Evidence map›Paper›PMID 25388641›Full record

ArticleMolecular microbiology2015

Specific N-terminal cleavage of ribosomal protein L27 in Staphylococcus aureus and related bacteria.

Erin A Wall, J Harry Caufield, Charles E Lyons, Keith A Manning, Terje Dokland, Gail E Christie

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2015. 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
1.6field-weighted citation impact, top 17% 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, 28 citations in OpenAlex.

  1. Analysis of essential genes inJournal of bacteriology · 2025
    Article
  2. Review
  3. Cleavage ofbioRxiv : the preprint server for biology · 2025
    Article
  4. Analysis of Essential Genes inbioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Origins of peptidases.Biochimie · 2019
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Structural insights into species-specific features of the ribosome from the pathogen Staphylococcus aureus.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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 at 2 institutions in 1 country.

Erin A WallDepartment of Microbiology and Immunology, Virginia Commonwealth University School of Medicine, Richmond, VA, 23298, USA.
J Harry Caufield
Charles E Lyons
Keith A Manning
Terje Dokland
Gail E Christie
Virginia Commonwealth University · USUniversity of Alabama at Birmingham · US

Funding

Structural basis for pathogenicity island mobilization in S. aureusR01AI083255 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI DOKLAND, TERJE · 2009 to 2023
$5.6M
Staphylococcus aureus ribosomal protein processing, a potential new drug targetR21AI109202 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI CHRISTIE, GAIL E · 2014 to 2015
$407k
NIAID NIH HHS R01 AI083255NIAID NIH HHS R21 AI109202
6 · The paper itself

Abstract

Ribosomal protein L27 is a component of the eubacterial large ribosomal subunit that has been shown to play a critical role in substrate stabilization during protein synthesis. This function is mediated by the L27 N-terminus, which protrudes into the peptidyl transferase center. In this report, we demonstrate that L27 in Staphylococcus aureus and other Firmicutes is encoded with an N-terminal extension that is not present in most Gram-negative organisms and is absent from mature ribosomes. We have identified a cysteine protease, conserved among bacteria containing the L27 N-terminal extension, which performs post-translational cleavage of L27. Ribosomal biology in eubacteria has largely been studied in the Gram-negative bacterium Escherichia coli; our findings indicate that there are aspects of the basic biology of the ribosome in S. aureus and other related bacteria that differ substantially from that of the E. coli ribosome. This research lays the foundation for the development of new therapeutic approaches that target this novel pathway.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceComputational BiologyCysteine ProteasesEscherichia coliMass SpectrometryModels, MolecularMolecular Sequence DataPhylogenyProtein BiosynthesisRibosomal ProteinsRibosomesSequence Homology, Amino AcidStaphylococcus aureusCysteine ProteasesRibosomal Proteinsribosomal proteins L27

Identifiers

PMID25388641
PMCPMC4418427
OpenAlexW2164058098

What OpenQuestion holds

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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.