8C93

Cryo-EM captures early ribosome assembly in action

Summary for 8C93

• Entry DOI: 10.2210/pdb8c93/pdb
• EMDB information: 16500
• Descriptor: 23S rRNA, 50S ribosomal protein L23, 50S ribosomal protein L24, ... (17 entities in total)
• Functional Keywords: ribosome, ribosome assembly, ribosome biogenesis, total reconstitution, rna, ribosomal protein.
• Biological source: Escherichia coli; More
• Total number of polymer chains: 17
• Total formula weight: 1143819.91

Authors

Lauer, S.,Nikolay, R.,Qin, B. (deposition date: 2023-01-21, release date: 2023-04-05, Last modification date: 2024-07-24)

Primary citation

Qin, B.,Lauer, S.M.,Balke, A.,Vieira-Vieira, C.H.,Burger, J.,Mielke, T.,Selbach, M.,Scheerer, P.,Spahn, C.M.T.,Nikolay, R.
Cryo-EM captures early ribosome assembly in action.
Nat Commun, 14:898-898, 2023

PubMed 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.

PubMed: 36797249
DOI: 10.1038/s41467-023-36607-9

Experimental method

ELECTRON MICROSCOPY (4.17 Å)