Evidence map›Paper›PMID 19589804›Full record

ArticleNucleic acids research2009

Determination of the target nucleosides for members of two families of 16S rRNA methyltransferases that confer resistance to partially overlapping groups of aminoglycoside antibiotics.

Miloje Savic, Josip Lovric, Tatjana Ilic Tomic, Branka Vasiljevic, Graeme L Conn

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Ribosome-targeting antibiotics and resistanceRSC medicinal chemistry · 2023
    Review
  3. Antibiotic Resistance in Bacteria-A Review.Antibiotics (Basel, Switzerland) · 2022
    Review
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  5. Review
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  16. Article
  17. Molecular recognition and modification of the 30S ribosome by the aminoglycoside-resistance methyltransferase NpmA.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  18. Review
  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

5 authors at 2 institutions in 3 countries.

Miloje SavicFaculty of Life Sciences, The University of Manchester, Manchester Interdisciplinary Biocentre, Manchester M1 7DN, UK.
Josip Lovric
Tatjana Ilic Tomic
Branka Vasiljevic
Graeme L Conn
Emory University · USUniversity of Manchester · GB

Funding

Wellcome Trust 078374
6 · The paper itself

Abstract

The 16S ribosomal RNA methyltransferase enzymes that modify nucleosides in the drug binding site to provide self-resistance in aminoglycoside-producing micro-organisms have been proposed to comprise two distinct groups of S-adenosyl-l-methionine (SAM)-dependent RNA enzymes, namely the Kgm and Kam families. Here, the nucleoside methylation sites for three Kgm family methyltransferases, Sgm from Micromonospora zionensis, GrmA from Micromonospora echinospora and Krm from Frankia sp. Ccl3, were experimentally determined as G1405 by MALDI-ToF mass spectrometry. These results significantly extend the list of securely characterized G1405 modifying enzymes and experimentally validate their grouping into a single enzyme family. Heterologous expression of the KamB methyltransferase from Streptoalloteichus tenebrarius experimentally confirmed the requirement for an additional 60 amino acids on the deduced KamB N-terminus to produce an active methyltransferase acting at A1408, as previously suggested by an in silico analysis. Finally, the modifications at G1405 and A1408, were shown to confer partially overlapping but distinct resistance profiles in Escherichia coli. Collectively, these data provide a more secure and systematic basis for classification of new aminoglycoside resistance methyltransferases from producers and pathogenic bacteria on the basis of their sequences and resistance profiles.

Indexed as

AminoglycosidesAnti-Bacterial AgentsBacterial ProteinsDrug Resistance, BacterialEscherichia coliMethyltransferasesNucleosidesPhylogenyRNA, Ribosomal, 16SAminoglycosidesAnti-Bacterial AgentsBacterial ProteinsMethyltransferasesNucleosidesRNA, Ribosomal, 16Ssgm protein, Micromonospora zionensis

Identifiers

PMID19589804
PMCPMC2760815
OpenAlexW2042397968

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.