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Potential Roles for Ubiquitin and the Proteasome during Ribosome Biogenesis

机译：泛素和蛋白酶体在核糖体生物发生过程中的潜在作用。

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We have investigated the possible involvement of the ubiquitin-proteasome system (UPS) in ribosome biogenesis. We find by immunofluorescence that ubiquitin is present within nucleoli and also demonstrate by immunoprecipitation that complexes associated with pre-rRNA processing factors are ubiquitinated. Using short proteasome inhibition treatments, we show by fluorescence microscopy that nucleolar morphology is disrupted for some but not all factors involved in ribosome biogenesis. Interference with proteasome degradation also induces the accumulation of 90S preribosomes, alters the dynamic properties of a number of processing factors, slows the release of mature rRNA from the nucleolus, and leads to the depletion of 18S and 28S rRNAs. Together, these results suggest that the UPS is probably involved at many steps during ribosome biogenesis, including the maturation of the 90S preribosome.
机译：我们已经研究了遍在蛋白-蛋白酶体系统（UPS）在核糖体生物发生中的可能参与。我们通过免疫荧光发现泛素存在于核仁中，并且还通过免疫沉淀证明与rRNA前加工因子相关的复合物被泛素化。使用短暂的蛋白酶体抑制处理，我们通过荧光显微镜显示，核糖体形态被某些但并非所有与核糖体生物发生有关的因素所破坏。蛋白酶体降解的干扰还诱导了90S前核糖体的积累，改变了许多加工因子的动力学特性，减缓了成熟rRNA从核仁中的释放，并导致18S和28S rRNA的消耗。总之，这些结果表明，UPS可能涉及核糖体生物发生的许多步骤，包括90S前核糖体的成熟。

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