Evidence map›Paper›PMID 25879934›Full record

ArticlePloS one2015

The large ribosomal subunit protein L9 enables the growth of EF-P deficient cells and enhances small subunit maturation.

Anusha Naganathan, Matthew P Wood, Sean D Moore

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. 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
1.7field-weighted citation impact, top 16% 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, 22 citations in OpenAlex.

  1. Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. The intrinsic macrolide resistome ofAntimicrobial agents and chemotherapy · 2024
    Article
  6. Article
  7. Review
  8. Review
  9. Ribosome collisions alter frameshifting at translational reprogramming motifs in bacterial mRNAs.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  10. Article
  11. 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

3 authors at 2 institutions in 1 country.

Anusha NaganathanThe Burnett School of Biomedical Sciences, College of Medicine, The University of Central Florida, Orlando, FL, 32816, United States of America.
Matthew P WoodSeattle Biomed, 307 Westlake Ave N, Suite 500, Seattle, WA, 98109, United States of America; Department of Global Health, University of Washington, 1510 N.E. San Juan Road, Seattle, WA, 98195, United States of America.
Sean D MooreThe Burnett School of Biomedical Sciences, College of Medicine, The University of Central Florida, Orlando, FL, 32816, United States of America.
University of Central Florida · USUniversity of Washington · US

Funding

Identification of Pathways Affected by Essential Proteins of Unknown FunctionR15GM102714 · NIGMS · UNIVERSITY OF CENTRAL FLORIDA · PI MOORE, SEAN DAVID · 2012 to 2012
$413k
NIGMS NIH HHS R15 GM102714NIGMS NIH HHS R15 GM102714-01
6 · The paper itself

Abstract

The loss of the large ribosomal protein L9 causes a reduction in translation fidelity by an unknown mechanism. To identify pathways affected by L9, we identified mutants of E. coli that require L9 for fitness. In a prior study, we characterized L9-dependent mutations in the essential GTPase Der (EngA). Here, we describe a second class of L9-dependent mutations that either compromise or inactivate elongation factor P (EF-P, eIF5A in eukaryotes). Without L9, Δefp cells are practically inviable. Cell fractionation studies revealed that, in both the Der and EF-P mutant cases, L9's activity reduces immature 16S rRNA in 30S particles and partially restores the abundance of monosomes. Inspired by these findings, we discovered that L9 also enhances 16S maturation in wild-type cells. Surprisingly, although the amount of immature 16S in 30S particles was found to be elevated in ΔrplI cells, the amount in polysomes was low and inversely correlated with the immature 16S abundance. These findings provide an explanation for the observed fitness increases afforded by L9 in these mutants and reveal particular physiological conditions in which L9 becomes critical. Additionally, L9 may affect the partitioning of small subunits containing immature 16S rRNA.

Indexed as

MutationPeptide Elongation FactorsRibosomal ProteinsRNA, Ribosomal, 16Sfactor EF-PPeptide Elongation Factorsribosomal protein L9Ribosomal ProteinsRNA, Ribosomal, 16S

Identifiers

PMID25879934
PMCPMC4399890
OpenAlexW2079297583

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.