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RNA-Binding Properties of the Plant Protein Nt-4/1

机译:植物蛋白Nt-4 / 1的RNA结合特性。

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摘要

The tobacco a-helical protein Nt-4/1 with unknown function forms ribonucleoprotein (RNP) complexes in vitro. Results obtained by retardation of RNP complexes in agarose gel were confirmed by Western—Northern hybridization. Several deletion and point mutants of Nt-4/1 were constructed, and the RNA-binding site was mapped in a positively charged region of the C-terminal domain of the protein. The results of this study and those described earlier support our hypothesis of the participation of Nt-4/1 protein in spreading RNA-containing pathogens in the plant.
机译:功能未知的烟草α-螺旋蛋白Nt-4 / 1在体外形成核糖核蛋白(RNP)复合物。 Western-Northern杂交证实了琼脂糖凝胶中RNP复合物阻滞所获得的结果。构建了几个Nt-4 / 1的缺失和点突变体,并将RNA结合位点定位在蛋白质C端结构域的带正电荷的区域。这项研究的结果以及先前所述的结果支持了我们的假设,即Nt-4 / 1蛋白参与了植物中含RNA传播的病原体的传播。

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