A charged and contoured surface on the nucleosome regulates chromatin compaction

被引：86
作者：
Chodaparambil, Jayanth V.
Barbera, Andrew J.
Lu, Xu
Kaye, Kenneth M.
Hansen, Jeffrey C.
Luger, Karolin [1 ]
机构：
[1] Colorado State Univ, Dept Biochem & Mol Biol, Ft Collins, CO 80523 USA
[2] Brigham & Womens Hosp, Dept Med, Boston, MA 02115 USA
[3] Harvard Univ, Sch Med, Dept Med, Boston, MA 02115 USA
[4] Howard Hughes Med Inst, Chevy Chase, MD 20815 USA
来源：
NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2007年 / 14卷 / 11期
关键词：
D O I：
10.1038/nsmb1334
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：
Local nucleosome-nucleosome interactions in cis drive chromatin folding, whereas interactions in trans lead to fiber-fiber oligomerization. Here we show that peptides derived from the histone H4 tail and Kaposi's sarcoma herpesvirus LANA protein can replace the endogenous H4 tail, resulting in array folding and oligomerization. Neutralization of a LANA binding site on the histone surface enhanced rather than abolished nucleosome-nucleosome interactions. We maintain that the contoured nucleosome surface is centrally involved in regulating chromatin condensation.
引用
收藏
页码：1105 / 1107
页数：3
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