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首页> 外文期刊>Molecular and Cellular Biology >Interdependence of Pes1, Bop1, and WDR12 Controls Nucleolar Localization and Assembly of the PeBoW Complex Required for Maturation of the 60S Ribosomal Subunit
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Interdependence of Pes1, Bop1, and WDR12 Controls Nucleolar Localization and Assembly of the PeBoW Complex Required for Maturation of the 60S Ribosomal Subunit

机译：Pes1，Bop1和WDR12的相互依赖性控制60S核糖体亚基成熟所需的PeBoW复合物的核仁定位和组装。

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The PeBoW complex is essential for cell proliferation and maturation of the large ribosomal subunit in mammalian cells. Here we examined the role of PeBoW-specific proteins Pes1, Bop1, and WDR12 in complex assembly and stability, nucleolar transport, and preribosome association. Recombinant expression of the three subunits is sufficient for complex formation. The stability of all three subunits strongly increases upon incorporation into the complex. Only overexpression of Bop1 inhibits cell proliferation and rRNA processing, and its negative effects could be rescued by coexpression of WDR12, but not Pes1. Elevated levels of Bop1 induce Bop1/WDR12 and Bop1/Pes1 subcomplexes. Knockdown of Bop1 abolishes the copurification of Pes1 with WDR12, demonstrating Bop1 as the integral component of the complex. Overexpressed Bop1 substitutes for endogenous Bop1 in PeBoW complex assembly, leading to the instability of endogenous Bop1. Finally, indirect immunofluorescence, cell fractionation, and sucrose gradient centrifugation experiments indicate that transport of Bop1 from the cytoplasm to the nucleolus is Pes1 dependent, while Pes1 can migrate to the nucleolus and bind to preribosomal particles independently of Bop1. We conclude that the assembly and integrity of the PeBoW complex are highly sensitive to changes in Bop1 protein levels.
机译：PeBoW复合物对于哺乳动物细胞中大核糖体亚基的细胞增殖和成熟至关重要。在这里，我们检查了PeBoW特异性蛋白Pes1，Bop1和WDR12在复杂的组装和稳定性，核仁转运和核糖体缔合中的作用。三个亚基的重组表达足以形成复合物。当掺入复合物中时，所有三个亚基的稳定性都大大提高。只有Bop1的过表达抑制细胞增殖和rRNA加工，并且WDR12的共表达可以挽救其负面影响，而Pes1不能。 Bop1水平升高会诱导Bop1 / WDR12和Bop1 / Pes1亚复合体。击倒Bop1可取消Pes1与WDR12的共纯化，证明Bop1是复合物的组成部分。过表达的Bop1在PeBoW复杂装配中替代了内源性Bop1，导致内源性Bop1不稳定。最后，间接免疫荧光，细胞分级分离和蔗糖梯度离心实验表明，Bop1从细胞质到核仁的转运是Pes1依赖性的，而Pes1可以迁移到核仁并独立于Bop1结合至核糖体颗粒。我们得出的结论是，PeBoW复合物的组装和完整性对​​Bop1蛋白水平的变化高度敏感。

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