ArticleCell research2014
Crystal structure of a TAF1-TAF7 complex in human transcription factor IID reveals a promoter binding module.
Article in Cell research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 55 citations in OpenAlex.
- TAF1 aggravates ferroptosis by promoting the ubiquitin-mediated degradation of nuclear GPX4.Journal of Zhejiang University. Science. B · 2026Article
- PROTAC-Mediated Degradation of TAF1 Induces Apoptosis in AML Cells and Inhibits Tumor Growth In Vivo.Molecular cancer therapeutics · 2025Article
- TAF1 is required for fetal but not adult hematopoiesis in mice.Developmental cell · 2025Article
- TAF7 directly targets SAA1 to enhance triple-negative breast cancer metastasis via phosphorylating E-cadherin and N-cadherin.iScience · 2025Article
- The roles of TAF1 in neuroscience and beyond.Royal Society open science · 2024Review
- LncR-GAS5 decrease in adenine phosphoribosyltransferase expresssion via binding TAF1 to increase kidney damage created by CIH.Heliyon · 2024Article
- Representing mutations for predicting cancer drug response.Bioinformatics (Oxford, England) · 2024Article
- AMPK Associates with Chromatin and Phosphorylates the TAF-1 Subunit of the Transcription Initiation Complex to Regulate Histone Gene Expression in ALL Cells.Molecular cancer research : MCR · 2023Article
- Hierarchical TAF1-dependent co-translational assembly of the basal transcription factor TFIID.Nature structural & molecular biology · 2023Article
- Deletion of taf1 and taf5 in zebrafish capitulate cardiac and craniofacial abnormalities associated with TAFopathies through perturbations in metabolism.Biology open · 2023Article
- Hierarchical TAF1-dependent co-translational assembly of the basal transcription factor TFIID.bioRxiv : the preprint server for biology · 2023Article
- Kinases on Double Duty: A Review of UniProtKB Annotated Bifunctionality within the Kinome.Biomolecules · 2022Review
- Applications of Pristine and Functionalized Carbon Nanotubes, Graphene, and Graphene Nanoribbons in Biomedicine.Nanomaterials (Basel, Switzerland) · 2021Review
- What do Transcription Factors Interact With?Journal of molecular biology · 2021Review
- Recent insights into the structure of TFIID, its assembly, and its binding to core promoter.Current opinion in structural biology · 2020Review
- Structure and mechanism of the RNA polymerase II transcription machinery.Genes & development · 2020Review
- SVA insertion in X-linked Dystonia Parkinsonism alters histone H3 acetylation associated with TAF1 gene.PloS one · 2020Article
- Neuronal-specific microexon splicing ofRNA biology · 2020Article
- TAF1 plays a critical role in AML1-ETO driven leukemogenesis.Nature communications · 2019Article
- Missense variants in TAF1 and developmental phenotypes: challenges of determining pathogenicity.Human mutation · 2019Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The general transcription factor IID (TFIID) initiates RNA polymerase II-mediated eukaryotic transcription by nucleating pre-initiation complex formation at the core promoter of protein-encoding genes. TAF1, the largest integral subunit of TFIID, contains an evolutionarily conserved yet poorly characterized central core domain, whose specific mutation disrupts cell proliferation in the temperature-sensitive mutant hamster cell line ts13. Although the impaired TAF1 function in the ts13 mutant has been associated with defective transcriptional regulation of cell cycle genes, the mechanism by which TAF1 mediates transcription as part of TFIID remains unclear. Here, we present the crystal structure of the human TAF1 central core domain in complex with another conserved TFIID subunit, TAF7, which biochemically solubilizes TAF1. The TAF1-TAF7 complex displays an inter-digitated compact architecture, featuring an unexpected TAF1 winged helix (WH) domain mounted on top of a heterodimeric triple barrel. The single TAF1 residue altered in the ts13 mutant is buried at the junction of these two structural domains. We show that the TAF1 WH domain has intrinsic DNA-binding activity, which depends on characteristic residues that are commonly used by WH fold proteins for interacting with DNA. Importantly, mutations of these residues not only compromise DNA binding by TAF1, but also abrogate its ability to rescue the ts13 mutant phenotype. Together, our results resolve the structural organization of the TAF1-TAF7 module in TFIID and unveil a critical promoter-binding function of TAF1 in transcription regulation.
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