Evidence map›Paper›PMID 35141754›Full record

ArticleNucleic acids research2022

RbgA ensures the correct timing in the maturation of the 50S subunits functional sites.

Amal Seffouh, Chirstian Trahan, Tanzila Wasi, Nikhil Jain, Kaustuv Basu, Robert A Britton, Marlene Oeffinger, Joaquin Ortega

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.0field-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

14 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
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  9. Complete list of canonical post-transcriptional modifications in thebioRxiv : the preprint server for biology · 2024
    Article
  10. Review
  11. Assembly of the Bacterial Ribosome with Circularly Permuted rRNA.bioRxiv : the preprint server for biology · 2024
    Article
  12. Article
  13. Review
  14. 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

8 authors at 3 institutions in 2 countries.

Amal SeffouhDepartment of Anatomy and Cell Biology, McGill University, Montreal, Quebec H3A 0C7, Canada.
Chirstian TrahanCenter for genetic and neurological diseases, Institut de Recherches Cliniques de Montréal (IRCM), Montréal, Quebec H2W 1R7, Canada.
Tanzila WasiDepartment 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.
Kaustuv BasuDepartment of Anatomy and Cell Biology, McGill University, Montreal, Quebec H3A 0C7, Canada.
Robert A BrittonDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX 77030, USA.
Marlene OeffingerCenter for genetic and neurological diseases, Institut de Recherches Cliniques de Montréal (IRCM), Montréal, Quebec H2W 1R7, Canada.
Joaquin OrtegaDepartment of Anatomy and Cell Biology, McGill University, Montreal, Quebec H3A 0C7, Canada.ORCID 0000-0002-9423-3344
McGill University · CABaylor College of Medicine · USMontreal Clinical Research Institute · CA

Funding

GTPase control of large ribosome subunit biogenesisR01GM110248 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI BRITTON, ROBERT A · 2015 to 2018
$1.5M
CIHR PJT-153044NIGMS NIH HHS R01 GM110248
6 · The paper itself

Abstract

RbgA is an essential protein for the assembly of the 50S subunit in Bacillus subtilis. Depletion of RbgA leads to the accumulation of the 45S intermediate. A strain expressing a RbgA variant with reduced GTPase activity generates spontaneous suppressor mutations in uL6. Each suppressor strain accumulates a unique 44S intermediate. We reasoned that characterizing the structure of these mutant 44S intermediates may explain why RbgA is required to catalyze the folding of the 50S functional sites. We found that in the 44S particles, rRNA helices H42 and H97, near the binding site of uL6, adopt a flexible conformation and allow the central protuberance and functional sites in the mutant 44S particles to mature in any order. Instead, the wild-type 45S particles exhibit a stable H42-H97 interaction and their functional sites always mature last. The dependence on RbgA was also less pronounced in the 44S particles. We concluded that the binding of uL6 pauses the maturation of the functional sites, but the central protuberance continues to fold. RbgA exclusively binds intermediates with a formed central protuberance and licenses the folding of the functional sites. Through this mechanism, RbgA ensures that the functional sites of the 50S mature last.

Indexed as

Ribosomal ProteinsRibosome Subunits, Large, BacterialBacillus subtilisGTP PhosphohydrolasesRNA, RibosomalGTP PhosphohydrolasesRibosomal ProteinsRNA, Ribosomal

Identifiers

PMID35141754
PMCPMC9638911
OpenAlexW4210520822

What OpenQuestion holds

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LicenceCC BY-NC
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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.