ArticleThe Journal of biological chemistry2015
Conformational flexibility and subunit arrangement of the modular yeast Spt-Ada-Gcn5 acetyltransferase complex.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- ATAC and SAGA co-activator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct.Cell reports · 2023Article
- Article
- 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
- Article
- Conformational landscape of the yeast SAGA complex as revealed by cryo-EM.Scientific reports · 2022Article
- The Molecular Basis of Spinocerebellar Ataxia Type 7.Frontiers in neuroscience · 2022Review
- Structure of the human SAGA coactivator complex.Nature structural & molecular biology · 2021Article
- SAGA-CORE subunit Spt7 is required for correct Ubp8 localization, chromatin association and deubiquitinase activity.Epigenetics & chromatin · 2020Article
- The SAGA chromatin-modifying complex: the sum of its parts is greater than the whole.Genes & development · 2020Review
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- Article
- Chaperone-mediated ordered assembly of the SAGA and NuA4 transcription co-activator complexes in yeast.Nature communications · 2019Article
- Article
- Characterization of a metazoan ADA acetyltransferase complex.Nucleic acids research · 2019Article
- Share and share alike: the role of Tra1 from the SAGA and NuA4 coactivator complexes.Transcription · 2019Review
- Architecture ofCell discovery · 2019Article
- Distinct requirements of linker DNA and transcriptional activators in promoting SAGA-mediated nucleosome acetylation.The Journal of biological chemistry · 2018Article
- Wheat microbiome bacteria can reduce virulence of a plant pathogenic fungus by altering histone acetylation.Nature communications · 2018Article
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Authors and funding
6 authors.
Funding
Abstract
The Spt-Ada-Gcn5 acetyltransferase (SAGA) complex is a highly conserved, 19-subunit histone acetyltransferase complex that activates transcription through acetylation and deubiquitination of nucleosomal histones in Saccharomyces cerevisiae. Because SAGA has been shown to display conformational variability, we applied gradient fixation to stabilize purified SAGA and systematically analyzed this flexibility using single-particle EM. Our two- and three-dimensional studies show that SAGA adopts three major conformations, and mutations of specific subunits affect the distribution among these. We also located the four functional modules of SAGA using electron microscopy-based labeling and transcriptional activator binding analyses and show that the acetyltransferase module is localized in the most mobile region of the complex. We further comprehensively mapped the subunit interconnectivity of SAGA using cross-linking mass spectrometry, revealing that the Spt and Taf subunits form the structural core of the complex. These results provide the necessary restraints for us to generate a model of the spatial arrangement of all SAGA subunits. According to this model, the chromatin-binding domains of SAGA are all clustered in one face of the complex that is highly flexible. Our results relate information of overall SAGA structure with detailed subunit level interactions, improving our understanding of its architecture and flexibility.
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