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PDBsum entry 5av5
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DNA binding protein/DNA
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PDB id
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5av5
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Contents |
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99 a.a.
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82 a.a.
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106 a.a.
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97 a.a.
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87 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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Intra- And inter-Nucleosomal interactions of the histone h4 tail revealed with a human nucleosome core particle with genetically-Incorporated h4 tetra-Acetylation.
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Authors
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M.Wakamori,
Y.Fujii,
N.Suka,
M.Shirouzu,
K.Sakamoto,
T.Umehara,
S.Yokoyama.
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Ref.
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Sci Rep, 2015,
5,
17204.
[DOI no: ]
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PubMed id
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Abstract
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Post-translational modifications (PTMs) of histones, such as lysine acetylation
of the N-terminal tails, play crucial roles in controlling gene expression. Due
to the difficulty in reconstituting site-specifically acetylated nucleosomes
with crystallization quality, structural analyses of histone acetylation are
currently performed using synthesized tail peptides. Through engineering of the
genetic code, translation termination, and cell-free protein synthesis, we
reconstituted human H4-mono- to tetra-acetylated nucleosome core particles
(NCPs), and solved the crystal structures of the
H4-K5/K8/K12/K16-tetra-acetylated NCP and unmodified NCP at 2.4 Å and
2.2 Å resolutions, respectively. The structure of the H4-tetra-acetylated NCP
resembled that of the unmodified NCP, and the DNA wrapped the histone octamer as
precisely as in the unmodified NCP. However, the B-factors were significantly
increased for the peripheral DNAs near the N-terminal tail of the intra- or
inter-nucleosomal H4. In contrast, the B-factors were negligibly affected by the
H4 tetra-acetylation in histone core residues, including those composing the
acidic patch, and at H4-R23, which interacts with the acidic patch of the
neighboring NCP. The present study revealed that the H4 tetra-acetylation
impairs NCP self-association by changing the interactions of the H4 tail with
DNA, and is the first demonstration of crystallization quality NCPs
reconstituted with genuine PTMs.
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