Evidence map›Paper›PMID 27382067›Full record

ArticleNucleic acids research2016

Binding properties of YjeQ (RsgA), RbfA, RimM and Era to assembly intermediates of the 30S subunit.

Brett Thurlow, Joseph H Davis, Vivian Leong, Trevor F Moraes, James R Williamson, Joaquin Ortega

Abstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
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

27 citing papers in PubMed.

  1. Review
  2. Article
  3. Mechanistic insights intobioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. GTPase Era at the heart of ribosome assembly.Frontiers in molecular biosciences · 2023
    Review
  11. Article
  12. Article
  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

6 authors.

Brett ThurlowDepartment of Biochemistry and Biomedical Sciences and M.G. DeGroote Institute for Infectious Diseases Research, McMaster University, 1280 Main Street West, Hamilton, Ontario L8S4K1, Canada.
Joseph H DavisDepartment of Integrative Computational and Structural Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Vivian LeongDepartment of Biochemistry and Biomedical Sciences and M.G. DeGroote Institute for Infectious Diseases Research, McMaster University, 1280 Main Street West, Hamilton, Ontario L8S4K1, Canada.
Trevor F MoraesDepartment of Biochemistry, University of Toronto, 1 King's College Circle, Toronto, Ontario M5S1A8, Canada.
James R WilliamsonDepartment of Integrative Computational and Structural Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Joaquin OrtegaDepartment of Biochemistry and Biomedical Sciences and M.G. DeGroote Institute for Infectious Diseases Research, McMaster University, 1280 Main Street West, Hamilton, Ontario L8S4K1, Canada ortegaj@mcmaster.ca.

Funding

Quantitation and biochemical characterization of autophagy's role in agingK99AG050749 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI DAVIS, JOSEPH HARRY · 2015 to 2016
$257k
NIA NIH HHS K99 AG050749
6 · The paper itself

Abstract

Our understanding regarding the function of YjeQ (also called RsgA), RbfA, RimM and Era in ribosome biogenesis has been derived in part from the study of immature 30S particles that accumulate in null strains lacking one of these factors. However, their mechanistic details are still unknown. Here, we demonstrate that these immature particles are not dead-end products of assembly, but progress into mature 30S subunits. Mass spectrometry analysis revealed that in vivo the occupancy level of these factors in these immature 30S particles is below 10% and that the concentration of factors does not increase when immature particles accumulate in cells. We measured by microscale thermophoresis that YjeQ and Era binds to the mature 30S subunit with high affinity. However, the binding affinity of these factors to the immature particles and of RimM and RbfA to mature or immature particles was weak, suggesting that binding is not occurring at physiological concentrations. These results suggest that in the absence of these factors, the immature particles evolve into a thermodynamically stable intermediate that exhibits low affinity for the assembly factors. These results imply that the true substrates of YjeQ, RbfA, RimM and Era are immature particles that precede the ribosomal particles accumulating in the knockouts strains.

Indexed as

Escherichia coliEscherichia coli ProteinsGTP-Binding ProteinsGTP PhosphohydrolasesKineticsModels, BiologicalMultiprotein ComplexesMutationProtein BindingRibosomal ProteinsRibosome Subunits, Large, BacterialRibosome Subunits, Small, BacterialRNA-Binding ProteinsRNA, Ribosomalera protein, E coliEscherichia coli ProteinsGTP-Binding ProteinsGTP PhosphohydrolasesMultiprotein ComplexesRbfA protein, E coliRibosomal ProteinsRimM protein, E coliRNA-Binding ProteinsRNA, RibosomalRsgA protein, E coli

Identifiers

PMID27382067
PMCPMC5175332

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.