论文摘要
<正>H2A.B and H2A.Z.2.2 （Z.2.2）, the histone H2A variants that lead to the least stable nucleosomes and highly dynamic chromatins, play critical roles in multiple biological processes.Here, by stabilizing the H2A.B-containing nucleosome core particle （H2A.B-NCP）, we successfully determine a 2.8?resolution cryo-EM structures of H2A.B-NCP at, in which the histone octamer is surrounded by only～93 base pairs of DNAs and undergoes large-scale conformational changes. The unusual nucleosome structure shows that multiple H2A.B residues in
论文目录
文章来源
类型: 国内会议
作者: Min ZHOU,Lin-chang DAI,Chen-min LI,Liu-xin SHI,Yan HUANG,Zhen-qian GUO,Fei WU,Xiao-yan XIE,Ping ZHU,Zheng ZHOU
来源: 第六届全国冷冻电子显微学与结构生物学专题研讨会 2019-06-16
年度: 2019
分类: 基础科学
专业: 生物学
单位: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules,Institute of Biophysics, Chinese Academy of Sciences,University of Chinese Academy of Sciences,University of Science and Technology of China
分类号: Q51
DOI: 10.26914/c.cnkihy.2019.038781
页码: 37
总页数: 1
文件大小: 120k
下载量: 4