ArticleThe Journal of biological chemistry2018
Distinct requirements of linker DNA and transcriptional activators in promoting SAGA-mediated nucleosome acetylation.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 12 citations in OpenAlex.
- Step-brothers in arms, SAGA and ATAC co-activator complexes, use different strategies.The EMBO journal · 2026Review
- Single-molecule analysis of transcription activation: dynamics of SAGA coactivator recruitment.Nature structural & molecular biology · 2025Article
- ATAC and SAGA histone acetyltransferase modules facilitate transcription factor binding to nucleosomes independent of their acetylation activity.Nucleic acids research · 2025Article
- Acetylation-dependent SAGA complex dimerization promotes nucleosome acetylation and gene transcription.Nature structural & molecular biology · 2022Article
- The SAGA core module is critical during Drosophila oogenesis and is broadly recruited to promoters.PLoS genetics · 2021Article
- Mechanisms of stimulation of SAGA-mediated nucleosome acetylation by a transcriptional activator.Biochemistry and biophysics reports · 2021Article
- The Ada2/Ada3/Gcn5/Sgf29 histone acetyltransferase module.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021Review
- Catalysis by protein acetyltransferase Gcn5.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021Review
- Article
- The Role of VP16 in the Life Cycle of Alphaherpesviruses.Frontiers in microbiology · 2020Review
- SAGA and SAGA-like SLIK transcriptional coactivators are structurally and biochemically equivalent.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Spt-Ada-Gcn5 acetyltransferase (SAGA) family of transcriptional coactivators are prototypical nucleosome acetyltransferase complexes that regulate multiple steps in gene transcription. The size and complexity of both the SAGA enzyme and the chromatin substrate provide numerous opportunities for regulating the acetylation process. To better probe this regulation, here we developed a bead-based nucleosome acetylation assay to characterize the binding interactions and kinetics of acetylation with different nucleosomal substrates and the full SAGA complex purified from budding yeast (
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