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PDBsum entry 2c1n
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Signaling protein
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PDB id
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2c1n
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References listed in PDB file
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Key reference
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Title
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Molecular basis for the recognition of phosphorylated and phosphoacetylated histone h3 by 14-3-3.
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Authors
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N.Macdonald,
J.P.Welburn,
M.E.Noble,
A.Nguyen,
M.B.Yaffe,
D.Clynes,
J.G.Moggs,
G.Orphanides,
S.Thomson,
J.W.Edmunds,
A.L.Clayton,
J.A.Endicott,
L.C.Mahadevan.
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Ref.
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Mol Cell, 2005,
20,
199-211.
[DOI no: ]
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PubMed id
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Abstract
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Phosphorylation of histone H3 is implicated in transcriptional activation and
chromosome condensation, but its immediate molecular function has remained
obscure. By affinity chromatography of nuclear extracts against modified H3 tail
peptides, we identified 14-3-3 isoforms as proteins that bind these tails in a
strictly phosphorylation-dependent manner. Acetylation of lysines 9 and 14 does
not impede 14-3-3 binding to serine 10-phosphorylated H3 tails. In vivo, 14-3-3
is inducibly recruited to c-fos and c-jun nucleosomes upon gene activation,
concomitant with H3 phosphoacetylation. We have determined the structures of
14-3-3zeta complexed with serine 10-phosphorylated or phosphoacetylated H3
peptides. These reveal a distinct mode of 14-3-3/phosphopeptide binding and
provide a structural understanding for the lack of effect of acetylation at
lysines 9 and 14 on this interaction. 14-3-3 isoforms thus represent a class of
proteins that mediate the effect of histone phosphorylation at inducible genes.
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Figure 3.
Figure 3. Binding Studies of H3 Tail Peptides to 14-3-3
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Figure 5.
Figure 5. Structure of 14-3-3 Complexed with Histone H3
Peptide Phosphorylated at Serine 10
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2005,
20,
199-211)
copyright 2005.
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