Transient Protein-RNA Interactions Guide Nascent Ribosomal RNA Folding.,Cell

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Transient Protein-RNA Interactions Guide Nascent Ribosomal RNA Folding.
Cell ( IF 45.5 ) Pub Date : 2019-11-21 , DOI: 10.1016/j.cell.2019.10.035
Olivier Duss ₁ , Galina A Stepanyuk ₂ , Joseph D Puglisi ₃ , James R Williamson ₂

Affiliation

Ribosome assembly is an efficient but complex and heterogeneous process during which ribosomal proteins assemble on the nascent rRNA during transcription. Understanding how the interplay between nascent RNA folding and protein binding determines the fate of transcripts remains a major challenge. Here, using single-molecule fluorescence microscopy, we follow assembly of the entire 3' domain of the bacterial small ribosomal subunit in real time. We find that co-transcriptional rRNA folding is complicated by the formation of long-range RNA interactions and that r-proteins self-chaperone the rRNA folding process prior to stable incorporation into a ribonucleoprotein (RNP) complex. Assembly is initiated by transient rather than stable protein binding, and the protein-RNA binding dynamics gradually decrease during assembly. This work questions the paradigm of strictly sequential and cooperative ribosome assembly and suggests that transient binding of RNA binding proteins to cellular RNAs could provide a general mechanism to shape nascent RNA folding during RNP assembly.

中文翻译：

瞬时蛋白质-RNA相互作用指导新生核糖体RNA折叠。

核糖体装配是一种有效但复杂且异质的过程，在此过程中，核糖体蛋白在转录过程中会装配在新生rRNA上。了解新生的RNA折叠与蛋白质结合之间的相互作用如何决定转录本的命运仍然是一个重大挑战。在这里，使用单分子荧光显微镜，我们实时跟踪细菌小核糖体亚基的整个3'结构域。我们发现共转录rRNA折叠是由远程RNA相互作用的形成而复杂的，并且r蛋白在稳定掺入核糖核蛋白（RNP）复合物中之前会自我陪伴rRNA折叠过程。组装是由瞬时而不是稳定的蛋白质结合开始的，并且蛋白质-RNA的结合动力学在组装过程中逐渐降低。

更新日期：2019-11-22

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