Bavykin S G, Usachenko S I, Mirzabekov A D
Mol Biol (Mosk). 1988 Mar-Apr;22(2):531-7.
We have reconstructed nucleosomes from a histone octamer (H2A, H2B, H3, H4)2 and DNA 146 b.p. or 2-3 thousands b.p. in length. Comparison by means of DNA-histone cross-links of the primary organization of minimal nucleosomes obtained by reconstruction or isolated from chromatin of chicken erythrocyte nuclei has demonstrated a high similarity in histone location on their DNAs. Simultaneously, there have been observed some variations in the character of interaction for all core histones with DNA on nucleosomes. Thus, the cross-link of histone H4 with DNA of a core particle at H4 sites (65), unlike H4(55) and H4(88) sites, significantly depends on the superstructure of chromatin, ionic strength of solution and the presence of denaturating agents. All these differences are expected to probe the existence of conformational isomers for core particles. (Bracketed is the distance from the histone interaction site with the DNA of the core particle to the DNA 5'-terminus.)
我们已经从组蛋白八聚体(H2A、H2B、H3、H4)₂和长度为146个碱基对或2000 - 3000个碱基对的DNA重构了核小体。通过DNA - 组蛋白交联对通过重构获得或从鸡红细胞核染色质中分离出的最小核小体的一级结构进行比较,结果表明组蛋白在其DNA上的定位具有高度相似性。同时,已观察到所有核心组蛋白与核小体上的DNA相互作用特征存在一些差异。因此,核心颗粒的DNA在H4位点(65)处与组蛋白H4的交联,与H4(55)和H4(88)位点不同,显著依赖于染色质的超结构、溶液的离子强度以及变性剂的存在。预计所有这些差异都能探测到核心颗粒构象异构体的存在。(括号内是从核心颗粒的DNA与组蛋白相互作用位点到DNA 5'端的距离。)