Potential roles for ubiquitin and the proteasome during ribosome biogenesis
Potential roles for ubiquitin and the proteasome during ribosome biogenesis
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DOI：
10.1128/mcb.02227-05
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发表时间：
2006-07-01
影响因子：
5.3
通讯作者：
McNally, James G.
中科院分区：
文献类型：
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作者：
Stavreva, Diana A.;Kawasaki, Miyuki;McNally, James G.
我们已经研究了泛素-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内，并通过免疫沉淀证明与前rrna加工因子相关的复合物是泛素化的。使用短时间蛋白酶体抑制处理，我们通过荧光显微镜显示核仁形态被一些但不是所有参与核糖体生物发生的因素破坏。对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态特性，减缓了核核中成熟rRNA的释放，并导致18S和28S rRNA的消耗。总之，这些结果表明UPS可能参与了核糖体生物发生的许多步骤，包括90S前核糖体的成熟。
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.