Asymmetries in the nucleosome core particle at 2.5 Å resolution
Asymmetries in the nucleosome core particle at 2.5 Å resolution
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DOI：
10.1107/s0907444900011847
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发表时间：
2000-12-01
影响因子：
2.2
通讯作者：
Bunick, GJ
中科院分区：
文献类型：
--
作者：
Harp, JM;Hanson, BL;Bunick, GJ
核小体核心颗粒的2.5埃X射线晶体结构为理解核小体提供了重要的补充，核小体是染色质结构的基本单位。对N-端组蛋白尾部的结构进行了延伸，并提供了关于水化和离子结合的细节。该结构由两个对称分子、天然鸡组蛋白八聚体核心和DNA回文组成，有望形成一个完美的双重对称核小体核心粒子。事实上，由于DNA与蛋白质表面的结合以及颗粒在晶格中的堆积，结果是不对称的。通过比较核小体核心颗粒内的不对称性和核小体的组蛋白八聚体核心的结构，对不对称性进行了分析。
The 2.5 Angstrom X-ray crystal structure of the nucleosome core particle presented here provides significant additions to the understanding of the nucleosome, the fundamental unit of chromatin structure. Extensions are made to the structure of the N-terminal histone tails and details are provided on hydration and ion binding. The structure is composed of twofold symmetric molecules, native chicken histone octamer cores and the DNA palindrome, which were expected to form a perfectly twofold symmetric nucleosome core particle. In fact, the result is asymmetric owing to the binding of the DNA to the protein surface and to the packing of the particles in the crystal lattice. An analysis is made of the asymmetries by comparisons both within the nucleosome core particle and to the structure of the histone octamer core of the nucleosome.