Evidence map›Paper›PMID 26276802›Full record

ArticleRNA (New York, N.Y.)2015

A glyS T-box riboswitch with species-specific structural features responding to both proteinogenic and nonproteinogenic tRNAGly isoacceptors.

Maria Apostolidi, Nizar Y Saad, Denis Drainas, Spyros Pournaras, Hubert D Becker, Constantinos Stathopoulos

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 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
0.6field-weighted citation impact, top 30% 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, 21 citations in OpenAlex.

  1. Article
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  4. A Riboswitch-Driven Era of New Antibacterials.Antibiotics (Basel, Switzerland) · 2022
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  10. Hydrogen Peroxide Affects Growth ofFrontiers in immunology · 2021
    Article
  11. Review
  12. Article
  13. Review
  14. Noncoding RNA.Microbiology spectrum · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Review
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 3 institutions in 2 countries.

Maria ApostolidiDepartment of Biochemistry, School of Medicine, University of Patras, 26504 Patras, Greece.
Nizar Y SaadUnité Mixte de Recherche 7156 Génétique Moléculaire, Génomique, Microbiologie, CNRS, Université de Strasbourg, F-67084 Strasbourg, France.
Denis DrainasDepartment of Biochemistry, School of Medicine, University of Patras, 26504 Patras, Greece.
Spyros PournarasDepartment of Microbiology, School of Medicine, University of Athens, 11527 Athens, Greece.
Hubert D BeckerUnité Mixte de Recherche 7156 Génétique Moléculaire, Génomique, Microbiologie, CNRS, Université de Strasbourg, F-67084 Strasbourg, France.
Constantinos StathopoulosDepartment of Biochemistry, School of Medicine, University of Patras, 26504 Patras, Greece.
University of Patras · GRCentre National de la Recherche Scientifique · FRNational and Kapodistrian University of Athens · GR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In Staphylococcus aureus, a T-box riboswitch exists upstream of the glyS gene to regulate transcription of the sole glycyl-tRNA synthetase, which aminoacylates five tRNA(Gly) isoacceptors bearing GCC or UCC anticodons. Subsequently, the glycylated tRNAs serve as substrates for decoding glycine codons during translation, and also as glycine donors for exoribosomal synthesis of pentaglycine peptides during cell wall formation. Probing of the predicted T-box structure revealed a long stem I, lacking features previously described for similar T-boxes. Moreover, the antiterminator stem includes a 42-nt long intervening sequence, which is staphylococci-specific. Finally, the terminator conformation adopts a rigid two-stem structure, where the intervening sequence forms the first stem followed by the second stem, which includes the more conserved residues. Interestingly, all five tRNA(Gly) isoacceptors interact with S. aureus glyS T-box with different binding affinities and they all induce transcription readthrough at different levels. The ability of both GCC and UCC anticodons to interact with the specifier loop indicates ambiguity during the specifier triplet reading, similar to the unconventional reading of glycine codons during protein synthesis. The S. aureus glyS T-box structure is consistent with the recent crystallographic and NMR studies, despite apparent differences, and highlights the phylogenetic variability of T-boxes when studied in a genome-dependent context. Our data suggest that the S. aureus glyS T-box exhibits differential tRNA selectivity, which possibly contributes toward the regulation and synchronization of ribosomal and exoribosomal peptide synthesis, two essential but metabolically unrelated pathways.

Indexed as

RiboswitchBase SequenceMolecular Sequence DataNucleic Acid ConformationProteinsRNA, Transfer, GlySequence Homology, Nucleic AcidStaphylococcus aureusTranscription, GeneticProteinsRiboswitchRNA, Transfer, Glyglycyl-tRNA synthetaseStaphylococcus aureusT-box riboswitchtranscription regulationtRNA

Identifiers

PMID26276802
PMCPMC4574755
OpenAlexW2270478603

What OpenQuestion holds

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Registered trials

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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.