ArticleNature structural & molecular biology2025
Single-molecule analysis of transcription activation: dynamics of SAGA coactivator recruitment.
Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Step-brothers in arms, SAGA and ATAC co-activator complexes, use different strategies.The EMBO journal · 2026Review
- Exchange dynamics and kinetic control of gene regulation complexes.Nature reviews. Molecular cell biology · 2026Review
- Nucleosomes and IDRs suppress promiscuous GCN4 binding on minichromosomes.Nature structural & molecular biology · 2026Article
- AID self-assembly and multistranded DNA binding drive synapsis in class switch recombination.Nucleic acids research · 2026Article
- Nascent RNA Folding and RNP Assembly Revealed by Single-molecule Microscopy.Journal of molecular biology · 2026Review
- A mechanism of synergistic Mediator recruitment in RNA polymerase II transcription activation revealed by single-molecule fluorescence.Molecular cell · 2025Article
- Short activation domains control chromatin association of transcription factors.bioRxiv : the preprint server for biology · 2025Article
- Single-molecule analysis of transcription activation: dynamics of SAGA coactivator recruitment.Nature structural & molecular biology · 2025Article
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Abstract
Transcription activators are said to stimulate gene expression by 'recruiting' coactivators, yet this vague term fits multiple kinetic models. To directly analyze the dynamics of activator-coactivator interactions, single-molecule microscopy was used to image promoter DNA, a transcription activator and the Spt-Ada-Gcn5 acetyltransferase (SAGA) complex within yeast nuclear extract. SAGA readily but transiently binds nucleosome-free DNA without an activator, while chromatin association occurs primarily when an activator is present. On both templates, an activator increases SAGA association rates by an order of magnitude and dramatically extends occupancy time. These effects reflect sustained interactions with the transactivation domain, as VP16 or Rap1 activation domains produce different SAGA dynamics. SAGA preferentially associates with templates carrying more than one activator. Unexpectedly, SAGA binding is substantially improved by nucleoside triphosphates but not histone H3 or H4 tail tetra-acetylations. Thus, we observe two modes of SAGA-template interaction: short-lived activator-independent binding to non-nucleosomal DNA and tethering to promoter-bound transcription activators for up to several minutes.
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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.