Wilhelm F X, de Murcia G M, Daune M P
Nucleic Acids Res. 1974 Aug;1(8):1043-57. doi: 10.1093/nar/1.8.1043.
In native nucleoprotein, the premelting structural changes of DNA are not observed by circular dichroism measurements. In order to determine which protein fraction of chromatin is responsible for the absence of premelting we have examined a series of nucleoproteins depleted of different protein fractions by treatment with sodium chloride or sodium deoxycholate.The premelting reappears as soon as non-histone proteins are removed or in residual complexes from which the two slightly lysine-rich histone fractions (F2a2+F2b) have been removed. On the other hand, it is shown that histone F1 alone is not able to suppress the premelting phenomenon. It is thus concluded that the absence of premelting is a property of native nucleoprotein where interactions between the different proteins complexed with DNA can occur and especially between the non-histone proteins and the two slightly lysine-rich histone fractions.
在天然核蛋白中,通过圆二色性测量未观察到DNA的预熔解结构变化。为了确定染色质的哪种蛋白质组分导致了预熔解的缺失,我们检测了一系列通过用氯化钠或脱氧胆酸钠处理而耗尽不同蛋白质组分的核蛋白。一旦去除非组蛋白或去除了两个轻度富含赖氨酸的组蛋白组分(F2a2 + F2b)的残留复合物,预熔解就会重新出现。另一方面,结果表明单独的组蛋白F1不能抑制预熔解现象。因此得出结论,预熔解的缺失是天然核蛋白的一种特性,在天然核蛋白中,与DNA复合的不同蛋白质之间可以发生相互作用,特别是在非组蛋白与两个轻度富含赖氨酸的组蛋白组分之间。