Evidence map›Paper›PMID 31665744›Full record

ArticleNucleic acids research2019

Structural consequences of the interaction of RbgA with a 50S ribosomal subunit assembly intermediate.

Amal Seffouh, Nikhil Jain, Dushyant Jahagirdar, Kaustuv Basu, Aida Razi, Xiaodan Ni, Alba Guarné, Robert A Britton, Joaquin Ortega

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.7field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

31 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. The late stages of yeast mitoribosome large subunit biogenesis.Biochimica et biophysica acta. Molecular cell research · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Complete list of canonical post-transcriptional modifications in thebioRxiv : the preprint server for biology · 2024
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 2 countries.

Amal SeffouhDepartment of Anatomy and Cell Biology, McGill University, Montreal, Quebec H3A 0C7, Canada.
Nikhil JainDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX 77030, USA.
Dushyant JahagirdarDepartment of Anatomy and Cell Biology, McGill University, Montreal, Quebec H3A 0C7, Canada.
Kaustuv BasuDepartment of Anatomy and Cell Biology, McGill University, Montreal, Quebec H3A 0C7, Canada.
Aida RaziDepartment of Anatomy and Cell Biology, McGill University, Montreal, Quebec H3A 0C7, Canada.
Xiaodan NiDepartment of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario L8S 4K1, Canada.
Alba GuarnéDepartment of Biochemistry, McGill University, Montreal, Quebec H3G 0B1, Canada.
Robert A BrittonDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX 77030, USA.
Joaquin OrtegaDepartment of Anatomy and Cell Biology, McGill University, Montreal, Quebec H3A 0C7, Canada.
McGill University · CABaylor College of Medicine · USMcMaster University · CA

Funding

GTPase control of large ribosome subunit biogenesisR01GM110248 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI BRITTON, ROBERT A · 2015 to 2018
$1.5M
NIGMS NIH HHS R01 GM110248
6 · The paper itself

Abstract

Bacteria harbor a number GTPases that function in the assembly of the ribosome and are essential for growth. RbgA is one of these GTPases and is required for the assembly of the 50S subunit in most bacteria. Homologs of this protein are also implicated in the assembly of the large subunit of the mitochondrial and eukaryotic ribosome. We present here the cryo-electron microscopy structure of RbgA bound to a Bacillus subtilis 50S subunit assembly intermediate (45SRbgA particle) that accumulates in cells upon RbgA depletion. Binding of RbgA at the P site of the immature particle stabilizes functionally important rRNA helices in the A and P-sites, prior to the completion of the maturation process of the subunit. The structure also reveals the location of the highly conserved N-terminal end of RbgA containing the catalytic residue Histidine 9. The derived model supports a mechanism of GTP hydrolysis, and it shows that upon interaction of RbgA with the 45SRbgA particle, Histidine 9 positions itself near the nucleotide potentially acting as the catalytic residue with minimal rearrangements. This structure represents the first visualization of the conformational changes induced by an assembly factor in a bacterial subunit intermediate.

Indexed as

Bacillus subtilisCryoelectron MicroscopyGTP PhosphohydrolasesHydrolysisModels, MolecularProtein ConformationRibosomal ProteinsRibosomesRibosome Subunits, Large, BacterialRNA, RibosomalGTP PhosphohydrolasesRibosomal ProteinsRNA, Ribosomal

Identifiers

PMID31665744
PMCPMC6821245
OpenAlexW2971693965

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.