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通过识别β-微管蛋白新生的氨基末端实现β-微管蛋白mRNA的自调节不稳定性。

Autoregulated instability of beta-tubulin mRNAs by recognition of the nascent amino terminus of beta-tubulin.

作者信息

Yen T J, Machlin P S, Cleveland D W

机构信息

Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.

出版信息

Nature. 1988 Aug 18;334(6183):580-5. doi: 10.1038/334580a0.

Abstract

Tubulin synthesis in animal cells is controlled by an autoregulatory mechanism that modulates the stability of polysome-bound tubulin messenger RNAs. The beta-tubulin RNAs are selectively targeted as substrates for destabilization not through the recognition of specific RNA sequences, but rather through co-translational recognition of the amino-terminal beta-tubulin tetrapeptide after its emergence from the ribosome. This motif is likely to be used in other systems where RNA degradation is coupled to ribosome attachment and translation.

摘要

动物细胞中的微管蛋白合成受一种自动调节机制控制,该机制可调节与多核糖体结合的微管蛋白信使核糖核酸的稳定性。β-微管蛋白核糖核酸被选择性地作为去稳定化的底物,其并非通过识别特定的核糖核酸序列,而是在氨基末端β-微管蛋白四肽从核糖体出现后通过共翻译识别来实现。这种基序可能在其他核糖核酸降解与核糖体附着及翻译相偶联的系统中也有应用。

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