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参与与延伸因子G相互作用的核糖体蛋白的鉴定。

Identity of the ribosomal proteins involved in the interaction with elongation factor G.

作者信息

Highland J H, Bodley J W, Gordon J, Hasenbank R, Stöffler G

出版信息

Proc Natl Acad Sci U S A. 1973 Jan;70(1):147-50. doi: 10.1073/pnas.70.1.147.

Abstract

Rabbit antibodies produced against 50 of the 55 individually purified ribosomal proteins of Escherichia coli were tested for their ability to interfere with the formation of the ribosome.EF-G.GDP complex. Only antibodies produced against proteins L7 and L12 inhibited complex formation, and they did so completely. These two proteins were previously shown to be immunologically indistinguishable and necessary for the interaction between ribosomes and EF-G. The present data are consistent with the view that the interaction between ribosomes and EF-G that results in GTP hydrolysis occurs on, and is limited to, proteins L7 and L12 on the surface of the 50S ribosomal subunit.

摘要

针对大肠杆菌55种单独纯化的核糖体蛋白中的50种产生的兔抗体,被检测其干扰核糖体-EF-G·GDP复合物形成的能力。只有针对蛋白L7和L12产生的抗体抑制复合物形成,且完全抑制。此前已表明这两种蛋白在免疫学上无法区分,并且对于核糖体与EF-G之间的相互作用是必需的。目前的数据与以下观点一致:导致GTP水解的核糖体与EF-G之间的相互作用发生在50S核糖体亚基表面的蛋白L7和L12上,且仅限于此。

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Protein biosynthesis.蛋白质生物合成
Annu Rev Biochem. 1971;40:409-48. doi: 10.1146/annurev.bi.40.070171.002205.

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