Visualization of protein S1 within the 30S ribosomal subunit and its interaction with messenger RNA
Visualization of protein S1 within the 30S ribosomal subunit and its interaction with messenger RNA
复制标题
DOI：
10.1073/pnas.211266898
复制
发表时间：
2001-10-09
影响因子：
11.1
通讯作者：
Frank, J
中科院分区：
文献类型：
--
作者：
Sengupta, J;Agrawal, RK;Frank, J
S1 是最大的核糖体蛋白，存在于细菌核糖体的小亚基中。它对于稳定核糖体上的 mRNA 具有关键作用。到目前为止，S1 尚未确定结构。通过将大肠杆菌核糖体的冷冻电子显微镜图谱与缺乏 S1 的 30S 亚基的最新 X 射线晶体结构进行比较，我们确定了该图谱中的 S1 蛋白质量。根据我们的发现，S1位于30S亚基的头部、平台和主体的连接处，从而解释了所有现有的生化和交联数据。我们图中识别出的蛋白质 S1 具有复杂的细长形状，其中心部分有两个孔。 IN 末端结构域形成延伸之一，渗透到 30S 亚基的头部。 S1 与紧邻 Shine-Dalgarno 序列上游的 mRNA 11 个核苷酸直接相互作用的证据解释了该蛋白质在识别 mRNA 5' 区域中的作用。
S1 is the largest ribosomal protein, present in the small subunit of the bacterial ribosome. It has a pivotal role in stabilizing the mRNA on the ribosome. Thus far, S1 has eluded structural determination. We have identified the S1 protein mass in the cryo-electron microscopic map of the Escherichia coli ribosome by comparing the map with a recent x-ray crystallographic structure of the 30S subunit, which lacks S1. According to our finding, S1 is located at the junction of head, platform, and main body of the 30S subunit, thus explaining all existing biochemical and crosslinking data. Protein S1 as identified in our map has a complex, elongated shape with two holes in its central portion. The IN-terminal domain, forming one of the extensions, penetrates into the head of the 30S subunit. Evidence for direct interaction of S1 with 11 nucleotides of the mRNA, immediately upstream of the Shine-Dalgarno sequence, explains the protein's role in the recognition of the 5' region of mRNA.