3IIY

Crystal structure of Eed in complex with a trimethylated histone H1K26 peptide

Summary for 3IIY

• Entry DOI: 10.2210/pdb3iiy/pdb
• Related: 2QXV 3IIW 3IJ0 3IJ1 3IJC
• Descriptor: Polycomb protein EED, Histone H1K26 peptide (3 entities in total)
• Functional Keywords: wd40 domain, alternative initiation, alternative splicing, chromatin regulator, nucleus, phosphoprotein, repressor, transcription, transcription regulation, wd repeat, gene regulation
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: O75530
• Total number of polymer chains: 2
• Total formula weight: 43302.37

Authors

Justin, N.,Sharpe, M.L.,Martin, S.,Taylor, W.R.,De Marco, V.,Gamblin, S.J. (deposition date: 2009-08-03, release date: 2009-09-15, Last modification date: 2024-04-03)

Primary citation

Margueron, R.,Justin, N.,Ohno, K.,Sharpe, M.L.,Son, J.,Drury, W.J.,Voigt, P.,Martin, S.R.,Taylor, W.R.,De Marco, V.,Pirrotta, V.,Reinberg, D.,Gamblin, S.J.
Role of the polycomb protein EED in the propagation of repressive histone marks.
Nature, 461:762-767, 2009

PubMed Abstract: Polycomb group proteins have an essential role in the epigenetic maintenance of repressive chromatin states. The gene-silencing activity of the Polycomb repressive complex 2 (PRC2) depends on its ability to trimethylate lysine 27 of histone H3 (H3K27) by the catalytic SET domain of the EZH2 subunit, and at least two other subunits of the complex: SUZ12 and EED. Here we show that the carboxy-terminal domain of EED specifically binds to histone tails carrying trimethyl-lysine residues associated with repressive chromatin marks, and that this leads to the allosteric activation of the methyltransferase activity of PRC2. Mutations in EED that prevent it from recognizing repressive trimethyl-lysine marks abolish the activation of PRC2 in vitro and, in Drosophila, reduce global methylation and disrupt development. These findings suggest a model for the propagation of the H3K27me3 mark that accounts for the maintenance of repressive chromatin domains and for the transmission of a histone modification from mother to daughter cells.

PubMed: 19767730
DOI: 10.1038/nature08398

Experimental method

X-RAY DIFFRACTION (2.65 Å)