Santisteban M S
Department of Microbiology, University of Virginia, HSC, School of Medicine, Charlottesville 22908, USA.
Pathol Biol (Paris). 1994 Nov;42(9):868-83.
This bibliographic review, the first of a series of three on chromatin structure, discusses the current knowledge and hypotheses concerning chromatin organization in nucleosomes and fibers. Presently, the structural features of the chromatin arrangement are better known for the low levels of organization, e.g. nucleosome, but there is much disagreement about levels of organization higher than the 10 nm fiber. The published reports are consistent with the model that, in the nucleosome, the DNA is wrapped around the histone octamer. The histone octamer whose structure and dimensions were investigated for years is viewed today as a tripartite particle with the (H3-H4)2 tetramer flanked by two H2A-H2B dimers. In the chromatosome, two turns of DNA around of the histone octamer are sealed by the histone H1 that binds DNA at the points of entry and exit. A chain of nucleosomes, each with about 200 bp associated DNA, forms a 10 nm fiber with a DNA packing ratio of 6-7. The 10 nm fiber is then condensed into a 30 nm fiber, likely of solenoid structure, that is stabilized by histone H1. All the different models proposed for the structure of the 30 nm fiber are consistent with a DNA packing ratio of 35-40.
这篇文献综述是关于染色质结构的系列三篇中的第一篇,讨论了目前关于核小体和纤维中染色质组织的知识及假说。目前,染色质排列的结构特征在较低组织水平(如核小体)上更为人所知,但对于高于10纳米纤维的组织水平存在诸多分歧。已发表的报告与核小体中DNA缠绕在组蛋白八聚体周围的模型一致。多年来对其结构和尺寸进行研究的组蛋白八聚体,如今被视为一个三方颗粒,由(H3-H4)2四聚体两侧各有一个H2A-H2B二聚体组成。在核小体中,组蛋白八聚体周围的两圈DNA由在进出点结合DNA的组蛋白H1封闭。一系列核小体,每个都有大约200个碱基对相关DNA,形成一个DNA压缩比为6至七的10纳米纤维。然后,10纳米纤维浓缩成一个可能具有螺线管结构的30纳米纤维,由组蛋白H1稳定。为30纳米纤维结构提出的所有不同模型都与35至40的DNA压缩比一致。