真核核糖体
真核起始因子
核糖体蛋白
核糖体
细胞生物学
核糖体RNA
真核翻译
蛋白质亚单位
真核小核糖体亚单位
翻译(生物学)
生物
30岁
起始因子
化学
生物化学
核糖核酸
信使核糖核酸
基因
作者
Christopher P. Lapointe,Rosslyn Grosely,Masaaki Sokabe,Carlos Alvarado,Jinfan Wang,Elizabeth Montabana,Nancy Villa,Byung‐Sik Shin,Thomas E. Dever,Christopher S. Fraser,I.S. Fernandez,Joseph D. Puglisi
出处
期刊:Nature
[Springer Nature]
日期:2022-06-22
卷期号:607 (7917): 185-190
被引量:35
标识
DOI:10.1038/s41586-022-04858-z
摘要
Translation initiation defines the identity and quantity of a synthesized protein. The process is dysregulated in many human diseases1,2. A key commitment step is when the ribosomal subunits join at a translation start site on a messenger RNA to form a functional ribosome. Here, we combined single-molecule spectroscopy and structural methods using an in vitro reconstituted system to examine how the human ribosomal subunits join. Single-molecule fluorescence revealed when the universally conserved eukaryotic initiation factors eIF1A and eIF5B associate with and depart from initiation complexes. Guided by single-molecule dynamics, we visualized initiation complexes that contained both eIF1A and eIF5B using single-particle cryo-electron microscopy. The resulting structure revealed how eukaryote-specific contacts between the two proteins remodel the initiation complex to orient the initiator aminoacyl-tRNA in a conformation compatible with ribosomal subunit joining. Collectively, our findings provide a quantitative and architectural framework for the molecular choreography orchestrated by eIF1A and eIF5B during translation initiation in humans. Single-molecule spectroscopy and structural studies were used to examine the dynamics of association of eIF1A and eIF5B with the human translation initiation complex and their role in presenting tRNA to the complex to initiate translation.
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