ASF1 binds to a heterodimer of histories H3 and H4: A two-step mechanism for the assembly of the H3-H4 heterotetramer on DNA

被引：110

作者：

English, CM

Maluf, NK

Tripet, B

Churchill, MEA

Tyler, JK

机构：

[1] Univ Colorado, Hlth Sci Ctr Fitzsimons, Dept Biochem & Mol Genet, Aurora, CO 80045 USA

[2] Univ Colorado, Hlth Sci Ctr, Dept Pharmaceut Sci, Denver, CO 80262 USA

[3] Univ Colorado, Hlth Sci Ctr, Dept Pharmacol, Aurora, CO 80045 USA

来源：

BIOCHEMISTRY | 2005年 / 44卷 / 42期

关键词：

D O I：

10.1021/bi051333h

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：

The first step in the formation of the nucleosome is commonly assumed to be the deposition of a histone H3-H4 heterotetramer onto DNA. Anti silencing function I (ASF1) is a major historic H3-H4 chaperone that deposits histones H3 and H4 onto DNA. With a goal of understanding the mechanism of deposition of histones H3 and H4 onto DNA, we have determined the stoichiometry of the Asf1-H3-H4 complex. We have established that a single molecule of Asf1 binds to an H3-H4 heterodimer using gel filtration, amino acid, reversed-phase chromatography, and analytical ultracentrifugation analyses. We demonstrate that Asf1 blocks formation of the H3-H4 heterotetramer by a mechanism that likely involves occlusion of the H3-H3 dimerization interface.

引用

页码：13673 / 13682

页数：10

共 53 条

[1] The histone chaperone Asf1p mediates global chromatin disassembly in vivo [J].