大肠杆菌核糖体蛋白L10的RNA和蛋白质结合位点研究。
Studies on the RNA and protein binding sites of the E. coli ribosomal protein L10.
作者信息
Pettersson I
出版信息
Nucleic Acids Res. 1979 Jun 11;6(7):2637-46. doi: 10.1093/nar/6.7.2637.
Abstract
We have used modification of specific amino acid residues in the E. coli ribosomal protein L10 as a tool to study its interactions with another ribosomal protein, L7/L12, as well as with ribosomal core particles and with 23S RNA. The ribosome and RNA binding capability of L10 was found to be inhibited by modification of one more of its arginine residues. This treatment does not affect the ability of L10 to bind four molecules of L7/L12 in a L7/L12-L10 complex. Our results support the view that L10's role in promoting the L7/L12-ribosome association is due primarily to its ability to bind to both 23S RNA and L7/L12 simultaneously.
摘要
我们利用对大肠杆菌核糖体蛋白L10中特定氨基酸残基的修饰作为一种工具，来研究其与另一种核糖体蛋白L7/L12、核糖体核心颗粒以及23S RNA之间的相互作用。发现L10的一个或多个精氨酸残基被修饰后，其核糖体和RNA结合能力受到抑制。这种处理并不影响L10在L7/L12-L10复合物中结合四个L7/L12分子的能力。我们的结果支持这样一种观点，即L10在促进L7/L12与核糖体结合中所起的作用主要归因于其同时结合23S RNA和L7/L12的能力。
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