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Cryo-EM captures early ribosome assembly in action

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Item Type:Article
Title:Cryo-EM captures early ribosome assembly in action
Creators Name:Qin, B. and Lauer, S.M. and Balke, A. and Vieira-Vieira, C.H. and Bürger, J. and Mielke, T. and Selbach, M. and Scheerer, P. and Spahn, C.M.T. and Nikolay, R.
Abstract:Ribosome biogenesis is a fundamental multi-step cellular process in all domains of life that involves the production, processing, folding, and modification of ribosomal RNAs (rRNAs) and ribosomal proteins. To obtain insights into the still unexplored early assembly phase of the bacterial 50S subunit, we exploited a minimal in vitro reconstitution system using purified ribosomal components and scalable reaction conditions. Time-limited assembly assays combined with cryo-EM analysis visualizes the structurally complex assembly pathway starting with a particle consisting of ordered density for only ~500 nucleotides of 23S rRNA domain I and three ribosomal proteins. In addition, our structural analysis reveals that early 50S assembly occurs in a domain-wise fashion, while late 50S assembly proceeds incrementally. Furthermore, we find that both ribosomal proteins and folded rRNA helices, occupying surface exposed regions on pre-50S particles, induce, or stabilize rRNA folds within adjacent regions, thereby creating cooperativity.
Keywords:23S Ribosomal RNA, Cryoelectron Microscopy, Nucleotides, Ribosomal Proteins, Ribosomes
Source:Nature Communications
Publisher:Nature Publishing Group
Page Range:898
Date:17 February 2023
Official Publication:https://doi.org/10.1038/s41467-023-36607-9
PubMed:View item in PubMed

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