Evidence map›Paper›PMID 23325847›Full record

ArticleNucleic acids research2013

Mutational analysis of the ribosome assembly GTPase RbgA provides insight into ribosome interaction and ribosome-stimulated GTPase activation.

Megha Gulati, Nikhil Jain, Baskaran Anand, Balaji Prakash, Robert A Britton

Open access · goldAbstract read
In one paragraph

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 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. The late stages of yeast mitoribosome large subunit biogenesis.Biochimica et biophysica acta. Molecular cell research · 2025
    Article
  3. Article
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  5. Review
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  13. Article
  14. ppGpp negatively impacts ribosome assembly affecting growth and antimicrobial tolerance in Gram-positive bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Article
  16. Mitochondrial ribosome assembly in health and disease.Cell cycle (Georgetown, Tex.) · 2015
    Review
  17. Article
  18. 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

5 authors at 2 institutions in 2 countries.

Megha GulatiDepartment of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI 48823, USA.
Nikhil Jain
Baskaran Anand
Balaji Prakash
Robert A Britton
Indian Institute of Technology Guwahati · INMichigan State University · US

Funding

The Impact of Microbiome Composition, Diversity, and Function on Enteric DiseaseU19AI090872 · NIAID · MICHIGAN STATE UNIVERSITY · PI MANSFIELD, LINDA S. · 2010 to 2014
$7.1M
NIAID NIH HHS U19 AI090872
6 · The paper itself

Abstract

Ribosome biogenesis GTPase A protein (RbgA) is an essential GTPase required for the biogenesis of the 50S subunit in Bacillus subtilis. Homologs of RbgA are widely distributed in bacteria and eukaryotes and are implicated in ribosome assembly in the mitochondria, chloroplast and cytoplasm. Cells depleted of RbgA accumulate an immature large subunit that is missing key ribosomal proteins. RbgA, unlike many members of the Ras superfamily of GTPases, lacks a defined catalytic residue for carrying out guanosine triphosphate (GTP) hydrolysis. To probe RbgA function in ribosome assembly, we used a combined bioinformatics, genetic and biochemical approach. We identified a RNA-binding domain within the C-terminus of RbgA that is structurally similar to AmiR-NasR Transcription Anti-termination Regulator (ANTAR) domains, which are known to bind structured RNA. Mutation of key residues in the ANTAR domain altered RbgA association with the ribosome. We identified a putative catalytic residue within a highly conserved region of RbgA, His9, which is contained within a similar PGH motif found in elongation factor Tu (EF-Tu) that is required for GTP hydrolysis on interaction with the ribosome. Finally, our results support a model in which the GTPase activity of RbgA directly participates in the maturation of the large subunit rather than solely promoting dissociation of RbgA from the 50S subunit.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionBacillus subtilisBacterial ProteinsBinding SitesConserved SequenceGTP PhosphohydrolasesGuanine NucleotidesHydrolysisModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPhenotypeProtein BindingProtein Structure, TertiaryRibosomal ProteinsBacterial ProteinsGTP PhosphohydrolasesGuanine NucleotidesRibosomal Proteins

Identifiers

PMID23325847
PMCPMC3597669
OpenAlexW1984004530

What OpenQuestion holds

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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.