5' exoribonucleases, which functions in a variety of cellular processes, all requiring the processing or degradation of RNA. We demonstrate that the two human protein'/> Protein-protein interactions of hCsl4p with other human exosome subunits.
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Protein-protein interactions of hCsl4p with other human exosome subunits.

机译:hCsl4p与其他人类外泌体亚基的蛋白质-蛋白质相互作用。

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摘要

The exosome is a complex of 3'-->5' exoribonucleases, which functions in a variety of cellular processes, all requiring the processing or degradation of RNA. We demonstrate that the two human proteins hCsl4p and hRrp42p, which have been identified on the basis of their sequence homology with Saccharomyces cerevisiae proteins, are associated with the human exosome. By mammalian two-hybrid and GST pull-down assays, we show that the hCsl4p protein interacts directly with two other exosome proteins, hRrp42p and hRrp46p. Mutants of hCsl4p that fail to interact with either hRrp42p or hRrp46p are also not able to associate with exosome complexes in vivo. These results indicate that the association of hCsl4p with the exosome is mediated by protein-protein interactions with hRrp42p and hRrp46p.
机译:外泌体是3'-> 5'外切核糖核酸酶的复合物,其在多种细胞过程中起作用,所有这些过程都需要RNA的加工或降解。我们证明这两个人类蛋白质hCsl4p和hRrp42p,已根据其与酿酒酵母蛋白质的序列同源性确定,与人类外泌体相关。通过哺乳动物的双杂交和GST下拉检测,我们显示hCsl4p蛋白与其他两种外泌体蛋白hRrp42p和hRrp46p直接相互作用。无法与hRrp42p或hRrp46p相互作用的hCsl4p突变体也无法与体内外泌体复合物缔合。这些结果表明,hCsl4p与外泌体的缔合是通过与hRrp42p和hRrp46p的蛋白质相互作用来介导的。

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