Evidence map›Paper›PMID 23700310›Full record

ArticleNucleic acids research2013

Cryo-EM structures of the late-stage assembly intermediates of the bacterial 50S ribosomal subunit.

Ningning Li, Yuling Chen, Qiang Guo, Yixiao Zhang, Yi Yuan, Chengying Ma, Haiteng Deng, Jianlin Lei, Ning Gao

Abstract read
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Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

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46citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

46 citing papers in PubMed.

  1. Article
  2. Article
  3. Autonomous ribosome biogenesis in vitro.Nature communications · 2025
    Article
  4. A roadmap for ribosome assembly in human mitochondria.Nature structural & molecular biology · 2024
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
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  11. Article
  12. Article
  13. Structural basis for the activation of the DEAD-box RNA helicase DbpA by the nascent ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Article
  15. Article
  16. Review
  17. Article
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  20. Article
4 · The record

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5 · Who and what money

Authors and funding

9 authors.

Ningning LiMinistry of Education Key Laboratory of Protein Sciences, Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Yuling Chen
Qiang Guo
Yixiao Zhang
Yi Yuan
Chengying Ma
Haiteng Deng
Jianlin Lei
Ning Gao

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribosome assembly is a process fundamental for all cellular activities. The efficiency and accuracy of the subunit assembly are tightly regulated and closely monitored. In the present work, we characterized, both compositionally and structurally, a set of in vivo 50S subunit precursors (45S), isolated from a mutant bacterial strain. Our qualitative mass spectrometry data indicate that L28, L16, L33, L36 and L35 are dramatically underrepresented in the 45S particles. This protein spectrum shows interesting similarity to many qualitatively analyzed 50S precursors from different genetic background, indicating the presence of global rate-limiting steps in the late-stage assembly of 50S subunit. Our structural data reveal two major intermediate states for the 45S particles. Consistently, both states severally lack those proteins, but they also differ in the stability of the functional centers of the 50S subunit, demonstrating that they are translationally inactive. Detailed analysis indicates that the orientation of H38 accounts for the global conformational differences in these intermediate structures, and suggests that the reorientation of H38 to its native position is rate-limiting during the late-stage assembly. Especially, H38 plays an essential role in stabilizing the central protuberance, through the interaction with the 5S rRNA, and the correctly orientated H38 is likely a prerequisite for further maturation of the 50S subunit.

Indexed as

Cryoelectron MicroscopyGTP PhosphohydrolasesModels, MolecularRibosome Subunits, Large, BacterialRNA, Ribosomal, 23SGTP PhosphohydrolasesRNA, Ribosomal, 23S

Identifiers

PMID23700310
PMCPMC3737534

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.