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PDBsum entry 4psx
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Histone/transferase
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PDB id
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4psx
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Contents |
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313 a.a.
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361 a.a.
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39 a.a.
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37 a.a.
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12 a.a.
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References listed in PDB file
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Key reference
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Title
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Hat2p recognizes the histone h3 tail to specify the acetylation of the newly synthesized h3/h4 heterodimer by the hat1p/hat2p complex.
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Authors
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Y.Li,
L.Zhang,
T.Liu,
C.Chai,
Q.Fang,
H.Wu,
P.A.Agudelo garcia,
Z.Han,
S.Zong,
Y.Yu,
X.Zhang,
M.R.Parthun,
J.Chai,
R.M.Xu,
M.Yang.
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Ref.
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Genes Dev, 2014,
28,
1217-1227.
[DOI no: ]
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PubMed id
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Abstract
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Post-translational modifications of histones are significant regulators of
replication, transcription, and DNA repair. Particularly, newly synthesized
histone H4 in H3/H4 heterodimers becomes acetylated on N-terminal lysine
residues prior to its incorporation into chromatin. Previous studies have
established that the histone acetyltransferase (HAT) complex Hat1p/Hat2p
medicates this modification. However, the mechanism of how Hat1p/Hat2p
recognizes and facilitates the enzymatic activities on the newly assembled H3/H4
heterodimer remains unknown. Furthermore, Hat2p is a WD40 repeat protein, which
is found in many histone modifier complexes. However, how the WD40 repeat
proteins facilitate enzymatic activities of histone modification enzymes is
unclear. In this study, we first solved the high-resolution crystal structure of
a Hat1p/Hat2p/CoA/H4 peptide complex and found that the H4 tail interacts with
both Hat1p and Hat2p, by which substrate recruitment is facilitated. We further
discovered that H3 N-terminal peptides can bind to the Hat2p WD40 domain and
solved the structure of the Hat1p/Hat2p/CoA/H4/H3 peptide complex. Moreover, the
interaction with Hat2p requires unmodified Arg2/Lys4 and Lys9 on the H3 tail,
suggesting a novel model to specify the activity of Hat1p/Hat2p toward newly
synthesized H3/H4 heterodimers. Together, our study demonstrated the substrate
recognition mechanism by the Hat1p/Hat2p complex, which is critical for DNA
replication and other chromatin remodeling processes.
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