Identification of a self-association domain in the Ewing's sarcoma protein: a novel function for arginine-glycine-glycine rich motifs?
Identification of a self-association domain in the Ewing's sarcoma protein: a novel function for arginine-glycine-glycine rich motifs?
复制标题
尤文氏肉瘤蛋白中自关联结构域的鉴定：富含精氨酸-甘氨酸-甘氨酸基序的新功能？
DOI：
10.1093/jb/mvq025
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发表时间：
2010
影响因子：
2.7
通讯作者：
Young,PhilipJ
中科院分区：
文献类型：
--
作者：
Shaw,DebraJ;Morse,Robert;Todd,AdrianG;Eggleton,Paul;Lorson,ChristianL;Young,PhilipJ
尤文肉瘤(EWS)蛋白是一种普遍表达的RNA伴侣蛋白。EWS蛋白主要定位于细胞核。此前的报道表明，EWS蛋白能够二聚化。然而，到目前为止，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。我们已经证明了所有三个精氨酸-甘氨酸-甘氨酸(RGG)基序都能够直接与存活运动神经元蛋白结合，后者是一个含有EWS结合伙伴的Tudor结构域。我们还证实了EWS具有自结合的能力，并将该结合结构域映射到RGG基序。我们还发现，EWS核进口可能需要自缔合。这是RGG结构域参与自结合的第一个直接证据，并对所有含有RGG的蛋白质都有影响。
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 anin vitrobiomolecular 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.