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* Residue conservation analysis
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PDB id:
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Gene regulation
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Title:
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Crystal structure of the chromo domain of human mrg15
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Structure:
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Mortality factor 4-like protein 1. Chain: a, b, c, d, e, f. Fragment: chromo domain. Synonym: morf-related gene 15 isoform 1. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: morf4l1, mrg15, fwp006, hspc008, hspc061, pp368. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Biol. unit:
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Trimer (from
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Resolution:
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2.20Å
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R-factor:
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0.227
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R-free:
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0.273
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Authors:
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P.Zhang,J.Du,J.Ding
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Key ref:
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P.Zhang
et al.
(2006).
Structure of human MRG15 chromo domain and its binding to Lys36-methylated histone H3.
Nucleic Acids Res,
34,
6621-6628.
PubMed id:
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Date:
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26-Nov-05
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Release date:
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14-Nov-06
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PROCHECK
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Headers
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References
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Enzyme class:
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Chains A, B, C, D, E, F:
E.C.?
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Nucleic Acids Res
34:6621-6628
(2006)
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PubMed id:
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Structure of human MRG15 chromo domain and its binding to Lys36-methylated histone H3.
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P.Zhang,
J.Du,
B.Sun,
X.Dong,
G.Xu,
J.Zhou,
Q.Huang,
Q.Liu,
Q.Hao,
J.Ding.
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ABSTRACT
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Human MRG15 is a transcription factor that plays a vital role in embryonic
development, cell proliferation and cellular senescence. It comprises a putative
chromo domain in the N-terminal part that has been shown to participate in
chromatin remodeling and transcription regulation. We report here the crystal
structure of human MRG15 chromo domain at 2.2 A resolution. The MRG15 chromo
domain consists of a beta-barrel and a long alpha-helix and assumes a structure
more similar to the Drosophila MOF chromo barrel domain than the typical HP1/Pc
chromo domains. The beta-barrel core contains a hydrophobic pocket formed by
three conserved aromatic residues Tyr26, Tyr46 and Trp49 as a potential binding
site for a modified residue of histone tail. However, the binding groove for the
histone tail seen in the HP1/Pc chromo domains is pre-occupied by an extra
beta-strand. In vitro binding assay results indicate that the MRG15 chromo
domain can bind to methylated Lys36, but not methylated Lys4, Lys9 and Lys27 of
histone H3. These data together suggest that the MRG15 chromo domain may
function as an adaptor module which can bind to a modified histone H3 in a mode
different from that of the HP1/Pc chromo domains.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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C.A.Musselman,
M.E.Lalonde,
J.Côté,
and
T.G.Kutateladze
(2012).
Perceiving the epigenetic landscape through histone readers.
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Nat Struct Mol Biol,
19,
1218-1227.
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E.L.Greer,
and
Y.Shi
(2012).
Histone methylation: a dynamic mark in health, disease and inheritance.
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Nat Rev Genet,
13,
343-357.
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L.Xie,
C.Pelz,
W.Wang,
A.Bashar,
O.Varlamova,
S.Shadle,
and
S.Impey
(2011).
KDM5B regulates embryonic stem cell self-renewal and represses cryptic intragenic transcription.
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EMBO J,
30,
1473-1484.
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T.Ma,
J.A.Keller,
and
X.Yu
(2011).
RNF8-dependent histone ubiquitination during DNA damage response and spermatogenesis.
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Acta Biochim Biophys Sin (Shanghai),
43,
339-345.
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A.Rechtsteiner,
S.Ercan,
T.Takasaki,
T.M.Phippen,
T.A.Egelhofer,
W.Wang,
H.Kimura,
J.D.Lieb,
and
S.Strome
(2010).
The histone H3K36 methyltransferase MES-4 acts epigenetically to transmit the memory of germline gene expression to progeny.
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PLoS Genet,
6,
0.
