Structure of the histone chaperone Asf1 bound to the histone H3C-terminal helix and functional insights

被引：39
作者：
Agez, Morgane
Chen, Jun
Guerois, Raphael
van Heijenoort, Carine
Thuret, Jean-Yves
Mann, Carl [1 ]
Ochsenbein, Francoise
机构：
[1] CEA Saclay, Inst Biol & Technol Saclay, F-91191 Gif Sur Yvette, France
[2] Uniformed Serv Univ Hlth Sci, F Edward Hebert Sch Med, Dept Biochem & Mol Biol, Bethesda, MD 20814 USA
[3] Inst Chim Substance Nat, Lab Resonance Magnet Nucl & Haut Champ, F-91190 Gif Sur Yvette, France
来源：
STRUCTURE | 2007年 / 15卷 / 02期
关键词：
D O I：
10.1016/j.str.2007.01.002
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Asf1 is a histone chaperone that favors histone H3/H4 assembly and disassembly. We solved the structure of the conserved domain of human ASH A in complex with the C-terminal helix of histone H3 using nuclear magnetic resonance spectroscopy. This structure is fully compatible with an association of ASH with the heteroclimeric form of histones H3/H4. In our model, ASH 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.
引用
收藏
页码：191 / 199
页数：9
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