Evidence map›Paper›PMID 25378333›Full record

ArticleNucleic acids research2014

The conserved GTPase LepA contributes mainly to translation initiation in Escherichia coli.

Rohan Balakrishnan, Kenji Oman, Shinichiro Shoji, Ralf Bundschuh, Kurt Fredrick

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 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

53 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Foods (Basel, Switzerland) · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Functions and Regulation of Translation Elongation Factors.Frontiers in molecular biosciences · 2021
    Review
  15. Monitoring Bacterial Translation Rates Genome-Wide.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  16. Article
  17. Article
  18. Multicopy Suppressor Analysis of Strains Lacking Cytoplasmic Peptidyl-ProlylInternational journal of molecular sciences · 2020
    Article
  19. Review
  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

5 authors at 1 institution in 1 country.

Rohan BalakrishnanOhio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.
Kenji OmanCenter for RNA Biology, The Ohio State University, Columbus, OH 43210, USA Department of Physics, The Ohio State University, Columbus, OH 43210, USA.
Shinichiro ShojiCenter for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.
Ralf BundschuhCenter for RNA Biology, The Ohio State University, Columbus, OH 43210, USA Department of Physics, The Ohio State University, Columbus, OH 43210, USA.
Kurt FredrickOhio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA fredrick.5@osu.edu.
The Ohio State University · US

Funding

Molecular analysis of accurate ribosomal translocationR01GM072528 · NIGMS · OHIO STATE UNIVERSITY · PI Kurt L Fredrick · 2005 to 2026
$5.8M
NIGMS NIH HHS GM072528NIGMS NIH HHS R01 GM072528
6 · The paper itself

Abstract

LepA is a paralog of EF-G found in all bacteria. Deletion of lepA confers no obvious growth defect in Escherichia coli, and the physiological role of LepA remains unknown. Here, we identify nine strains (ΔdksA, ΔmolR1, ΔrsgA, ΔtatB, ΔtonB, ΔtolR, ΔubiF, ΔubiG or ΔubiH) in which ΔlepA confers a synthetic growth phenotype. These strains are compromised for gene regulation, ribosome assembly, transport and/or respiration, indicating that LepA contributes to these functions in some way. We also use ribosome profiling to deduce the effects of LepA on translation. We find that loss of LepA alters the average ribosome density (ARD) for hundreds of mRNA coding regions in the cell, substantially reducing ARD in many cases. By contrast, only subtle and codon-specific changes in ribosome distribution along mRNA are seen. These data suggest that LepA contributes mainly to the initiation phase of translation. Consistent with this interpretation, the effect of LepA on ARD is related to the sequence of the Shine-Dalgarno region. Global perturbation of gene expression in the ΔlepA mutant likely explains most of its phenotypes.

Indexed as

Peptide Chain Initiation, TranslationalCatalytic DomainEscherichia coliEscherichia coli ProteinsGene DeletionGTP PhosphohydrolasesPeptide Chain Elongation, TranslationalPeptide Initiation FactorsPhenotypeProkaryotic Initiation FactorsProtein Structure, TertiaryRibosomesRNA, MessengerEscherichia coli ProteinsGTP PhosphohydrolasesLepA protein, E coliPeptide Initiation FactorsProkaryotic Initiation FactorsRNA, Messenger

Identifiers

PMID25378333
PMCPMC4245954
OpenAlexW2148448069

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.