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G.J.Filion,
J.G.van Bemmel,
U.Braunschweig,
W.Talhout,
J.Kind,
L.D.Ward,
W.Brugman,
I.J.de Castro,
R.M.Kerkhoven,
H.J.Bussemaker,
and
B.van Steensel
(2010).
Systematic protein location mapping reveals five principal chromatin types in Drosophila cells.
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Cell,
143,
212-224.
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K.L.Yap,
and
M.M.Zhou
(2010).
Keeping it in the family: diverse histone recognition by conserved structural folds.
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Crit Rev Biochem Mol Biol,
45,
488-505.
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K.Nimura,
K.Ura,
and
Y.Kaneda
(2010).
Histone methyltransferases: regulation of transcription and contribution to human disease.
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J Mol Med,
88,
1213-1220.
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R.F.Luco,
Q.Pan,
K.Tominaga,
B.J.Blencowe,
O.M.Pereira-Smith,
and
T.Misteli
(2010).
Regulation of alternative splicing by histone modifications.
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Science,
327,
996.
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D.J.Bua,
A.J.Kuo,
P.Cheung,
C.L.Liu,
V.Migliori,
A.Espejo,
F.Casadio,
C.Bassi,
B.Amati,
M.T.Bedford,
E.Guccione,
and
O.Gozani
(2009).
Epigenome microarray platform for proteome-wide dissection of chromatin-signaling networks.
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PLoS One,
4,
e6789.
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E.Hallacli,
and
A.Akhtar
(2009).
X chromosomal regulation in flies: when less is more.
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Chromosome Res,
17,
603-619.
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M.Chen,
M.Takano-Maruyama,
O.M.Pereira-Smith,
G.O.Gaufo,
and
K.Tominaga
(2009).
MRG15, a component of HAT and HDAC complexes, is essential for proliferation and differentiation of neural precursor cells.
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J Neurosci Res,
87,
1522-1531.
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N.Lee,
H.Erdjument-Bromage,
P.Tempst,
R.S.Jones,
and
Y.Zhang
(2009).
The H3K4 demethylase lid associates with and inhibits histone deacetylase Rpd3.
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Mol Cell Biol,
29,
1401-1410.
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S.M.Sy,
M.S.Huen,
and
J.Chen
(2009).
MRG15 is a novel PALB2-interacting factor involved in homologous recombination.
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J Biol Chem,
284,
21127-21131.
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B.Sun,
J.Hong,
P.Zhang,
X.Dong,
X.Shen,
D.Lin,
and
J.Ding
(2008).
Molecular basis of the interaction of Saccharomyces cerevisiae Eaf3 chromo domain with methylated H3K36.
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J Biol Chem,
283,
36504-36512.
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PDB codes:
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C.Xu,
G.Cui,
M.V.Botuyan,
and
G.Mer
(2008).
Structural basis for the recognition of methylated histone H3K36 by the Eaf3 subunit of histone deacetylase complex Rpd3S.
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Structure,
16,
1740-1750.
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PDB codes:
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J.G.Doheny,
R.Mottus,
and
T.A.Grigliatti
(2008).
Telomeric position effect--a third silencing mechanism in eukaryotes.
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PLoS ONE,
3,
e3864.
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M.Zhang,
M.R.Pritchard,
F.A.Middleton,
J.A.Horton,
and
T.A.Damron
(2008).
Microarray analysis of perichondral and reserve growth plate zones identifies differential gene expressions and signal pathways.
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Bone,
43,
511-520.
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S.N.Garcia,
and
O.Pereira-Smith
(2008).
MRGing chromatin dynamics and cellular senescence.
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Cell Biochem Biophys,
50,
133-141.
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T.H.Sural,
S.Peng,
B.Li,
J.L.Workman,
P.J.Park,
and
M.I.Kuroda
(2008).
The MSL3 chromodomain directs a key targeting step for dosage compensation of the Drosophila melanogaster X chromosome.
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Nat Struct Mol Biol,
15,
1318-1325.
|
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|
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S.Lall
(2007).
Primers on chromatin.
|
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Nat Struct Mol Biol,
14,
1110-1115.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
