Evidence map›Paper›PMID 30597160›Full record

ArticleJournal of molecular biology2019

ABCF ATPases Involved in Protein Synthesis, Ribosome Assembly and Antibiotic Resistance: Structural and Functional Diversification across the Tree of Life.

Victoriia Murina, Marje Kasari, Hiraku Takada, Mariliis Hinnu, Chayan Kumar Saha, James W Grimshaw, Takahiro Seki, Michael Reith, Marta Putrinš, Tanel Tenson and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed, 1 pooled it
4.9field-weighted citation impact, top 3% 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

81 citing papers in PubMed, 1 synthesis or guideline pooled it, 136 citations in OpenAlex.

  1. Pooled it
  2. Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  3. Collided ribosomes are rescued by the endonuclease Rae1 andbioRxiv : the preprint server for biology · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Ribosomal protection as a linezolid resistance mechanism inAntimicrobial agents and chemotherapy · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Ribosomal protection as a linezolid resistance mechanism inbioRxiv : the preprint server for biology · 2025
    Article
  17. Review
  18. Linezolid in the Focus of Antimicrobial Resistance ofInternational journal of molecular sciences · 2025
    Review
  19. Article
  20. Review

21 more citing papers are in PubMed but not listed here.

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

13 authors at 4 institutions in 4 countries.

Victoriia MurinaDepartment of Molecular Biology, Umeå University, 901 87 Umeå, Sweden; Laboratory for Molecular Infection Medicine Sweden (MIMS), Umeå University, 901 87 Umeå, Sweden.
Marje KasariDepartment of Molecular Biology, Umeå University, 901 87 Umeå, Sweden.
Hiraku TakadaDepartment of Molecular Biology, Umeå University, 901 87 Umeå, Sweden; Laboratory for Molecular Infection Medicine Sweden (MIMS), Umeå University, 901 87 Umeå, Sweden.
Mariliis HinnuUniversity of Tartu, Institute of Technology, Nooruse 1, 50411 Tartu, Estonia.
Chayan Kumar SahaDepartment of Molecular Biology, Umeå University, 901 87 Umeå, Sweden.
James W GrimshawCentre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences Newcastle University, Richardson Road, Newcastle upon Tyne, NE2 4AX, United Kingdom.
Takahiro SekiDepartment of Applied Chemistry and Biotechnology, Faculty of Engineering, Chiba University, 263-8522 Chiba, Japan.
Michael ReithDepartment of Molecular Biology, Umeå University, 901 87 Umeå, Sweden.
Marta PutrinšUniversity of Tartu, Institute of Technology, Nooruse 1, 50411 Tartu, Estonia.
Tanel TensonUniversity of Tartu, Institute of Technology, Nooruse 1, 50411 Tartu, Estonia.
Henrik StrahlCentre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences Newcastle University, Richardson Road, Newcastle upon Tyne, NE2 4AX, United Kingdom.
Vasili HauryliukDepartment of Molecular Biology, Umeå University, 901 87 Umeå, Sweden; Laboratory for Molecular Infection Medicine Sweden (MIMS), Umeå University, 901 87 Umeå, Sweden; University of Tartu, Institute of Technology, Nooruse 1, 50411 Tartu, Estonia.
Gemma Catherine AtkinsonDepartment of Molecular Biology, Umeå University, 901 87 Umeå, Sweden. Electronic address: gemma.atkinson@umu.se.
Umeå University · SEUniversity of Tartu · EENewcastle University · GBChiba University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Within the larger ABC superfamily of ATPases, ABCF family members eEF3 in Saccharomyces cerevisiae and EttA in Escherichia coli have been found to function as ribosomal translation factors. Several other ABCFs including biochemically characterized VgaA, LsaA and MsrE confer resistance to antibiotics that target the peptidyl transferase center and exit tunnel of the ribosome. However, the diversity of ABCF subfamilies, the relationships among subfamilies and the evolution of antibiotic resistance (ARE) factors from other ABCFs have not been explored. To address this, we analyzed the presence of ABCFs and their domain architectures in 4505 genomes across the tree of life. We find 45 distinct subfamilies of ABCFs that are widespread across bacterial and eukaryotic phyla, suggesting that they were present in the last common ancestor of both. Surprisingly, currently known ARE ABCFs are not confined to a distinct lineage of the ABCF family tree, suggesting that ARE can readily evolve from other ABCF functions. Our data suggest that there are a number of previously unidentified ARE ABCFs in antibiotic producers and important human pathogens. We also find that ATPase-deficient mutants of all four E. coli ABCFs (EttA, YbiT, YheS and Uup) inhibit protein synthesis, indicative of their ribosomal function, and demonstrate a genetic interaction of ABCFs Uup and YheS with translational GTPase BipA involved in assembly of the 50S ribosome subunit. Finally, we show that the ribosome-binding resistance factor VmlR from Bacillus subtilis is localized to the cytoplasm, ruling out a role in antibiotic efflux.

Indexed as

Adenosine TriphosphatasesAnti-Bacterial AgentsATP-Binding Cassette TransportersBacillus subtilisDrug Resistance, BacterialDrug Resistance, MicrobialEscherichia coliEscherichia coli ProteinsGTP PhosphohydrolasesHumansModels, MolecularPeptidyl TransferasesProtein BiosynthesisProtein ConformationProtein DomainsRibosomesAdenosine TriphosphatasesAnti-Bacterial AgentsATP-Binding Cassette TransportersEscherichia coli ProteinsEttA protein, E coliGTP PhosphohydrolasesPeptidyl TransferasestypA protein, E coliUup protein, E coliABCFantibiotic resistanceAREribosometranslation

Identifiers

PMID30597160
PMCPMC6723617
OpenAlexW2950693336

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.