Utp14 interaction with the small subunit processome.
Utp14 interaction with the small subunit processome.
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DOI：
10.1261/rna.066373.118
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发表时间：
2018-09
期刊：
影响因子：
--
通讯作者：
Johnson AW
中科院分区：
文献类型：
--
作者：
Black JJ;Wang Z;Goering LM;Johnson AW
SSU过程体（有时被称为90S）是真核生物小核糖体亚基生物发生途径的早期稳定中间体。SSU过程向40s前颗粒的进展需要RNA的大规模压实和许多生物发生因子的释放。U3 snoRNA是SSU加工体的主要组成部分，并在多个位置与rRNA杂交以组织SSU加工体的结构。因此，U3的释放是过渡到40s前的先决条件。我们的实验室提出，RNA解旋酶Dhr1在通过解绕U3的转变中起着至关重要的作用，并且这种活性是由SSU过程蛋白Utp14控制的。Utp14如何激活Dhr1是一个悬而未决的问题。尽管高度保守，但Utp14不包含可识别的结构域，并且Utp14如何与SSU过程相互作用尚未得到很好的表征。在这里，我们使用紫外交联和分析cDNA （CRAC）和酵母双杂交相互作用来表征Utp14如何与前核糖体相互作用。此外，缺乏Utp14的SSU颗粒的蛋白质组学分析显示，Utp14的存在是RNA外泌体有效募集所必需的。我们的分析表明，Utp14具有独特的定位，可以将SSU过程的组装状态传递给Dhr1，也可能传递给外泌体。
The SSU processome (sometimes referred to as 90S) is an early stable intermediate in the small ribosomal subunit biogenesis pathway of eukaryotes. Progression of the SSU processome to a pre-40S particle requires a large-scale compaction of the RNA and release of many biogenesis factors. The U3 snoRNA is a primary component of the SSU processome and hybridizes to the rRNA at multiple locations to organize the structure of the SSU processome. Thus, release of U3 is a prerequisite for the transition to pre-40S. Our laboratory proposed that the RNA helicase Dhr1 plays a crucial role in the transition by unwinding U3 and that this activity is controlled by the SSU processome protein Utp14. How Utp14 times the activation of Dhr1 is an open question. Despite being highly conserved, Utp14 contains no recognizable domains, and how Utp14 interacts with the SSU processome is not well characterized. Here, we used UV crosslinking and analysis of cDNA (CRAC) and yeast two-hybrid interaction to characterize how Utp14 interacts with the preribosome. Moreover, proteomic analysis of SSU particles lacking Utp14 revealed that the presence of Utp14 is needed for efficient recruitment of the RNA exosome. Our analysis positions Utp14 to be uniquely poised to communicate the status of assembly of the SSU processome to Dhr1 and possibly to the exosome as well.
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