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蛋白质L7/L12的二聚体状态与核糖体的EF-G依赖性反应。

Dimer state of protein L7/L12 and EF-G-dependent reactions of ribosomes.

作者信息

Koteliansky V E, Domogatsky S P, Gudkov A T

出版信息

Eur J Biochem. 1978 Oct;90(2):319-23. doi: 10.1111/j.1432-1033.1978.tb12607.x.

Abstract

A number of different monomer and dimer derivatives of protein L7/L12 has been studied in EF-G-dependent reactions on the ribosome. It has been shown that only dimer derivatives of protein L7/L12 are able to interact with the ribosome. This means that it is the dimer forms of protein L7/L12 that are present in the functionally active ribosome. It is likely that the N-terminal sequence of protein L7/L12 is responsible for dimerization of the protein in solution and at the same time contributes mainly to the interaction of the protein L7/L12 dimer with the ribosome. The results obtained suggest that there are four copies of protein L7/L12 in the translating ribosome.

摘要

已经在核糖体上依赖EF-G的反应中研究了蛋白质L7/L12的多种不同单体和二聚体衍生物。结果表明,只有蛋白质L7/L12的二聚体衍生物能够与核糖体相互作用。这意味着在功能活跃的核糖体中存在的是蛋白质L7/L12的二聚体形式。蛋白质L7/L12的N端序列可能负责该蛋白质在溶液中的二聚化,同时主要有助于蛋白质L7/L12二聚体与核糖体的相互作用。所得结果表明,在进行翻译的核糖体中有四个蛋白质L7/L12拷贝。

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