ArticleThe EMBO journal2014
Architecture of the Saccharomyces cerevisiae SAGA transcription coactivator complex.
Article in The EMBO journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
68 citing papers in PubMed, 114 citations in OpenAlex.
- Insights into the structure and evolution of the human SAGA complex by affinity-ligand purification.Science advances · 2026Article
- Spt7 Deletion Reveals Vulnerabilities inMicroorganisms · 2026Article
- Structure of the transcriptional co-activator SAGA complex, including the histone acetyltransferase module.Molecular cell · 2025Article
- Histone acetyltransferase Gcn5-mediated histone H3 acetylation facilitates cryptococcal morphogenesis and sexual reproduction.mSphere · 2023Article
- SAGA Complex Subunit Hfi1 Is Important in the Stress Response and Pathogenesis ofJournal of fungi (Basel, Switzerland) · 2023Article
- ATAC and SAGA co-activator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct.Cell reports · 2023Article
- ATAC and SAGA coactivator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct.bioRxiv : the preprint server for biology · 2023Article
- The SAGA HAT module is tethered by its SWIRM domain and modulates activity of the SAGA DUB module.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023Article
- Spt3 and Spt8 Are Involved in the Formation of a Silencing Boundary by Interacting with TATA-Binding Protein.Biomolecules · 2023Article
- Involvement of the SAGA and TFIID coactivator complexes in transcriptional dysregulation caused by the separation of core and tail Mediator modules.G3 (Bethesda, Md.) · 2022Article
- Development of Artificial System to Induce Chromatin Loosening inBiomolecules · 2022Article
- SUPT3H-less SAGA coactivator can assemble and function without significantly perturbing RNA polymerase II transcription in mammalian cells.Nucleic acids research · 2022Article
- Conformational landscape of the yeast SAGA complex as revealed by cryo-EM.Scientific reports · 2022Article
- Genome-Wide Regulations of the Preinitiation Complex Formation and Elongating RNA Polymerase II by an E3 Ubiquitin Ligase, San1.Molecular and cellular biology · 2022Article
- Spt20, a Structural Subunit of the SAGA Complex, Regulates Aspergillus fumigatus Biofilm Formation, Asexual Development, and Virulence.Applied and environmental microbiology · 2022Article
- SAGA Complex Subunits inFrontiers in cellular and infection microbiology · 2022Article
- The related coactivator complexes SAGA and ATAC control embryonic stem cell self-renewal through acetyltransferase-independent mechanisms.Cell reports · 2021Article
- Proteomic analysis revealed the roles of YRR1 deletion in enhancing the vanillin resistance of Saccharomyces cerevisiae.Microbial cell factories · 2021Article
- The biochemical and genetic discovery of the SAGA complex.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021Review
- SAGA-CORE subunit Spt7 is required for correct Ubp8 localization, chromatin association and deubiquitinase activity.Epigenetics & chromatin · 2020Article
8 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The conserved transcription coactivator SAGA is comprised of several modules that are involved in activator binding, TBP binding, histone acetylation (HAT) and deubiquitination (DUB). Crosslinking and mass spectrometry, together with genetic and biochemical analyses, were used to determine the molecular architecture of the SAGA-TBP complex. We find that the SAGA Taf and Taf-like subunits form a TFIID-like core complex at the center of SAGA that makes extensive interactions with all other SAGA modules. SAGA-TBP binding involves a network of interactions between subunits Spt3, Spt8, Spt20, and Spt7. The HAT and DUB modules are in close proximity, and the DUB module modestly stimulates HAT function. The large activator-binding subunit Tra1 primarily connects to the TFIID-like core via its FAT domain. These combined results were used to derive a model for the arrangement of the SAGA subunits and its interactions with TBP. Our results provide new insight into SAGA function in gene regulation, its structural similarity with TFIID, and functional interactions between the SAGA modules.
Indexed as
Identifiers
What OpenQuestion holds
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.