1TEY

NMR structure of human histone chaperone, ASF1A

Summary for 1TEY

• Entry DOI: 10.2210/pdb1tey/pdb
• NMR Information: BMRB: 6298
• Descriptor: ASF1 anti-silencing function 1 homolog A (1 entity in total)
• Functional Keywords: beta-sandwich, distorted immunoglobulin-like, chaperone
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q9Y294
• Total number of polymer chains: 1
• Total formula weight: 17928.00

Authors

Mousson, F.,Lautrette, A.,Thuret, J.Y.,Agez, M.,Amigues, B.,Courbeyrette, R.,Neumann, J.M.,Guerois, R.,Mann, C.,Ochsenbein, F. (deposition date: 2004-05-26, release date: 2005-04-12, Last modification date: 2024-05-22)

Primary citation

Mousson, F.,Lautrette, A.,Thuret, J.Y.,Agez, M.,Courbeyrette, R.,Amigues, B.,Becker, E.,Neumann, J.M.,Guerois, R.,Mann, C.,Ochsenbein, F.
Structural basis for the interaction of Asf1 with histone H3 and its functional implications.
Proc.Natl.Acad.Sci.Usa, 102:5975-5980, 2005

PubMed Abstract: Asf1 is a conserved histone chaperone implicated in nucleosome assembly, transcriptional silencing, and the cellular response to DNA damage. We solved the NMR solution structure of the N-terminal functional domain of the human Asf1a isoform, and we identified by NMR chemical shift mapping a surface of Asf1a that binds the C-terminal helix of histone H3. This binding surface forms a highly conserved hydrophobic groove surrounded by charged residues. Mutations within this binding site decreased the affinity of Asf1a for the histone H3/H4 complex in vitro, and the same mutations in the homologous yeast protein led to transcriptional silencing defects, DNA damage sensitivity, and thermosensitive growth. We have thus obtained direct experimental evidence of the mode of binding between a histone and one of its chaperones and genetic data suggesting that this interaction is important in both the DNA damage response and transcriptional silencing.

PubMed: 15840725
DOI: 10.1073/pnas.0500149102

Experimental method

SOLUTION NMR