ArticleProceedings of the National Academy of Sciences of the United States of America2014
Structural and functional insight into TAF1-TAF7, a subcomplex of transcription factor II D.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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.
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Who cites it
30 citing papers in PubMed, 47 citations in OpenAlex.
- Epigenetic mechanisms of inflammatory memory in the central nervous system.Nature immunology · 2026Review
- Histone modification cross-talk: analytical tools and molecular mechanisms.The Biochemical journal · 2026Review
- 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
- The KASH protein UNC-83 differentially regulates kinesin-1 activity to control developmental stage-specific nuclear migration.Current biology : CB · 2025Article
- Harnessing the TAF1 Acetyltransferase for Targeted Acetylation of the Tumor Suppressor p53.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- LncR-GAS5 decrease in adenine phosphoribosyltransferase expresssion via binding TAF1 to increase kidney damage created by CIH.Heliyon · 2024Article
- Ino2, activator of yeast phospholipid biosynthetic genes, interacts with basal transcription factors TFIIA and Bdf1.Current genetics · 2023Article
- 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
- Genome-Wide Acetylation Modification of H3K27ac in Bovine Rumen Cell Following Butyrate Exposure.Biomolecules · 2023Article
- Pseudo-chromosome-length genome assembly for a deep-sea eel Ilyophis brunneus sheds light on the deep-sea adaptation.Science China. Life sciences · 2023Article
- What do Transcription Factors Interact With?Journal of molecular biology · 2021Review
- Structure and mechanism of the RNA polymerase II transcription machinery.Genes & development · 2020Review
- Recent insights into the structure of TFIID, its assembly, and its binding to core promoter.Current opinion in structural biology · 2020Review
- Prediction of tumor location in prostate cancer tissue using a machine learning system on gene expression data.BMC bioinformatics · 2020Article
- Neuronal-specific microexon splicing ofRNA biology · 2020Article
- TAF1 plays a critical role in AML1-ETO driven leukemogenesis.Nature communications · 2019Article
- Epigenetics and transcription regulation during eukaryotic diversification: the saga of TFIID.Genes & development · 2019Article
- On the problem of confounders in modeling gene expression.Bioinformatics (Oxford, England) · 2019Review
- Molecular structure of promoter-bound yeast TFIID.Nature communications · 2018Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 1 country.
Funding
Abstract
Transcription factor II D (TFIID) is a multiprotein complex that nucleates formation of the basal transcription machinery. TATA binding protein-associated factors 1 and 7 (TAF1 and TAF7), two subunits of TFIID, are integral to the regulation of eukaryotic transcription initiation and play key roles in preinitiation complex (PIC) assembly. Current models suggest that TAF7 acts as a dissociable inhibitor of TAF1 histone acetyltransferase activity and that this event ensures appropriate assembly of the RNA polymerase II-mediated PIC before transcriptional initiation. Here, we report the 3D structure of a complex of yeast TAF1 with TAF7 at 2.9 Å resolution. The structure displays novel architecture and is characterized by a large predominantly hydrophobic heterodimer interface and extensive cofolding of TAF subunits. There are no obvious similarities between TAF1 and known histone acetyltransferases. Instead, the surface of the TAF1-TAF7 complex contains two prominent conserved surface pockets, one of which binds selectively to an inhibitory trimethylated histone H3 mark on Lys27 in a manner that is also regulated by phosphorylation at the neighboring H3 serine. Our findings could point toward novel roles for the TAF1-TAF7 complex in regulation of PIC assembly via reading epigenetic histone marks.
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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.