| Literature DB >> 17292837 |
Morgane Agez1, Jun Chen, Raphaël Guerois, Carine van Heijenoort, Jean-Yves Thuret, Carl Mann, Francoise Ochsenbein.
Abstract
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.Entities:
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Year: 2007 PMID： 17292837 DOI： 10.1016/j.str.2007.01.002
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006