美国斯克里普斯研究所James R. Williamson与斯坦福大学Joseph D. Puglisi等研究人员合作发现，短暂的蛋白质与RNA相互作用引导新生的核糖体RNA的折叠。这一研究成果于2019年11月21日在线发表在国际学术期刊《细胞》上。

使用单分子荧光显微镜，研究人员实时跟踪了细菌小核糖体亚基的整个3'结构域。研究人员发现共转录rRNA折叠是通过远程RNA相互作用的形成而变得复杂，并且r蛋白在稳定掺入核糖核蛋白（RNP）复合物中之前会自促进rRNA折叠过程。组装是由瞬时而非稳定的蛋白质结合开始的，并且蛋白质与RNA的结合动态在组装过程中逐渐降低。

这项工作挑战了严格顺序和协作核糖体组装的模型，并认为RNA结合蛋白与细胞RNA的瞬时结合可以提供一种在RNP组装过程中改变新生RNA折叠的通用机制。

据介绍，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。理解新生的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。

附：英文原文

Title: Transient Protein-RNA Interactions Guide Nascent Ribosomal RNA Folding

Author: Olivier Duss, Galina A. Stepanyuk, Joseph D. Puglisi, James R. Williamson

Issue&Volume: November 21, 2019

Abstract: Ribosome assembly is an efficient but complex and heterogeneous process during whichribosomal proteins assemble on the nascent rRNA during transcription. Understandinghow the interplay between nascent RNA folding and protein binding determines the fateof transcripts remains a major challenge. Here, using single-molecule fluorescencemicroscopy, we follow assembly of the entire 3′ domain of the bacterial small ribosomalsubunit in real time. We find that co-transcriptional rRNA folding is complicatedby the formation of long-range RNA interactions and that r-proteins self-chaperonethe rRNA folding process prior to stable incorporation into a ribonucleoprotein (RNP)complex. Assembly is initiated by transient rather than stable protein binding, andthe protein-RNA binding dynamics gradually decrease during assembly. This work questionsthe paradigm of strictly sequential and cooperative ribosome assembly and suggeststhat transient binding of RNA binding proteins to cellular RNAs could provide a generalmechanism to shape nascent RNA folding during RNP assembly.

DOI: 10.1016/j.cell.2019.10.035

Source: https://www.cell.com/cell/fulltext/S0092-8674(19)31212-7