ArticleGenes & development2009
Structures of three distinct activator-TFIID complexes.
Article in Genes & development, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
48 citing papers in PubMed, 63 citations in OpenAlex.
- A transcription factor by any other name - function beyond DNA binding and transactivation.EMBO reports · 2026Review
- Regulation of the RNA polymerase II pre-initiation complex by its associated coactivators.Nature reviews. Genetics · 2023Review
- What do Transcription Factors Interact With?Journal of molecular biology · 2021Review
- Structure of the p53/RNA polymerase II assembly.Communications biology · 2021Article
- Multiple direct interactions of TBP with the MYC oncoprotein.Nature structural & molecular biology · 2019Article
- Structure of human TFIID and mechanism of TBP loading onto promoter DNA.Science (New York, N.Y.) · 2018Article
- Article
- Eukaryotic core promoters and the functional basis of transcription initiation.Nature reviews. Molecular cell biology · 2018Review
- A new era of studying p53-mediated transcription activation.Transcription · 2018Article
- Towards a mechanistic understanding of core promoter recognition from cryo-EM studies of human TFIID.Current opinion in structural biology · 2017Review
- p53 Dynamically Directs TFIID Assembly on Target Gene Promoters.Molecular and cellular biology · 2017Article
- Structural Insights into the Eukaryotic Transcription Initiation Machinery.Annual review of biophysics · 2017Review
- Functional specialization of two paralogous TAF12 variants by their selective association with SAGA and TFIID transcriptional regulatory complexes.The Journal of biological chemistry · 2017Article
- Discovery and validation of information theory-based transcription factor and cofactor binding site motifs.Nucleic acids research · 2017Article
- Structural dynamics and DNA interaction of human TFIID.Transcription · 2017Article
- Regulatory Enhancer-Core-Promoter Communication via Transcription Factors and Cofactors.Trends in genetics : TIG · 2016Review
- Structural visualization of the p53/RNA polymerase II assembly.Genes & development · 2016Article
- The C Terminus of the RNA Polymerase II Transcription Factor IID (TFIID) Subunit Taf2 Mediates Stable Association of Subunit Taf14 into the Yeast TFIID Complex.The Journal of biological chemistry · 2016Article
- Cryo-EM in the study of challenging systems: the human transcription pre-initiation complex.Current opinion in structural biology · 2016Review
- JNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnerships.Microbiology and molecular biology reviews : MMBR · 2016Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Sequence-specific DNA-binding activators, key regulators of gene expression, stimulate transcription in part by targeting the core promoter recognition TFIID complex and aiding in its recruitment to promoter DNA. Although it has been established that activators can interact with multiple components of TFIID, it is unknown whether common or distinct surfaces within TFIID are targeted by activators and what changes if any in the structure of TFIID may occur upon binding activators. As a first step toward structurally dissecting activator/TFIID interactions, we determined the three-dimensional structures of TFIID bound to three distinct activators (i.e., the tumor suppressor p53 protein, glutamine-rich Sp1 and the oncoprotein c-Jun) and compared their structures as determined by electron microscopy and single-particle reconstruction. By a combination of EM and biochemical mapping analysis, our results uncover distinct contact regions within TFIID bound by each activator. Unlike the coactivator CRSP/Mediator complex that undergoes drastic and global structural changes upon activator binding, instead, a rather confined set of local conserved structural changes were observed when each activator binds holo-TFIID. These results suggest that activator contact may induce unique structural features of TFIID, thus providing nanoscale information on activator-dependent TFIID assembly and transcription initiation.
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Registered trials
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.