ArticleProceedings of the National Academy of Sciences of the United States of America2018
Structural basis for activation of SAGA histone acetyltransferase Gcn5 by partner subunit Ada2.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 58 citations in OpenAlex.
- GCN5 and TADA2B constitutively regulate XRCC1 function during DNA repair to maintain cell survival.Cell death and differentiation · 2026Article
- Transcriptional adapter ADA2 regulates yield and end-use quality through liquid-liquid phase separation in wheat.Journal of integrative plant biology · 2026Article
- A role for the poly-asparagine repeat in the Plasmodium histone acetyltransferase, PfGCN5.Nature communications · 2026Article
- Deficiency of GCN5 exacerbates pulmonary fibrosis by disrupting the LKB1-AMPK pathway.Cell communication and signaling : CCS · 2026Article
- Structure of the transcriptional co-activator SAGA complex, including the histone acetyltransferase module.Molecular cell · 2025Article
- Article
- Optogenetic Control of Phosphate-Responsive Genes Using Single-Component Fusion Proteins inACS synthetic biology · 2024Article
- Optogenetic control of phosphate-responsive genes using single component fusion proteins inbioRxiv : the preprint server for biology · 2024Article
- The SAGA acetyltransferase module is required for the maintenance of MAF and MYC oncogenic gene expression programs in multiple myeloma.Genes & development · 2024Article
- The SAGA acetyltransferase module is required for the maintenance of MAF and MYC oncogenic gene expression programs in multiple myeloma.bioRxiv : the preprint server for biology · 2024Article
- Lysine acetylation of histone acetyltransferase adaptor protein ADA2 is a mechanism of metabolic control of chromatin modification in plants.Nature plants · 2024Article
- Article
- SAGA Complex Subunit Hfi1 Is Important in the Stress Response and Pathogenesis ofJournal of fungi (Basel, Switzerland) · 2023Article
- The multifaceted roles of Myb domain-containing proteins in apicomplexan parasites.Current opinion in microbiology · 2023Review
- Advances in direct detection of lysine methylation and acetylation by nuclear magnetic resonance usingMethods (San Diego, Calif.) · 2023Article
- Conformation-specific Synthetic Antibodies Discriminate Multiple Functional States of the Ion Channel CorA.Journal of molecular biology · 2023Article
- SUB1A-1 anchors a regulatory cascade for epigenetic and transcriptional controls of submergence tolerance in rice.PNAS nexus · 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
- Overcoming the Limitations of CRISPR-Cas9 Systems inMicroorganisms · 2023Review
- Posttranslational regulation of the GCN5 and PCAF acetyltransferases.PLoS genetics · 2022Review
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
The Gcn5 histone acetyltransferase (HAT) subunit of the SAGA transcriptional coactivator complex catalyzes acetylation of histone H3 and H2B N-terminal tails, posttranslational modifications associated with gene activation. Binding of the SAGA subunit partner Ada2 to Gcn5 activates Gcn5's intrinsically weak HAT activity on histone proteins, but the mechanism for this activation by the Ada2 SANT domain has remained elusive. We have employed Fab antibody fragments as crystallization chaperones to determine crystal structures of a yeast Ada2/Gcn5 complex. Our structural and biochemical results indicate that the Ada2 SANT domain does not activate Gcn5's activity by directly affecting histone peptide binding as previously proposed. Instead, the Ada2 SANT domain enhances Gcn5 binding of the enzymatic cosubstrate acetyl-CoA. This finding suggests a mechanism for regulating chromatin modification enzyme activity: controlling binding of the modification cosubstrate instead of the histone substrate.
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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.