Evidence map›Paper›PMID 24335279›Full record

ArticleNucleic acids research2014

Functional domains of the 50S subunit mature late in the assembly process.

Ahmad Jomaa, Nikhil Jain, Joseph H Davis, James R Williamson, Robert A Britton, Joaquin Ortega

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

58 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
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  3. The late stages of yeast mitoribosome large subunit biogenesis.Biochimica et biophysica acta. Molecular cell research · 2025
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  6. A roadmap for ribosome assembly in human mitochondria.Nature structural & molecular biology · 2024
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  10. Complete list of canonical post-transcriptional modifications in thebioRxiv : the preprint server for biology · 2024
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  11. Review
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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

6 authors at 1 institution in 1 country.

Ahmad JomaaDepartment of Biochemistry and Biomedical Sciences and MG. DeGroote Institute for Infectious Diseases Research, McMaster University, 1280 Main Street West, Hamilton, Ontario L8S4K1, Canada, Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI 48824, USA and Department of Integrative Structural and Computational Biology, Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Nikhil Jain
Joseph H Davis
James R Williamson
Robert A Britton
Joaquin Ortega
Scripps Research Institute · US

Funding

Assembly of E. coli ribosomes in vitro and in cellsR37GM053757 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI WILLIAMSON, JAMES R · 2008 to 2017
$5.1M
CIHR MOP-82930NIGMS NIH HHS R37-GM-053757
6 · The paper itself

Abstract

Despite the identification of many factors that facilitate ribosome assembly, the molecular mechanisms by which they drive ribosome biogenesis are poorly understood. Here, we analyze the late stages of assembly of the 50S subunit using Bacillus subtilis cells depleted of RbgA, a highly conserved GTPase. We found that RbgA-depleted cells accumulate late assembly intermediates bearing sub-stoichiometric quantities of ribosomal proteins L16, L27, L28, L33a, L35 and L36. Using a novel pulse labeling/quantitative mass spectrometry technique, we show that this particle is physiologically relevant and is capable of maturing into a complete 50S particle. Cryo-electron microscopy and chemical probing revealed that the central protuberance, the GTPase associating region and tRNA-binding sites in this intermediate are unstructured. These findings demonstrate that key functional sites of the 50S subunit remain unstructured until late stages of maturation, preventing the incomplete subunit from prematurely engaging in translation. Finally, structural and biochemical analysis of a ribosome particle depleted of L16 indicate that L16 binding is necessary for the stimulation of RbgA GTPase activity and, in turn, release of this co-factor, and for conversion of the intermediate to a complete 50S subunit.

Indexed as

Bacillus subtilisGTP PhosphohydrolasesModels, MolecularRibosomal ProteinsRibosome Subunits, Large, BacterialRNA, TransferGTP Phosphohydrolasesribosomal protein L16Ribosomal ProteinsRNA, Transfer

Identifiers

PMID24335279
PMCPMC3950693
OpenAlexW1969820654

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.