A novel association between two trypanosome-specific factors and the conserved L5-5S rRNA complex.

A novel association between two trypanosome-specific factors and the conserved L5-5S rRNA complex.
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DOI:
10.1371/journal.pone.0041398
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发表时间:
2012
期刊:
影响因子:
3.7
通讯作者:
Williams N
Williams N
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Ciganda M;Prohaska K;Hellman K;Williams N

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P34和P37是先前在鞭毛原生动物布氏锥虫中鉴定出的两种RNA结合蛋白。RNA干扰研究已确定这些蛋白参与核糖体生物发生且对其至关重要。这些蛋白与5S rRNA相互作用,且结合特性几乎相同。我们已经表明这种相互作用主要是通过RNA的LoopA区域实现的,但P34和P37也保护位于LoopC上的L5结合位点。我们现在提供证据表明这些因子通过与5S rRNA和L5核糖体蛋白的相互作用形成一种新的核糖体前颗粒。对布氏锥虫L5进一步的计算机模拟和体外分析表明,基于其他真核生物的L5蛋白,它对5S rRNA的亲和力比预期的要低。我们假设P34和P37补充L5并在与5S rRNA的相互作用中起桥梁作用,使其稳定并有助于核糖体生物发生的早期步骤。
P34 and P37 are two previously identified RNA binding proteins in the flagellate protozoan Trypanosoma brucei. RNA interference studies have determined that the proteins are involved in and essential for ribosome biogenesis. The proteins interact with the 5S rRNA with nearly identical binding characteristics. We have shown that this interaction is achieved mainly through the LoopA region of the RNA, but P34 and P37 also protect the L5 binding site located on LoopC. We now provide evidence to show that these factors form a novel pre-ribosomal particle through interactions with both 5S rRNA and the L5 ribosomal protein. Further in silico and in vitro analysis of T. brucei L5 indicates a lower affinity for 5S rRNA than expected, based on other eukaryotic L5 proteins. We hypothesize that P34 and P37 complement L5 and bridge the interaction with 5S rRNA, stabilizing it and aiding in the early steps of ribosome biogenesis.