ArticleNature structural & molecular biology2022
Acetylation-dependent SAGA complex dimerization promotes nucleosome acetylation and gene transcription.
Article in Nature structural & molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 31 citations in OpenAlex.
- Research progress on lysine acetylation (Review).International journal of molecular medicine · 2026Review
- Multi-Omics Dissection and Functional Validation of Candidate Regulators Modulating Stress Tolerance and Xylose Utilization in the Natural Yeast Strain YB-2625.Journal of fungi (Basel, Switzerland) · 2026Article
- The Transcription Factor FgSge1 Harnesses the SAGA Complex to Activate Mycotoxin Biosynthesis and Fungal Virulence.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Roles of ubiquitin‑specific peptidase 22 in cellular fate: From embryonic survival to tissue repair, inflammation and metabolism (Review).International journal of molecular medicine · 2026Review
- Metformin Impairs Breast Cancer Growth through the Inhibition of PRMT6.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Global profiling of protein complex dynamics with an experimental library of protein interaction markers.Nature biotechnology · 2025Article
- Csn5 Depletion Reverses Mitochondrial Defects in GCN5-NullInternational journal of molecular sciences · 2025Article
- PKA plays a conserved role in regulating gene expression and metabolic adaptation by phosphorylating Rpd3/HDAC1.Nature communications · 2025Article
- PDHX acetylation facilitates tumor progression by disrupting PDC assembly and activating lactylation-mediated gene expression.Protein & cell · 2025Article
- Convallatoxin inhibits proliferation and angiogenesis of glioma cells via regulating JAK/STAT3 pathway.Open life sciences · 2025Article
- Genome-Wide Association Studies on the Kernel Row Number in a Multi-Parent Maize Population.International journal of molecular sciences · 2024Article
- USF2 promotes autophagy and proliferation in chronic lymphocytic leukemia by inhibiting STUB1-induced NFAT5 ubiquitination.Annals of hematology · 2024Article
- SAGA Complex Subunit Hfi1 Is Important in the Stress Response and Pathogenesis ofJournal of fungi (Basel, Switzerland) · 2023Article
- Cla4 phosphorylates histone methyltransferase Set1 to prevent its degradation by the APC/CScience advances · 2023Article
- KDM2B regulates inflammation and oxidative stress of sepsis via targeting NF-κB and AP-1 pathways.Immunity, inflammation and disease · 2023Article
- Glc7/PP1 dephosphorylates histone H3T11 to regulate autophagy and telomere silencing in response to nutrient availability.Cell discovery · 2023Article
- The TORC1 activates Rpd3L complex to deacetylate Ino80 and H2A.Z and repress autophagy.Science advances · 2023Article
- Antisense non-coding transcription represses the PHO5 model gene at the level of promoter chromatin structure.PLoS genetics · 2022Article
- Phosphorylation of Jhd2 by the Ras-cAMP-PKA(Tpk2) pathway regulates histone modifications and autophagy.Nature communications · 2022Article
- Posttranslational regulation of the GCN5 and PCAF acetyltransferases.PLoS genetics · 2022Review
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cells reprogram their transcriptomes to adapt to external conditions. The SAGA (Spt-Ada-Gcn5 acetyltransferase) complex is a highly conserved transcriptional coactivator that plays essential roles in cell growth and development, in part by acetylating histones. Here, we uncover an autoregulatory mechanism of the Saccharomyces cerevisiae SAGA complex in response to environmental changes. Specifically, the SAGA complex acetylates its Ada3 subunit at three sites (lysines 8, 14 and 182) that are dynamically deacetylated by Rpd3. The acetylated Ada3 lysine residues are bound by bromodomains within SAGA subunits Gcn5 and Spt7 that synergistically facilitate formation of SAGA homo-dimers. Ada3-mediated dimerization is enhanced when cells are grown under sucrose or under phosphate-starvation conditions. Once dimerized, SAGA efficiently acetylates nucleosomes, promotes gene transcription and enhances cell resistance to stress. Collectively, our work reveals a mechanism for regulation of SAGA structure and activity and provides insights into how cells adapt to environmental conditions.
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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 Socratic graph.