ArticleMolecular systems biology2011
Combinatorial depletion analysis to assemble the network architecture of the SAGA and ADA chromatin remodeling complexes.
Article in Molecular systems biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.
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Who cites it
99 citing papers in PubMed.
- Structure of the transcriptional co-activator SAGA complex, including the histone acetyltransferase module.Molecular cell · 2025Article
- Leveraging synthetic genetic array screening to identify therapeutic targets and inhibitors for combatting azole resistance inMicrobiology spectrum · 2025Article
- Integrative approaches for predicting protein network perturbations through machine learning and structural characterization.Journal of proteomics · 2025Article
- ATAC and SAGA histone acetyltransferase modules facilitate transcription factor binding to nucleosomes independent of their acetylation activity.Nucleic acids research · 2025Article
- The transcription factor CAMTA2 interacts with the histone acetyltransferase GCN5 and regulates grain weight in wheat.The Plant cell · 2024Article
- UPS writes a new saga of SAGA.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023Review
- 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
- Article
- 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
- Conserved and plant-specific histone acetyltransferase complexes cooperate to regulate gene transcription and plant development.Nature plants · 2023Article
- Adaptive partitioning of a gene locus to the nuclear envelope in Saccharomyces cerevisiae is driven by polymer-polymer phase separation.Nature communications · 2023Article
- Histone H2Bub dynamics in the 5' region of active genes are tightly linked to the UV-induced transcriptional response.Computational and structural biotechnology journal · 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
- Posttranslational regulation of the GCN5 and PCAF acetyltransferases.PLoS genetics · 2022Review
- 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
- Acetylation-dependent SAGA complex dimerization promotes nucleosome acetylation and gene transcription.Nature structural & molecular biology · 2022Article
- Deubiquitinases in Neurodegeneration.Cells · 2022Review
39 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors.
Funding
Abstract
Despite the availability of several large-scale proteomics studies aiming to identify protein interactions on a global scale, little is known about how proteins interact and are organized within macromolecular complexes. Here, we describe a technique that consists of a combination of biochemistry approaches, quantitative proteomics and computational methods using wild-type and deletion strains to investigate the organization of proteins within macromolecular protein complexes. We applied this technique to determine the organization of two well-studied complexes, Spt-Ada-Gcn5 histone acetyltransferase (SAGA) and ADA, for which no comprehensive high-resolution structures exist. This approach revealed that SAGA/ADA is composed of five distinct functional modules, which can persist separately. Furthermore, we identified a novel subunit of the ADA complex, termed Ahc2, and characterized Sgf29 as an ADA family protein present in all Gcn5 histone acetyltransferase complexes. Finally, we propose a model for the architecture of the SAGA and ADA complexes, which predicts novel functional associations within the SAGA complex and provides mechanistic insights into phenotypical observations in SAGA mutants.
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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.