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HSP90 Protein Stabilizes Unloaded Argonaute Complexes and Microscopic P-bodies in Human Cells

机译:HSP90蛋白可稳定人细胞中未装载的Argonaute复合物和微观P体

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Key components of the miRNA-mediated gene regulation pathway are localized in cytoplasmic processing bodies (P-bodies). Mounting evidence suggests that the presence of microscopic P-bodies are not always required for miRNA-mediated gene regulation. Here we have shown that geldanamycin, a well-characterized HSP90 inhibitor, abolishes P-bodies and significantly reduces Argonaute and GW182 protein levels but does not affect the miRNA level and the efficiency of miRNA-mediated gene repression; however, it significantly impairs siRNA loading and the efficacy of exogenous siRNA. Our data suggests that HSP90 protein chaperones Argonautes before binding RNA and may facilitate efficient loading of small RNA.
机译:miRNA介导的基因调控途径的关键成分位于细胞质加工体(P体)中。越来越多的证据表明,miRNA介导的基因调控并不总是需要存在微观P体。在这里,我们显示了良好表征的HSP90抑制剂格尔德霉素可废除P体并显着降低Argonaute和GW182蛋白水平,但不影响miRNA水平和miRNA介导的基因阻遏效率。但是,它显着削弱了siRNA的装载量和外源siRNA的功效。我们的数据表明,在结合RNA之前,HSP90蛋白伴侣可能是Argonautes,并且可能有助于有效装载小RNA。

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