依赖延伸因子Tu和核糖体蛋白L7/L12的鸟苷三磷酸酶活性
Guanosinetriphosphatase activity dependent on elongation factor Tu and ribosomal protein L7/L12.
作者信息
Donner D, Villems R, Liljas A, Kurland C G
出版信息
Proc Natl Acad Sci U S A. 1978 Jul;75(7):3192-5. doi: 10.1073/pnas.75.7.3192.
Abstract
Incubation of electrophoretically pure samples of the Escherichia coli 50S ribosomal protein L7/L12 together with elongation factor Tu leads to the hydrolysis of GTP. Addition of elongation factor Ts stimulates this reaction. Elongation factor G cannot replace elongation factor Tu for the ribosome-free GTPase reaction dependent on L7/L12. The data suggest that elongation factor Tu and the protein L7/L12 interact directly at the ribosomal A site.
摘要
将大肠杆菌50S核糖体蛋白L7/L12的电泳纯样品与延伸因子Tu一起温育会导致GTP水解。添加延伸因子Ts会刺激此反应。在依赖L7/L12的无核糖体GTP酶反应中，延伸因子G不能替代延伸因子Tu。数据表明延伸因子Tu和蛋白L7/L12在核糖体A位点直接相互作用。
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