ArticleNature communications2018
Structural insights into the π-π-π stacking mechanism and DNA-binding activity of the YEATS domain.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
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Who cites it
42 citing papers in PubMed, 34 citations in OpenAlex.
- Distinct roles of the JADE and BRPF scaffolding subunits of the acetyltransferase HBO1 complex.Nature communications · 2026Article
- Coming to light: the transcriptional regulatory roles of histone lysine crotonylation in health and disease.Cellular & molecular biology letters · 2026Review
- Histone modification cross-talk: analytical tools and molecular mechanisms.The Biochemical journal · 2026Review
- A SWI/SNF-specific Ig-like domain, SWIFT, is a transcription factor binding platform.Science (New York, N.Y.) · 2026Article
- HP1γ self-assembles and cooperates with KAP1 in repression of long noncoding RNA AI662270 in ESCs.Cell reports · 2026Article
- Recruitment of BRD4 to the ASXL1 genomic targets depends on the extra-terminal domain of BRD4.Nature communications · 2026Article
- Metabolite-driven protein modifications in immune signaling: from established principles to emerging pyruvylation.Frontiers in immunology · 2026Review
- Discovery and Development of a Small-Molecule Inhibitor Targeting the GAS41 YEATS Domain in Nonsmall Cell Lung Cancer.Journal of medicinal chemistry · 2025Article
- Mechanistic insights into histone recognition and H3K14 acetylation by the NuA3 histone acetyltransferase complex.Nature communications · 2025Article
- Advancing Genetically Encoded Lysine (GEK) Chemistry: From Precision Modulation to Therapeutic Innovation.Accounts of chemical research · 2025Review
- The YEATS domain is a selective reader of histone methacrylation.Structure (London, England : 1993) · 2025Article
- Cracking Lysine Crotonylation (Kcr): Enlightening a Promising Post-Translational Modification.Chembiochem : a European journal of chemical biology · 2025Review
- Modelling protein-protein interactions for the design of vaccine chimeric antigens with protective epitopes.PloS one · 2025Article
- Development of Xanthoangelol-Derived Compounds with Membrane-Disrupting Effects against Gram-Positive Bacteria.Antibiotics (Basel, Switzerland) · 2024Article
- Post-translational modification-dependent oligomerization switch in regulation of global transcription and DNA damage repair during genotoxic stress.Nature communications · 2024Article
- Unveiling the role of GAS41 in cancer progression.Cancer cell international · 2023Review
- BcTaf14 regulates growth and development, virulence, and stress responses in the phytopathogenic fungus Botrytis cinerea.Molecular plant pathology · 2023Article
- YEATS2 regulates the activation of TAK1/NF-κB pathway and is critical for pancreatic ductal adenocarcinoma cell survival.Cell biology and toxicology · 2023Article
- Conformational and Thermodynamic Differences Underlying Wild-Type and Mutant Eleven-Nineteen-Leukemia YEATS Domain Specificity for Epigenetic Marks.Journal of chemical information and modeling · 2023Article
- Engaging with benzoyllysine through a π-π-π mechanism.Current opinion in chemical biology · 2023Review
Corrections and comments
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Authors and funding
15 authors at 6 institutions in 2 countries.
Funding
Abstract
The YEATS domain has been identified as a reader of histone acylation and more recently emerged as a promising anti-cancer therapeutic target. Here, we detail the structural mechanisms for π-π-π stacking involving the YEATS domains of yeast Taf14 and human AF9 and acylated histone H3 peptides and explore DNA-binding activities of these domains. Taf14-YEATS selects for crotonyllysine, forming π stacking with both the crotonyl amide and the alkene moiety, whereas AF9-YEATS exhibits comparable affinities to saturated and unsaturated acyllysines, engaging them through π stacking with the acyl amide. Importantly, AF9-YEATS is capable of binding to DNA, whereas Taf14-YEATS is not. Using a structure-guided approach, we engineered a mutant of Taf14-YEATS that engages crotonyllysine through the aromatic-aliphatic-aromatic π stacking and shows high selectivity for the crotonyl H3K9 modification. Our findings shed light on the molecular principles underlying recognition of acyllysine marks and reveal a previously unidentified DNA-binding activity of AF9-YEATS.
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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.