8c91

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Cryo-EM captures early ribosome assembly in action

Structural highlights

8c91 is a 10 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 4.19Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RL2_ECOLI One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial.[HAMAP-Rule:MF_01320_B] In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G.[HAMAP-Rule:MF_01320_B]

Publication Abstract from PubMed

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.

Cryo-EM captures early ribosome assembly in action.,Qin B, Lauer SM, Balke A, Vieira-Vieira CH, Burger J, Mielke T, Selbach M, Scheerer P, Spahn CMT, Nikolay R Nat Commun. 2023 Feb 17;14(1):898. doi: 10.1038/s41467-023-36607-9. PMID:36797249[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
2 reviews cite this structure
Emerging Quantitative Biochemical, Structural, and Biophysical Methods for Studying Ribosome and Protein-RNA Complex Assembly.
Gor et al. (2023)
1 more
7 other articles
No citations found

See Also

References

  1. ↑ Qin B, Lauer SM, Balke A, Vieira-Vieira CH, Bürger J, Mielke T, Selbach M, Scheerer P, Spahn CMT, Nikolay R. Cryo-EM captures early ribosome assembly in action. Nat Commun. 2023 Feb 17;14(1):898. PMID:36797249 doi:10.1038/s41467-023-36607-9

Contents


PDB ID 8c91

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OCA

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