 |
PDBsum entry 3kqi
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Nuclear protein
|
PDB id
|
|
|
|
3kqi
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Recognition of histone h3k4 trimethylation by the plant homeodomain of phf2 modulates histone demethylation.
|
|
|
Authors
|
|
H.Wen,
J.Li,
T.Song,
M.Lu,
P.Y.Kan,
M.G.Lee,
B.Sha,
X.Shi.
|
|
|
Ref.
|
|
J Biol Chem, 2010,
285,
9322-9326.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Distinct lysine methylation marks on histones create dynamic signatures
deciphered by the "effector" modules, although the underlying mechanisms remain
unclear. We identified the plant homeodomain- and Jumonji C domain-containing
protein PHF2 as a novel histone H3K9 demethylase. We show in biochemical and
crystallographic analyses that PHF2 recognizes histone H3K4 trimethylation
through its plant homeodomain finger and that this interaction is essential for
PHF2 occupancy and H3K9 demethylation at rDNA promoters. Our study provides
molecular insights into the mechanism by which distinct effector domains within
a protein cooperatively modulate the "cross-talk" of histone modifications.
|
|
|
|
|
|
|
