Serdiuk I N, Agalarov S Ch, Gongadze G M, Gudkov A T, Sedel'nikova S E
Mol Biol (Mosk). 1984 Jan-Feb;18(1):244-61.
X-ray and neutron scattering, as well as velocity sedimentation, were used to study the shape and dimensions (compactness) of isolated ribosomal (16S and 23S) RNA's and their complexes with ribosomal proteins. The neutron scattering of ribosomal particles in 42% 2H2O where the protein component is contrast-matched, were taken as a standard of comparison characterizing the dimensions and shape of the 16S and 23S RNA in situ. This comparison allowed the following conclusions: (1) The shape of the isolated 16S RNA at a sufficient Mg2+ concentration (e. g., in the reconstruction buffer) is similar to that of the 16S RNA in situ, but its compactness is somewhat less. (2) The 16S RNA in the complex with protein S4 has a shape and compactness similar to those of the isolated 16S RNA. (3) The 16S RNA in the complex with four core proteins, namely S4, S7, S8 and S15, has a shape and compactness similar to those of the isolated 16S RNA. (4). The six ribosomal proteins, S4, S7, S8, S15, S16, and S17, are necessary and sufficient for the 16S RNA to acquire a compactness similar to that in situ.
利用X射线和中子散射以及速度沉降法,研究了分离出的核糖体(16S和23S)RNA及其与核糖体蛋白复合物的形状和尺寸(紧密程度)。以核糖体颗粒在42% 2H2O中的中子散射(其中蛋白质成分的对比度匹配)作为比较标准,用以表征原位16S和23S RNA的尺寸和形状。通过这种比较得出了以下结论:(1)在足够的Mg2+浓度下(例如,在重建缓冲液中),分离出的16S RNA的形状与原位16S RNA相似,但其紧密程度稍低。(2)与蛋白质S4形成复合物的16S RNA的形状和紧密程度与分离出的16S RNA相似。(3)与四种核心蛋白(即S4、S7、S8和S15)形成复合物的16S RNA的形状和紧密程度与分离出的16S RNA相似。(4)六种核糖体蛋白S4、S7、S8、S15、S16和S17对于16S RNA获得与原位相似的紧密程度是必要且充分的。