Cryo-EM Study of the Chromatin Fiber Reveals a Double Helix Twisted by Tetranucleosomal Units

被引：471

作者：

Song, Feng ^{[1
,2
]}

Chen, Ping ^{[1
]}

Sun, Dapeng ^{[1
,2
]}

Wang, Mingzhu ^{[1
]}

Dong, Liping ^{[1
,2
]}

Liang, Dan ^{[1
,2
]}

Xu, Rui-Ming ^{[1
]}

Zhu, Ping ^{[1
]}

Li, Guohong ^{[1
]}

机构：

[1] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China

[2] Univ Chinese Acad Sci, Beijing 100049, Peoples R China

来源：

SCIENCE | 2014年 / 344卷 / 6182期

基金：

中国国家自然科学基金;

关键词：

HIGHER-ORDER STRUCTURE; LINKER HISTONE H5; X-RAY-DIFFRACTION; NUCLEOSOME; ORGANIZATION; MICROSCOPY; RESOLUTION; FILAMENT; LOCATION; OCTAMER;

D O I：

10.1126/science.1251413

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The hierarchical packaging of eukaryotic chromatin plays a central role in transcriptional regulation and other DNA-related biological processes. Here, we report the 11-angstrom-resolution cryogenic electron microscopy (cryo-EM) structures of 30-nanometer chromatin fibers reconstituted in the presence of linker histone H1 and with different nucleosome repeat lengths. The structures show a histone H1-dependent left-handed twist of the repeating tetranucleosomal structural units, within which the four nucleosomes zigzag back and forth with a straight linker DNA. The asymmetric binding and the location of histone H1 in chromatin play a role in the formation of the 30-nanometer fiber. Our results provide mechanistic insights into how nucleosomes compact into higher-order chromatin fibers.

引用

页码：376 / 380

页数：5

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