Ribosome assembly factors prevent premature translation initiation by 40S assembly intermediates.

Ribosome assembly factors prevent premature translation initiation by 40S assembly intermediates.
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DOI:
10.1126/science.1208245
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发表时间:
2011-09-09
期刊:
Science (New York, N.Y.)
影响因子:
--
通讯作者:
Skiniotis G
Skiniotis G
中科院分区:
其他
文献类型:
--
作者:
Strunk BS;Loucks CR;Su M;Vashisth H;Cheng S;Schilling J;Brooks CL 3rd;Karbstein K;Skiniotis G

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真核生物中的核糖体组装需要大约200个必需的组装因子(AF),并且通过在核仁中起始并在细胞质中达到高潮的有序事件发生。在这里,我们展示了来自酿酒酵母的晚期细胞质40 S核糖体组装中间体的冷冻电子显微镜(cryo-EM)结构。使用缺乏单个组分的前核糖体复合物的冷冻-EM重建来定义结合的AF的位置。所有七个AF的位置,以防止翻译起始途径中的每一步,通过阻断起始因子的结合位点,通过阻止mRNA通道的开放,通过阻断60 S亚基连接,并通过破坏解码位点。我们认为,这些高度冗余的机制,确保前40 S颗粒不进入翻译途径,这将导致其快速降解。40 S成熟的调节的影响进行了讨论。
Ribosome assembly in eukaryotes requires approximately 200 essential assembly factors (AFs), and occurs via ordered events that initiate in the nucleolus and culminate in the cytoplasm. Here we present the cryo-electron microscopy (cryo-EM) structure of a late cytoplasmic 40S ribosome assembly intermediate from Saccharomyces cerevisiae. The positions of bound AFs were defined using cryo-EM reconstructions of pre-ribosomal complexes lacking individual components. All seven AFs are positioned to prevent each step in the translation initiation pathway by obstructing the binding sites for initiation factors, by preventing the opening of the mRNA channel, by blocking 60S subunit joining, and by disrupting the decoding site. We suggest that these highly redundant mechanisms ensure that pre-40S particles do not enter the translation pathway, which would result in their rapid degradation. Implications for the regulation of 40S maturation are also discussed.
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40S 前后期核糖体内的蛋白质-蛋白质相互作用。
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