ArticleScientific reports2019
The EZH2 SANT1 domain is a histone reader providing sensitivity to the modification state of the H4 tail.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- The conserved N-terminal SANT1-binding domain (SBD) of EZH2 regulates PRC2 activity.Genes & development · 2026Article
- From Overgrowth to Complex Malformations: A NovelChildren (Basel, Switzerland) · 2025Article
- Multiple transactivation domains of EZH2 bind to the TAZ2 domain of p300 and stimulate the acetyltransferase function of p300.The Biochemical journal · 2025Article
- The SAGA acetyltransferase module is required for the maintenance of MAF and MYC oncogenic gene expression programs in multiple myeloma.Genes & development · 2024Article
- Article
- The SAGA acetyltransferase module is required for the maintenance of MAF and MYC oncogenic gene expression programs in multiple myeloma.bioRxiv : the preprint server for biology · 2024Article
- Regulation of fungal raw-starch-degrading enzyme production depends on transcription factor phosphorylation and recruitment of the Mediator complex.Communications biology · 2023Article
- Survivin prevents the polycomb repressor complex 2 from methylating histone 3 lysine 27.iScience · 2023Article
- ImitateDB: A database for domain and motif mimicry incorporating host and pathogen protein interactions.Amino acids · 2022Article
- The molecular principles of gene regulation by Polycomb repressive complexes.Nature reviews. Molecular cell biology · 2021Review
- Noncanonical Functions of the Polycomb Group Protein EZH2 in Breast Cancer.The American journal of pathology · 2021Review
- Characterization of functional disordered regions within chromatin-associated proteins.iScience · 2021Review
- Profile of Basal Cell Carcinoma Mutations and Copy Number Alterations - Focus on Gene-Associated Noncoding Variants.Frontiers in oncology · 2021Article
- A partially disordered region connects gene repression and activation functions of EZH2.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Dynamic Competition of Polycomb and Trithorax in Transcriptional Programming.Annual review of biochemistry · 2020Review
- Engaging chromatin: PRC2 structure meets function.British journal of cancer · 2020Review
- Loss of SIRT4 promotes the self-renewal of Breast Cancer Stem Cells.Theranostics · 2020Article
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7 authors at 2 institutions in 1 country.
Funding
Abstract
SANT domains are found in a number of chromatin regulators. They contain approximately 50 amino acids and have high similarity to the DNA binding domain of Myb related proteins. Though some SANT domains associate with DNA others have been found to bind unmodified histone tails. There are two SANT domains in Enhancer of Zeste 2 (EZH2), the catalytic subunit of the Polycomb Repressive Complex 2 (PRC2), of unknown function. Here we show that the first SANT domain (SANT1) of EZH2 is a histone binding domain with specificity for the histone H4 N-terminal tail. Using NMR spectroscopy, mutagenesis, and molecular modeling we structurally characterize the SANT1 domain and determine the molecular mechanism of binding to the H4 tail. Though not important for histone binding, we find that the adjacent stimulation response motif (SRM) stabilizes SANT1 and transiently samples its active form in solution. Acetylation of H4K16 (H4K16ac) or acetylation or methylation of H4K20 (H4K20ac and H4K20me3) are seen to abrogate binding of SANT1 to H4, which is consistent with these modifications being anti-correlated with H3K27me3 in-vivo. Our results provide significant insight into this important regulatory region of EZH2 and the first characterization of the molecular mechanism of SANT domain histone binding.
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