Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites.

By B. Czermin, R. Melfi, D. Mccabe, Volker Seitz, A. Imhof, Vincenzo Pirrotta. Cell, 2002

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Enhancer of Zeste is a Polycomb Group protein essential for the establishment and maintenance of repression of homeotic and other genes. In the early embryo it is found in a complex that includes ESC and is recruited to Polycomb Response Elements. We show that this complex contains a methyltransferase activity that methylates lysine 9 and lysine 27 of histone H3, but the activity is lost when the E(Z) SET domain is mutated. The lysine 9 position is trimethylated and this mark is closely associated with Polycomb binding sites on polytene chromosomes but is also found in centric heterochromatin, chromosome 4, and telomeric sites. Histone H3 methylated in vitro by the E(Z)/ESC complex binds specifically to Polycomb protein.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/01c42b59e00da71b86d09aa53d23a8719a2feac6

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Citations in the corpus

EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in maintaining stem cell identity and executing pluripotency. (2008, background): “…2 (EZH2), embryonic ectoderm development (EED), and suppressor of zeste 12 homolog (SUZ12), comprise the core of Polycomb repressive complex 2 (PRC2), which mediates methylation on histone H3 lysine 27 (H3K27) (Cao et al., 2002; Czermin et al., 2002; Kuzmichev et al., 2002; Muller et al., 2002).”
Regulation of MLL1 H3K4 methyltransferase activity by its core components (2006, background): “For example, the E(Z)-family HMTs, specific for H3K27 methylation, have a core-complex organization analogous to that of the MLL1 core complex, and the enzyme is fully active only in the comple”
A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin. (2004, background): “Histone lysine residues can be mono-, di-, or trimethylated (Paik and Kim 1971; DeLange et al. 1973), thereby extending the coding potential of a methylatable lysine position.”
Histone methylation by PRC2 is inhibited by active chromatin marks. (2011, background): “Among the PcG protein complexes, Polycomb repressive complex 2 (PRC2) is a histone methyl-transferase (HMTase) that methylates Lys27 of H3 (H3K27) (Cao et al., 2002; Czermin et al., 2002; Kuzmichev et al., 2004; Müller et al., 2002).”
Variant PRC1 Complex-Dependent H2A Ubiquitylation Drives PRC2 Recruitment and Polycomb Domain Formation (2014, background): “In mammals, the catalytic core of PRC2 is comprised of EZH1 or EZH2, which trimethylate histone H3 on lysine 27 (H3K27me3) (Cao et al., 2002; Czermin et al., 2002; Kuzmichev et al., 2002; Müller et al., 2002).”
Vernalization requires epigenetic silencing of FLC by histone methylation (2004, background): “The ESC-E(Z) Pc-G complex in mammals and flies has been shown to contain histone lysine methyltransferase activity for K27 and possibly K9 of histone H”
Poised chromatin at the ZEB1 promoter enables cell plasticity and enhances tumorigenicity (2013, neutral): “In contrast, trimethylation of lysine 27 (H3K27me3) is often associated with transcriptional repression mediated by the Polycomb group of proteins (Cao et al., 2002; Czermin et al., 2002; Kuzmichev et al., 2002; Muller et al., 2002).”
Bmi1 is essential in Twist1-induced epithelial–mesenchymal transition (2010, background): “Binding of PRC2 to its target genes allows EZH2, a subunit of PRC2, to methylate Lys 27 of histone H3 (H3K27”
Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains. (2003, background): “Furthermore, it has been suggested that the PcG chromodomain protein Polycomb (Pc) could act as a binding module for methyl-Lys 9 and methyl-Lys 27 in the H3 tail, thereby critically mediating the targeting of PcG complexes to different sites of the epigenome (Cao et al. 2002; Czermin et al. 2002; K”