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PDBsum entry 6hts
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DNA binding protein
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PDB id
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6hts
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Contents |
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434 a.a.
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429 a.a.
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680 a.a.
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326 a.a.
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96 a.a.
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82 a.a.
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106 a.a.
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96 a.a.
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86 a.a.
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72 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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Structure and regulation of the human ino80-Nucleosome complex.
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Authors
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R.Ayala,
O.Willhoft,
R.J.Aramayo,
M.Wilkinson,
E.A.Mccormack,
L.Ocloo,
D.B.Wigley,
X.Zhang.
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Ref.
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Nature, 2018,
556,
391-395.
[DOI no: ]
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PubMed id
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Abstract
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Access to DNA within nucleosomes is required for a variety of processes in cells
including transcription, replication and repair. Consequently, cells encode
multiple systems that remodel nucleosomes. These complexes can be simple,
involving one or a few protein subunits, or more complicated multi-subunit
machines 1 . Biochemical studies2-4 have placed the motor
domains of several chromatin remodellers in the superhelical location 2 region
of the nucleosome. Structural studies of yeast Chd1 and Snf2-a subunit in the
complex with the capacity to remodel the structure of chromatin (RSC)-in complex
with nucleosomes5-7 have provided insights into the basic mechanism
of nucleosome sliding performed by these complexes. However, how larger,
multi-subunit remodelling complexes such as INO80 interact with nucleosomes and
how remodellers carry out functions such as nucleosome sliding 8 ,
histone exchange 9 and nucleosome spacing10-12 remain
poorly understood. Although some remodellers work as monomers 13 ,
others work as highly cooperative dimers11, 14, 15. Here we present
the structure of the human INO80 chromatin remodeller with a bound nucleosome,
which reveals that INO80 interacts with nucleosomes in a previously undescribed
manner: the motor domains are located on the DNA at the entry point to the
nucleosome, rather than at superhelical location 2. The ARP5-IES6 module of
INO80 makes additional contacts on the opposite side of the nucleosome. This
arrangement enables the histone H3 tails of the nucleosome to have a role in the
regulation of the activities of the INO80 motor domain-unlike in other
characterized remodellers, for which H4 tails have been shown to regulate the
motor domains.
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