与30S核糖体亚基平台结构域相对应的核糖核蛋白颗粒的体外组装。
In vitro assembly of a ribonucleoprotein particle corresponding to the platform domain of the 30S ribosomal subunit.
作者信息
Agalarov S C, Zheleznyakova E N, Selivanova O M, Zheleznaya L A, Matvienko N I, Vasiliev V D, Spirin A S
机构信息
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142292 Russia.
出版信息
Proc Natl Acad Sci U S A. 1998 Feb 3;95(3):999-1003. doi: 10.1073/pnas.95.3.999.
A fragment of the 16S RNA of Thermus thermophilus corresponding to the central domain (nucleotides 547-895) has been prepared by transcription in vitro. Incubation of this fragment with the total 30S ribosomal proteins has resulted in the formation of a compact 12S ribonucleoprotein particle. This particle contained five T. thermophilus proteins corresponding to Escherichia coli ribosomal proteins S6, S8, S11, S15, and possibly S18, all of which were previously shown to interact with the central domain of the 16S RNA and to be localized in the platform (side bulge) of the 30S ribosomal subunit. When examined by electron microscopy, isolated particles have an appearance that is similar in size and shape to the corresponding morphological features of the 30S subunit. We conclude that the central domain of the 16S RNA can independently and specifically assemble with a defined subset of ribosomal proteins into a compact ribonucleoprotein particle corresponding to the platform (side bulge) of the 30S subunit.
嗜热栖热菌（Thermus thermophilus）16S RNA对应中央结构域（核苷酸547 - 895）的一个片段已通过体外转录制备。将该片段与完整的30S核糖体蛋白一起温育，导致形成了一个紧密的12S核糖核蛋白颗粒。该颗粒包含五种与大肠杆菌核糖体蛋白S6、S8、S11、S15以及可能的S18相对应的嗜热栖热菌蛋白，所有这些蛋白先前已被证明可与16S RNA的中央结构域相互作用，并定位于30S核糖体亚基的平台（侧凸起）中。通过电子显微镜检查时，分离出的颗粒在大小和形状上的外观与30S亚基相应的形态特征相似。我们得出结论，16S RNA的中央结构域可以独立且特异性地与核糖体蛋白的特定子集组装成一个与30S亚基的平台（侧凸起）相对应的紧密核糖核蛋白颗粒。
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