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PDBsum entry 4xzq
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Structural protein/DNA
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PDB id
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4xzq
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Contents |
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98 a.a.
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79 a.a.
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106 a.a.
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93 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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Histone acetylation near the nucleosome dyad axis enhances nucleosome disassembly by rsc and swi/snf.
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Authors
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N.Chatterjee,
J.A.North,
M.L.Dechassa,
M.Manohar,
R.Prasad,
K.Luger,
J.J.Ottesen,
M.G.Poirier,
B.Bartholomew.
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Ref.
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Mol Cell Biol, 2015,
35,
4083-4092.
[DOI no: ]
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PubMed id
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Abstract
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Signaling associated with transcription activation occurs through
posttranslational modification of histones and is best exemplified by lysine
acetylation. Lysines are acetylated in histone tails and the core domain/lateral
surface of histone octamers. While acetylated lysines in histone tails are
frequently recognized by other factors referred to as "readers," which
promote transcription, the mechanistic role of the modifications in the lateral
surface of the histone octamer remains unclear. By using X-ray crystallography,
we found that acetylated lysines 115 and 122 in histone H3 are solvent
accessible, but in biochemical assays they appear not to interact with the
bromodomains of SWI/SNF and RSC to enhance recruitment or nucleosome
mobilization, as previously shown for acetylated lysines in H3 histone tails.
Instead, we found that acetylation of lysines 115 and 122 increases the
predisposition of nucleosomes for disassembly by SWI/SNF and RSC up to 7-fold,
independent of bromodomains, and only in conjunction with contiguous
nucleosomes. Thus, in combination with SWI/SNF and RSC, acetylation of lateral
surface lysines in the histone octamer serves as a crucial regulator of
nucleosomal dynamics distinct from the histone code readers and writers.
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