ArticleMolecular and cellular biology2009
The SAGA subunit Ada2 functions in transcriptional silencing.
Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 35 citations in OpenAlex.
- PfGCN5 is essential for Plasmodium falciparum survival and transmission and regulates Pf H2B.Z acetylation and chromatin structure.Nucleic acids research · 2025Article
- Non-canonical chromatin-based functions for the threonine metabolic pathway.Scientific reports · 2024Article
- Increased Agrobacterium-mediated transformation of Saccharomyces cerevisiae after deletion of the yeast ADA2 gene.Letters in applied microbiology · 2022Article
- Metabolic regulation of telomere silencing by SESAME complex-catalyzed H3T11 phosphorylation.Nature communications · 2021Article
- Dynamic modules of the coactivator SAGA in eukaryotic transcription.Experimental & molecular medicine · 2020Review
- The evolutionarily conserved factor Sus1/ENY2 plays a role in telomere length maintenance.Current genetics · 2018Article
- Global reorganization of budding yeast chromosome conformation in different physiological conditions.The Journal of cell biology · 2016Article
- Sgf73, a subunit of SAGA complex, is required for the assembly of RITS complex in fission yeast.Scientific reports · 2015Article
- Acetylome profiling reveals overlap in the regulation of diverse processes by sirtuins, gcn5, and esa1.Molecular & cellular proteomics : MCP · 2015Article
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- The SAGA histone deubiquitinase module controls yeast replicative lifespan via Sir2 interaction.Cell reports · 2014Article
- Sgf29p facilitates the recruitment of TATA box binding protein but does not alter SAGA's global structural integrity in vivo.Biochemistry · 2012Article
- Recruitment of Rpd3 to the telomere depends on the protein arginine methyltransferase Hmt1.PloS one · 2012Article
- The tail-module of yeast Mediator complex is required for telomere heterochromatin maintenance.Nucleic acids research · 2012Article
- Genome-wide H4 K16 acetylation by SAS-I is deposited independently of transcription and histone exchange.Nucleic acids research · 2012Article
- Toward an integrated model of capsule regulation in Cryptococcus neoformans.PLoS pathogens · 2011Article
- Mediator influences telomeric silencing and cellular life span.Molecular and cellular biology · 2011Article
- The implication of Sir2 in replicative aging and senescence in Saccharomyces cerevisiae.Aging · 2011Review
- Distinct regulatory mechanisms of eukaryotic transcriptional activation by SAGA and TFIID.Biochimica et biophysica acta · 2011Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cellular role of the Ada2 coactivator is currently understood in the context of the SAGA histone acetyltransferase (HAT) complex, where Ada2 increases the HAT activity of Gcn5 and interacts with transcriptional activators. Here we report a new function for Ada2 in promoting transcriptional silencing at telomeres and ribosomal DNA. This silencing function is the first characterized role for Ada2 distinct from its involvement with Gcn5. Ada2 binds telomeric chromatin and the silencing protein Sir2 in vivo. Loss of ADA2 causes the spreading of Sir2 and Sir3 into subtelomeric regions and decreased histone H4 K16 acetylation. This previously uncharacterized boundary activity of Ada2 is functionally similar to, but mechanistically distinct from, that of the MYST family HAT Sas2. Mounting evidence in the literature indicates that boundary activities create chromosomal domains important for regulating gene expression in response to environmental changes. Consistent with this, we show that upon nutritional changes, Ada2 occupancy increases at a subtelomeric region proximal to a SAGA-inducible gene and causes derepression of a silenced telomeric reporter gene. Thus, Ada2, likely in the context of SAGA, is positioned at chromosomal termini to participate in both transcriptional repression and activation in response to nutrient signaling.
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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.