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核小体核心颗粒的X射线结构。

X-ray structure of the nucleosome core particle.

作者信息

Uberbacher E C, Bunick G J

机构信息

University of Tennessee-Oak Ridge Graduate School of Biomedical Sciences and Biology 37831.

出版信息

J Biomol Struct Dyn. 1985 Jun;2(6):1033-55. doi: 10.1080/07391102.1985.10507623.

Abstract

Two monoclinic crystal forms (P2(1),C2) of chicken erythrocyte nucleosomes have been under study in this laboratory. The x-ray structure of the P2(1) crystal form has been solved to 15 A resolution. The B-DNA superhelix has a relatively uniform curvature, with only several local distortions observed in the superhelix. The individual histone domains have been localized and specific contacts between each histone and the DNA can be observed. Histone contacts to the inner surface of the DNA superhelix occur predominantly at the minor groove sites. Most of the histone core is contained within the inner surface of the superhelical DNA, except for part of H2A which extends between the DNA gyres near the terminus of the DNA. No part of H2A blocks the DNA terminus or would prevent a smooth exit of the DNA into the linker region. A similar extension of a portion of histone H4 between the DNA gyres occurs close to the dyad axis. Both unique nucleosomes in the P2(1) asymmetric unit demonstrate good dyad symmetry and are similar to each other throughout the histone core and DNA regions.

摘要

本实验室一直在研究鸡红细胞核小体的两种单斜晶型(P2(1)、C2)。P2(1)晶型的X射线结构已解析至15埃分辨率。B型DNA超螺旋具有相对均匀的曲率,在超螺旋中仅观察到一些局部扭曲。各个组蛋白结构域已定位,并且可以观察到每个组蛋白与DNA之间的特定接触。组蛋白与DNA超螺旋内表面的接触主要发生在小沟部位。除了H2A的一部分在DNA末端附近的DNA螺旋之间延伸外,大多数组蛋白核心都包含在超螺旋DNA的内表面内。H2A的任何部分都不会阻塞DNA末端,也不会阻止DNA顺利进入连接区。组蛋白H4的一部分在靠近二分轴的DNA螺旋之间有类似的延伸。P2(1)不对称单元中的两个独特核小体都表现出良好的二分对称性,并且在整个组蛋白核心和DNA区域彼此相似。

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