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两种DNA结合蛋白对翻译调控的特异性

Specificity of translational regulation by two DNA-binding proteins.

作者信息

Fulford W, Model P

出版信息

J Mol Biol. 1984 Feb 25;173(2):211-26. doi: 10.1016/0022-2836(84)90190-6.

Abstract

The gene V protein of the filamentous bacteriophages fl, fd and M13, and the gene 32 protein of bacteriophage T4 share the property of binding strongly and co-operatively to single-stranded nucleic acids, especially DNA. Moreover, both are capable of repressing the translation of specific mRNAs (gene 32 protein its own, and gene V protein that of the filamentous phage gene II), both in vivo and in vitro. If the mechanism of repression by either of these proteins were based solely on its ability to bind single strands co-operatively, then the other would be expected to mimic or interfere with its effect in vitro. We have found no such mimicry or interference, even at protein concentrations high enough to have substantial non-specific effects on translation. This suggests that the sites of repression on the mRNAs must offer something other than simple "unstructuredness" for binding and repression to occur.

摘要

丝状噬菌体fl、fd和M13的基因V蛋白,以及噬菌体T4的基因32蛋白,具有与单链核酸(尤其是DNA)强烈且协同结合的特性。此外,二者在体内和体外均能抑制特定mRNA的翻译(基因32蛋白抑制其自身的翻译,基因V蛋白抑制丝状噬菌体基因II的翻译)。如果这两种蛋白中任一种的抑制机制仅基于其协同结合单链的能力,那么另一种蛋白有望在体外模拟或干扰其效应。但我们并未发现此类模拟或干扰现象,即便蛋白浓度高到足以对翻译产生显著的非特异性影响。这表明,mRNA上的抑制位点必定提供了除简单的“无结构状态”之外的其他因素,以便结合和抑制得以发生。

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