ArticleProceedings of the National Academy of Sciences of the United States of America2014
A sequence-specific transcription activator motif and powerful synthetic variants that bind Mediator using a fuzzy protein interface.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed.
- A transcription factor by any other name - function beyond DNA binding and transactivation.EMBO reports · 2026Review
- Mediator Tail Subunits Hierarchically Couple Transcriptional Condensates to Gene Activation and Genome Organization.bioRxiv : the preprint server for biology · 2026Article
- Evolutionary turnover of key amino acids explains conservation of function without conservation of sequence in transcriptional activation domains.PLoS genetics · 2026Article
- Combinatorial protein engineering identifies potent CRISPR activators with reduced toxicity.Nature communications · 2025Article
- FINCHES: A Computational Framework for Predicting Intermolecular Interactions in Intrinsically Disordered Proteins.International journal of molecular sciences · 2025Review
- Hierarchy in regulator interactions with distant transcriptional activation domains empowers rheostatic regulation.Protein science : a publication of the Protein Society · 2025Article
- Toward universal models for collective interactions in biomolecular condensates.Biophysics reviews · 2025Article
- Boosting transcriptional activities by employing repeated activation domains in transcription factors.The Plant cell · 2025Article
- Fuzzy protein-DNA interactions and beyond: A common theme in transcription?Current opinion in structural biology · 2024Review
- Article
- High-throughput affinity measurements of direct interactions between activation domains and co-activators.bioRxiv : the preprint server for biology · 2024Article
- Fuzzy recognition by the prokaryotic transcription factor HigA2 from Vibrio cholerae.Nature communications · 2024Article
- Commonly asked questions about transcriptional activation domains.Current opinion in structural biology · 2024Review
- Molecular switching in transcription through splicing and proline-isomerization regulates stress responses in plants.Nature communications · 2024Article
- Rational optimization of a transcription factor activation domain inhibitor.Nature structural & molecular biology · 2023Article
- Clusters of acidic and hydrophobic residues can predict acidic transcriptional activation domains from protein sequence.Genetics · 2023Article
- Ancient transcriptional regulators can easily evolve new pair-wise cooperativity.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Transcription factor clusters enable target search but do not contribute to target gene activation.Nucleic acids research · 2023Article
- Interaction modules that impart specificity to disordered protein.Trends in biochemical sciences · 2023Review
- Molecular insights into alginate β-lactoglobulin A multivalencies-The foundation for their amorphous aggregates and coacervation.Protein science : a publication of the Protein Society · 2023Article
5 more citing papers are in PubMed but not listed here.
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5 authors.
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Abstract
Although many transcription activators contact the same set of coactivator complexes, the mechanism and specificity of these interactions have been unclear. For example, do intrinsically disordered transcription activation domains (ADs) use sequence-specific motifs, or do ADs of seemingly different sequence have common properties that encode activation function? We find that the central activation domain (cAD) of the yeast activator Gcn4 functions through a short, conserved sequence-specific motif. Optimizing the residues surrounding this short motif by inserting additional hydrophobic residues creates very powerful ADs that bind the Mediator subunit Gal11/Med15 with high affinity via a "fuzzy" protein interface. In contrast to Gcn4, the activity of these synthetic ADs is not strongly dependent on any one residue of the AD, and this redundancy is similar to that of some natural ADs in which few if any sequence-specific residues have been identified. The additional hydrophobic residues in the synthetic ADs likely allow multiple faces of the AD helix to interact with the Gal11 activator-binding domain, effectively forming a fuzzier interface than that of the wild-type cAD.
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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.