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Proteins binding to 5' untranslated region sites: a general mechanism for translational regulation of mRNAs in human and yeast cells.

机译:结合5'非翻译区位点的蛋白质:在人类和酵母细胞中翻译调节mRNA的一般机制。

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摘要

We demonstrate that a bacteriophage protein and a spliceosomal protein can be converted into eukaryotic translational repressor proteins. mRNAs with binding sites for the bacteriophage MS2 coat protein or the spliceosomal human U1A protein were expressed in human HeLa cells and yeast. The presence of the appropriate binding protein resulted in specific, dose-dependent translational repression when the binding sites were located in the 5' untranslated region (UTR) of the reporter mRNAs. Neither mRNA export from the nucleus to the cytoplasm nor mRNA stability was demonstrably affected by the binding proteins. The data thus reveal a general mechanism for translational regulation: formation of mRNA-protein complexes in the 5' UTR controls translation initiation by steric blockage of a sensitive step in the initiation pathway. Moreover, the findings establish the basis for novel strategies to study RNA-protein interactions in vivo and to clone RNA-binding proteins.
机译:我们证明了噬菌体蛋白和剪接体蛋白可以转化为真核翻译阻遏蛋白。带有噬菌体MS2外壳蛋白或剪接体人U1A蛋白结合位点的mRNA在人HeLa细胞和酵母中表达。当结合位点位于报道基因mRNA的5'非翻译区(UTR)时,适当结合蛋白的存在导致特异性的,剂量依赖性的翻译抑制。结合蛋白既没有显示出mRNA从细胞核输出到细胞质,也没有显示出mRNA的稳定性。因此,数据揭示了翻译调节的一般机制:5'UTR中mRNA-蛋白质复合物的形成通过起始途径中敏感步骤的空间阻滞来控制翻译起始。而且,这些发现为研究体内RNA-蛋白质相互作用和克隆RNA结合蛋白的新策略奠定了基础。

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