2C1J: Molecular Basis For The Recognition Of Phosphorylated And Phosphoacetylated Histone H3 By 14-3-3

Citation:
Abstract
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.
PDB ID: 2C1JDownload
MMDB ID: 36227
PDB Deposition Date: 2005/9/15
Updated in MMDB: 2005/12
Experimental Method:
x-ray diffraction
Resolution: 2.6  Å
Source Organism:
synthetic construct
Similar Structures:
Biological Unit for 2C1J: tetrameric; determined by author and by software (PISA)
Molecular Components in 2C1J
Label Count Molecule
Proteins (4 molecules)
2
14-3-3 Protein Zeta/delta(Gene symbol: YWHAZ)
Molecule annotation
2
Histone H3 Acetylphosphopeptide
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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