ArticleThe EMBO journal2002
Mapping histone fold TAFs within yeast TFIID.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 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
54 citing papers in PubMed, 104 citations in OpenAlex.
- The SAGA chromatin-modifying complex: the sum of its parts is greater than the whole.Genes & development · 2020Review
- The Structures of Eukaryotic Transcription Pre-initiation Complexes and Their Functional Implications.Sub-cellular biochemistry · 2019Review
- Structure of human TFIID and mechanism of TBP loading onto promoter DNA.Science (New York, N.Y.) · 2018Article
- Molecular structure of promoter-bound yeast TFIID.Nature communications · 2018Article
- Towards a mechanistic understanding of core promoter recognition from cryo-EM studies of human TFIID.Current opinion in structural biology · 2017Review
- Article
- The TAF10-containing TFIID and SAGA transcriptional complexes are dispensable for early somitogenesis in the mouse embryo.Development (Cambridge, England) · 2017Article
- Transcription of Nearly All Yeast RNA Polymerase II-Transcribed Genes Is Dependent on Transcription Factor TFIID.Molecular cell · 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
- Structural dynamics and DNA interaction of human TFIID.Transcription · 2017Article
- 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
- Zooming in on Transcription Preinitiation.Journal of molecular biology · 2016Review
- Article
- TAF10 Interacts with the GATA1 Transcription Factor and Controls Mouse Erythropoiesis.Molecular and cellular biology · 2015Article
- Structural basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2015Review
- dTAF10- and dTAF10b-Containing Complexes Are Required for Ecdysone-Driven Larval-Pupal Morphogenesis in Drosophila melanogaster.PloS one · 2015Article
- Structural and functional insight into TAF1-TAF7, a subcomplex of transcription factor II D.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Direct TFIIA-TFIID protein contacts drive budding yeast ribosomal protein gene transcription.The Journal of biological chemistry · 2013Article
- Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The transcription factor TFIID is a large multiprotein complex, composed of the TATA box-binding protein (TBP) and 14 TBP-associated factors (TAFs), which plays a key role in the regulation of gene expression by RNA polymerase II. The three-dimensional structure of yeast (y) TFIID, determined at approximately 3 nm resolution by electron microscopy and image analysis, resembles a molecular clamp formed by three major lobes connected by thin linking domains. The yTFIID is structurally similar to the human factor although the clamp appears more closed in the yeast complex, probably reflecting the conformational flexibility of the structure. Immunolabelling experiments showed that nine TAFs that contain the histone fold structural motif were located in three distinct substructures of TFIID. The distribution of these TAFs showed that the previously reported pair-wise interactions between histone fold domain (HFD)-containing TAFs are likely to occur in the native yTFIID complex. Most of the HFD-containing TAFs have been found in two distinct lobes, thus revealing an unexpected and novel molecular organization of TFIID.
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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.