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PDBsum entry 5erc
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Transcription
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PDB id
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5erc
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References listed in PDB file
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Key reference
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Title
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Bivalent interaction of the pzp domain of brpf1 with the nucleosome impacts chromatin dynamics and acetylation.
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Authors
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B.J.Klein,
U.M.Muthurajan,
M.E.Lalonde,
M.D.Gibson,
F.H.Andrews,
M.Hepler,
S.Machida,
K.Yan,
H.Kurumizaka,
M.G.Poirier,
J.Côté,
K.Luger,
T.G.Kutateladze.
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Ref.
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Nucleic Acids Res, 2016,
44,
472-484.
[DOI no: ]
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PubMed id
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Abstract
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BRPF1 (bromodomain PHD finger 1) is a core subunit of the MOZ histone
acetyltransferase (HAT) complex, critical for normal developmental programs and
implicated in acute leukemias. BRPF1 contains a unique assembly of zinc fingers,
termed a PZP domain, the physiological role of which remains unclear. Here, we
elucidate the structure-function relationship of this novel epigenetic reader
and detail the biological and mechanistic consequences of its interaction with
nucleosomes. PZP has a globular architecture and forms a 2:1 stoichiometry
complex with the nucleosome, bivalently interacting with histone H3 and DNA.
This binding impacts the nucleosome dynamics, shifting the DNA
unwrapping/rewrapping equilibrium toward the unwrapped state and increasing DNA
accessibility. We demonstrate that the DNA-binding function of the BRPF1 PZP
domain is required for the MOZ-BRPF1-ING5-hEaf6 HAT complex to be recruited to
chromatin and to acetylate nucleosomal histones. Our findings reveal a novel
link between chromatin dynamics and MOZ-mediated acetylation.
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