in which protein factors bind stably to the promoter DNA sequentially to build a functional PIC. However, recent dynamic measurements in live cells suggest that transcription factors mostly interact with chromatin DNA rather transiently. To gain a clearer dynamic picture of PIC assembly, we established an integrated in vitro single-molecule transcription platform reconstituted from highly purified human transcription factors and complemented it by live-cell imaging. Here we performed real-time measurements of the hierarchal promoter-specific binding of TFIID, TFIIA, and TFIIB. Surprisingly, we found that while promoter binding of TFIID and TFIIA is stable, promoter binding by TFIIB is highly transient and dynamic (with an average residence time of 1.5 sec). Stable TFIIB-promoter association and progression beyond this apparent PIC assembly checkpoint control occurs only in the presence of Pol II-TFIIF. This transient-to-stable transition of TFIIB-binding dynamics has gone undetected previously and underscores the advantages of single-molecule assays for revealing the dynamic nature of complex biological reactions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.