Structure of the histone chaperone ASF1 bound to the histone H3 C-terminal helix and functional insights. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Structure / Struct Fold Des; Structure (Camb ) Année : 2007

Structure of the histone chaperone ASF1 bound to the histone H3 C-terminal helix and functional insights.

M. Agez
  • Fonction : Auteur
Jie Chen
  • Fonction : Auteur
  • PersonId : 761941
  • IdRef : 200253832
R. Guerois
  • Fonction : Auteur
J. Y. Thuret
  • Fonction : Auteur
C. Mann
  • Fonction : Auteur
F. Ochsenbein
  • Fonction : Auteur

Résumé

Asf1 is a histone chaperone that favors histone H3/H4 assembly and disassembly. We solved the structure of the conserved domain of human ASF1A in complex with the C-terminal helix of histone H3 using nuclear magnetic resonance spectroscopy. This structure is fully compatible with an association of ASF1 with the heterodimeric form of histones H3/H4. In our model, ASF1 substitutes for the second H3/H4 heterodimer that is normally found in heterotetrameric H3/H4 complexes. This result constitutes an essential step in the fundamental understanding of the mechanisms of nucleosome assembly by histone chaperones. Point mutations that perturb the Asf1/histone interface were designed from the structure. The decreased binding affinity of the Asf1-H3/H4 complex correlates with decreased levels of H3-K56 acetylation and phenotypic defects in vivo.

Dates et versions

hal-00275479 , version 1 (24-04-2008)

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Citer

M. Agez, Jie Chen, R. Guerois, C. van Heijenoort, J. Y. Thuret, et al.. Structure of the histone chaperone ASF1 bound to the histone H3 C-terminal helix and functional insights.. Structure / Struct Fold Des; Structure (Camb ), 2007, 15 (2), pp.191-9. ⟨10.1016/j.str.2007.01.002⟩. ⟨hal-00275479⟩
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