Clinical Neurobiology, institute of biomedical and Clinical Science, Peninsula College of Medicine and Dentistry, Exeter EX1 2LU, UK.
J Biochem. 2010 Jun;147(6):885-93. doi: 10.1093/jb/mvq025. Epub 2010 Mar 7.
The Ewing's sarcoma (EWS) protein is a ubiquitously expressed RNA chaperone. The EWS protein localizes predominantly to the nucleus. Previous reports have suggested that the EWS protein is capable of dimerizing. However, to date this has not been confirmed. Here, using a novel panel of recombinant proteins, we have performed an in vitro biomolecular interaction analysis of the EWS protein. We have demonstrated that all three arginine-glycine-glycine (RGG) motifs are capable of binding directly to the survival motor neuron protein, a Tudor domain containing EWS binding partner. We have also confirmed EWS is capable of self-associating, and we have mapped this binding domain to the RGG motifs. We have also found that self-association may be required for EWS nuclear import. This is the first direct evidence of RGG domains being involved in self-association and has implications on all RGG-containing proteins.
尤文肉瘤（EWS）蛋白是一种普遍表达的 RNA 伴侣。EWS 蛋白主要定位于细胞核。先前的报告表明，EWS 蛋白能够二聚化。然而，迄今为止，这一点尚未得到证实。在这里，我们使用一组新的重组蛋白，对 EWS 蛋白进行了体外生物分子相互作用分析。我们已经证明，所有三个精氨酸-甘氨酸-甘氨酸（RGG）基序都能够直接与生存运动神经元蛋白结合，生存运动神经元蛋白是一个含有 EWS 结合伙伴的结构域。我们还证实 EWS 能够自我缔合，并且我们已经将该结合结构域映射到 RGG 基序上。我们还发现，自我缔合可能是 EWS 核输入所必需的。这是 RGG 结构域参与自我缔合的第一个直接证据，对所有含有 RGG 的蛋白质都有影响。
