Cryo-electron microscopy structure of the H3-H4 octasome without histones H2A and H2B

Cryo-electron microscopy structure of the H3-H4 octasome without histones H2A and H2B
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不含组蛋白 H2A 和 H2B 的 H3-H4 八体的冷冻电镜结构

DOI:
10.1101/2021.10.27.466091
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发表时间:
2021
期刊:
bioRxiv
影响因子:
--
通讯作者:
Kurumizaka.
Kurumizaka.
中科院分区:
--
文献类型:
--
作者:
K;Nozawa.;Y;Takizawa.;L;Pierrakeas.;K;Saikusa.;S Akashi.;E;Luk.; H;Kurumizaka.

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典型核小体是真核生物染色质的主要包装单位,其核心由两个组蛋白H2 A-H2 B和H3-H4二聚体组成,周围包裹着约147个碱基对的DNA。在这里,我们解决了H3-H4八体的结构,这是一个核小体样颗粒的核心组成的四个H3-H4二聚体。两种构象,开放和关闭,确定在3.9毫米和3.6毫米的分辨率,分别由冷冻电子显微镜。H3-H4八体由一个二-四聚体核心组成,被约120 bp的DNA包裹在1.5个负超螺旋圈中。H3-H4八酶体是一个由H4-H4'组成的八酶体,位于H3-H3'之间的半胱氨酸探针在细胞内交联证实了H3-H4八酶体的存在。
The canonical nucleosome, which represents the predominant packaging unit in eukaryotic chromatin, has an octameric core made up of two histone H2A-H2B and H3-H4 dimers with ~147 base-pair (bp) DNA wrapping around it. Non-nucleosome particles with alterative histone stoichiometries and DNA wrapping configurations have been found, and they could profoundly influence genome architecture and function. Here we solved the structure of the H3-H4 octasome, which is a nucleosome-like particle with a core made up of four H3-H4 dimers. Two conformations, open and closed, are determined at 3.9 Å and 3.6 Å resolutions by cryo-electron microscopy, respectively. The H3-H4 octasome, made up of a di-tetrameric core, is wrapped by ~120 bp DNA in 1.5 negative superhelical turns. The symmetrical halves are connected by a unique H4-H4’ interface along the dyad axis.In vivocrosslinking of cysteine probes placed at another unique H3-H3’ interface demonstrated the existence of the H3-H4 octasome in cells.
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