 |
PDBsum entry 3ij0
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Gene regulation
|
PDB id
|
|
|
|
3ij0
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Role of the polycomb protein eed in the propagation of repressive histone marks.
|
|
|
Authors
|
|
R.Margueron,
N.Justin,
K.Ohno,
M.L.Sharpe,
J.Son,
W.J.Drury,
P.Voigt,
S.R.Martin,
W.R.Taylor,
V.De marco,
V.Pirrotta,
D.Reinberg,
S.J.Gamblin.
|
|
|
Ref.
|
|
Nature, 2009,
461,
762-767.
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
