Chromatin fiber folding: Requirement for the histone H4N-terminal tail

被引:418
作者
Dorigo, B [1 ]
Schalch, T [1 ]
Bystricky, K [1 ]
Richmond, TJ [1 ]
机构
[1] Swiss Fed Inst Technol, Inst Mol Biol & Biophys, ETH Honggerberg, CH-8093 Zurich, Switzerland
关键词
chromatin fiber; higher-order structure; nucleosome array; histone tails; sedimentation;
D O I
10.1016/S0022-2836(03)00025-1
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
We have developed a self-assembly system for nucleosome arrays in which recombinant, post-translationally unmodified histone proteins are combined with DNA of defined-sequence to form chromatin higher-order structure. The nucleosome arrays obtained are highly homogeneous and sediment at 53 S when maximally folded in 1 mM or 100 mM MgCl2. The folding properties are comparable to established systems. Analytical ultracentrifugation is used to determine the consequence of individual histone tail domain deletions on array folding. Fully compacted chromatin fibers are obtained with any one of the histone tails deleted with the exception of the H4 N terminus. The region of the H4 tail, which mediates compaction, resides in the stretch of amino acids 14-19. (C) 2003 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:85 / 96
页数:12
相关论文
共 74 条