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组蛋白F2a1的自组装

Self assembly of histone F2a1.

作者信息

Sperling R, Bustin M

出版信息

Proc Natl Acad Sci U S A. 1974 Nov;71(11):4625-9. doi: 10.1073/pnas.71.11.4625.

Abstract

Purified F(2)a(1) histone molecules assemble into organized structures observable by electron microscopy. The basic structure observed at pH 8 and ionic strength of 0.15 has the shape of a bent rod with an average width of 22 A. The average circumferential length of the rod is 220 A and the average distance between the tips of the rod is 150 A. When the ionic strength is increased the rods align lengthwise into intertwined fiber-like structures. In some cases bent rods assemble "face-to-face" to give circular structures. At high protein concentrations the long fibers form paracrystalline arrays. Examination of these arrays by optical diffraction yielded a meridional reflection with a spacing of 150 A. The main additional reflections are compatible with a structure having a repeat unit of 300 A. We suggest that in chromatin the DNA is packed around organized periodic histone structures and that the periodicity of the histone structure may dictate the periodicity of the repeating unit in chromatin.

摘要

纯化的F(2)a(1)组蛋白分子组装成电子显微镜下可观察到的有序结构。在pH值为8、离子强度为0.15时观察到的基本结构呈弯曲杆状,平均宽度为22埃。杆的平均周长为220埃,杆尖之间的平均距离为150埃。当离子强度增加时,杆状结构沿长度方向排列成相互交织的纤维状结构。在某些情况下,弯曲的杆状结构“面对面”组装形成圆形结构。在高蛋白质浓度下,长纤维形成准晶体阵列。通过光学衍射对这些阵列进行检查,得到了间距为150埃的子午线反射。主要的额外反射与具有300埃重复单元的结构相符。我们认为,在染色质中,DNA围绕有组织的周期性组蛋白结构包装,并且组蛋白结构的周期性可能决定染色质中重复单元的周期性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75b8/433941/05ffe22e79de/pnas00074-0360-a.jpg

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