ArticleMolecular and cellular biology2007
The N terminus of Drosophila ESC binds directly to histone H3 and is required for E(Z)-dependent trimethylation of H3 lysine 27.
Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
- Article
- Recurrent innovation of protein-protein interactions in the Drosophila piRNA pathway.The EMBO journal · 2026Article
- Epigenetic Regulation by Polycomb Complexes from Drosophila to Human and Its Relation to Communicable Disease Pathogenesis.International journal of molecular sciences · 2022Review
- Review
- Epigenetic regulation of drosophila germline stem cell maintenance and differentiation.Developmental biology · 2021Review
- Epigenetics and beyond: targeting writers of protein lysine methylation to treat disease.Nature reviews. Drug discovery · 2021Review
- Ezh1 arises from Ezh2 gene duplication but its function is not required for zebrafish development.Scientific reports · 2019Article
- Structure, mechanism, and regulation of polycomb-repressive complex 2.The Journal of biological chemistry · 2018Review
- Polycomb and Trithorax Group Genes inGenetics · 2017Review
- Deletion of the Polycomb-Group Protein EZH2 Leads to Compromised Self-Renewal and Differentiation Defects in Human Embryonic Stem Cells.Cell reports · 2016Article
- Stuxnet Facilitates the Degradation of Polycomb Protein during Development.Developmental cell · 2016Article
- Polycomb repressive complex 2 structure with inhibitor reveals a mechanism of activation and drug resistance.Nature communications · 2016Article
- Homodimeric PHD Domain-containing Rco1 Subunit Constitutes a Critical Interaction Hub within the Rpd3S Histone Deacetylase Complex.The Journal of biological chemistry · 2016Article
- Polycomb inhibits histone acetylation by CBP by binding directly to its catalytic domain.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Targeting histone methyltransferases and demethylases in clinical trials for cancer therapy.Clinical epigenetics · 2016Review
- Towards understanding methyllysine readout.Biochimica et biophysica acta · 2014Review
- Histone target selection within chromatin: an exemplary case of teamwork.Genes & development · 2014Review
- EZH2: biology, disease, and structure-based drug discovery.Acta pharmacologica Sinica · 2014Review
- Nucleosome-binding activities within JARID2 and EZH1 regulate the function of PRC2 on chromatin.Genes & development · 2013Article
- Polycomb silencing of the Drosophila 4E-BP gene regulates imaginal disc cell growth.Developmental biology · 2013Article
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4 authors.
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Abstract
Polycomb group proteins mediate heritable transcriptional silencing and function through multiprotein complexes that methylate and ubiquitinate histones. The 600-kDa E(Z)/ESC complex, also known as Polycomb repressive complex 2 (PRC2), specifically methylates histone H3 lysine 27 (H3 K27) through the intrinsic histone methyltransferase (HMTase) activity of the E(Z) SET domain. By itself, E(Z) exhibits no detectable HMTase activity and requires ESC for methylation of H3 K27. The molecular basis for this requirement is unknown. ESC binds directly, via its C-terminal WD repeats (beta-propeller domain), to E(Z). Here, we show that the N-terminal region of ESC that precedes its beta-propeller domain interacts directly with histone H3, thereby physically linking E(Z) to its substrate. We show that when expressed in stable S2 cell lines, an N-terminally truncated ESC (FLAG-ESC61-425), like full-length ESC, is incorporated into complexes with E(Z) and binds to a Ubx Polycomb response element in a chromatin immunoprecipitation assay. However, incorporation of this N-terminally truncated ESC into E(Z) complexes prevents trimethylation of histone H3 by E(Z). We also show that a closely related Drosophila melanogaster paralog of ESC, ESC-like (ESCL), and the mammalian homolog of ESC, EED, also interact with histone H3 via their N termini, indicating that the interaction of ESC with histone H3 is evolutionarily conserved, reflecting its functional importance. Our data suggest that one of the roles of ESC (and ESCL and EED) in PRC2 complexes is to enable E(Z) to utilize histone H3 as a substrate by physically linking enzyme and substrate.
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