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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Targeted modification and transportation of cellular proteins
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Targeted modification and transportation of cellular proteins

机译：细胞蛋白的靶向修饰和转运

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Peptide aptamers are proteins selected from combinatorial li- braries that display conformationally constrained variable re- gions. Peptide aptamers can disrupt specific protein interactions and thus represent a useful method for manipulating protein functian in vivo. Here, we describe aptamer derivatives that extend the range of functional manipulations. We isolated an aptamer with increased affinity for its Cdk2 target by mu- tagenizing an existing aptamer and identifying tighter binding mutants with calibrated two-hybrid reporter genes. We used this and other anti-Cdk2 aptamers as recognition domains in chimeric proteins that contained other functional moieties. Aptamers fused to the catalytic domain of a ubiquitin ligase specifically decorated LexA-Cdk2 with ubiquitin moieties in vivo. Aptamers against Cdk2 and another protein, Ste5. that carried a nuclear localization sequence transported their targets into the nucleus. These experiments indicate that fusion proteins con- taining aptameric recognition moieties will be useful for specific modification of protein function in vivo.
机译：肽适体是选自组合文库的蛋白，其显示构象受限的可变区。肽适体可以破坏特定的蛋白质相互作用，因此代表了一种在体内操纵蛋白质功能的有用方法。在这里，我们描述了适体衍生物，扩展了功能操纵的范围。我们通过对现有的适体进行诱变并用校准的双杂交报告基因鉴定出更紧密的结合突变体，从而分离出了对其Cdk2靶具有更高亲和力的适体。我们使用此和其他抗Cdk2适体作为包含其他功能部分的嵌合蛋白中的识别域。融合至泛素连接酶催化结构域的适体在体内用泛素部分特异性修饰了LexA-Cdk2。针对Cdk2和另一种蛋白质Ste5的适体。携带核定位序列的分子将其靶标转运到核中。这些实验表明，包含适体识别部分的融合蛋白可用于体内蛋白质功能的特异性修饰。

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