Evidence map›Paper›PMID 23948732›Full record

ArticleRNA biology2013

Indigenous and acquired modifications in the aminoglycoside binding sites of Pseudomonas aeruginosa rRNAs.

Belen Gutierrez, Stephen Douthwaite, Bruno Gonzalez-Zorn

Open access · bronzeAbstract read
In one paragraph

Article in RNA biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.4field-weighted citation impact, top 34% 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

12 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Anaerobiosis and Mutations Can Reduce Susceptibility ofPathogens (Basel, Switzerland) · 2025
    Article
  3. Article
  4. Complete list of canonical post-transcriptional modifications in thebioRxiv : the preprint server for biology · 2024
    Article
  5. The Building Blocks of Antimicrobial Resistance inFrontiers in cellular and infection microbiology · 2021
    Review
  6. Article
  7. Article
  8. Mutations in GeneAntimicrobial agents and chemotherapy · 2018
    Article
  9. Article
  10. Article
  11. Article
  12. 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 2 countries.

Belen GutierrezDepartamento de Sanidad Animal; Facultad de Veterinaria; Universidad Complutense de Madrid; Madrid, Spain; Centro de Vigilancia Sanitaria Veterinaria (VISAVET); Universidad Complutense de Madrid; Madrid, Spain.
Stephen Douthwaite
Bruno Gonzalez-Zorn
Universidad Complutense de Madrid · ESUniversity of Southern Denmark · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aminoglycoside antibiotics remain the drugs of choice for treatment of Pseudomonas aeruginosa infections, particularly for respiratory complications in cystic-fibrosis patients. Previous studies on other bacteria have shown that aminoglycosides have their primary target within the decoding region of 16S rRNA helix 44 with a secondary target in 23S rRNA helix 69. Here, we have mapped P. aeruginosa rRNAs using MALDI mass spectrometry and reverse transcriptase primer extension to identify nucleotide modifications that could influence aminoglycoside interactions. Helices 44 and 45 contain indigenous (housekeeping) modifications at m (4)Cm1402, m (3)U1498, m (2)G1516, m (6) 2A1518, and m (6) 2A1519; helix 69 is modified at m (3)Ψ1915, with m (5)U1939 and m (5)C1962 modification in adjacent sequences. All modifications were close to stoichiometric, with the exception of m (3)Ψ1915, where about 80% of rRNA molecules were methylated. The modification status of a virulent clinical strain expressing the acquired methyltransferase RmtD was altered in two important respects: RmtD stoichiometrically modified m (7)G1405 conferring high resistance to the aminoglycoside tobramycin and, in doing so, impeded one of the methylation reactions at C1402. Mapping the nucleotide methylations in P. aeruginosa rRNAs is an essential step toward understanding the architecture of the aminoglycoside binding sites and the rational design of improved drugs against this bacterial pathogen.

Indexed as

AminoglycosidesBacterial ProteinsBinding SitesCircular DichroismEscherichia coliEscherichia coli ProteinsMethylationMethyltransferasesModels, MolecularNucleic Acid ConformationProtein Structure, TertiaryPseudomonas aeruginosaRNA, BacterialRNA, Ribosomal, 16SRNA, Ribosomal, 23SSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationAminoglycosidesBacterial ProteinsEscherichia coli ProteinsMethyltransferasesRNA, BacterialRNA, Ribosomal, 16SRNA, Ribosomal, 23SaminoglycosidesmethyltransferasespseudomonasRmtDrRNA modifications

Identifiers

PMID23948732
PMCPMC3817154
OpenAlexW2071043444

What OpenQuestion holds

Textmetadata
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.