Defining the pathway of cytoplasmic maturation of the 60S ribosomal subunit.

Defining the pathway of cytoplasmic maturation of the 60S ribosomal subunit.
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DOI:
10.1016/j.molcel.2010.06.018
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发表时间:
2010-07-30
期刊:
影响因子:
16
通讯作者:
Johnson AW
Johnson AW
中科院分区:
生物学1区
文献类型:
--
作者:
Lo KY;Li Z;Bussiere C;Bresson S;Marcotte EM;Johnson AW

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在真核细胞中,核糖体的最终成熟发生在细胞质中,其中反式作用因子被去除,关键的核糖体蛋白被添加以发挥功能。在这里,我们对细胞质成熟进行了全面的分析,将已知的步骤排列成一个连贯的途径。成熟是由atp酶Drg1启动的。下游,核糖体柄的组装对Tif6的释放至关重要。茎在翻译过程中吸收gtp酶。由于释放Tif6所需的GTPase Efl1与翻译伸长因子eEF2相似,我们认为茎秆的组装会招募Efl1,从而触发60S生物发生过程中模仿易位的一个步骤。因此,Efl1可以提供一种功能检查新生亚基的机制。最后,Tif6的发布是核出口适配器Nmd3发布的先决条件。建立这一途径为理解核糖体成熟提供了一个重要的概念框架。
In eukaryotic cells the final maturation of ribosomes occurs in the cytoplasm, where trans-acting factors are removed and critical ribosomal proteins are added for functionality. Here, we have carried out a comprehensive analysis of cytoplasmic maturation, ordering the known steps into a coherent pathway. Maturation is initiated by the ATPase Drg1. Downstream, assembly of the ribosome stalk is essential for the release of Tif6. The stalk recruits GTPases during translation. Because the GTPase Efl1, which is required for the release of Tif6, resembles the translation elongation factor eEF2, we suggest that assembly of the stalk recruits Efl1, triggering a step in 60S biogenesis that mimics aspects of translocation. Efl1 could thereby provide a mechanism to functionally check the nascent subunit. Finally, the release of Tif6 is a prerequisite for the release of the nuclear export adapter Nmd3. Establishing this pathway provides an important conceptual framework for understanding ribosome maturation.
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