Evidence map›Paper›PMID 33237283›Full record

ArticleNucleic acids research2020

Discovery and characterization of a fourth class of guanidine riboswitches.

Felina Lenkeit, Iris Eckert, Jörg S Hartig, Zasha Weinberg

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

32 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Review
  3. Deciphering guanidine assimilation and riboswitch-based gene regulation in cyanobacteria for synthetic biology applications.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  7. Review
  8. Biomolecular NMR assignments · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The current riboswitch landscape inMicrobiology (Reading, England) · 2024
    Review
  14. Article
  15. Article
  16. Article
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  18. Article
  19. Crystal structure of a GCN5-related N-acetyltransferase from Lactobacillus curiae.Acta crystallographica. Section F, Structural biology communications · 2023
    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

4 authors at 2 institutions in 1 country.

Felina LenkeitDepartment of Chemistry, University of Konstanz, Universitätsstraße 10, 78457 Konstanz, Germany.
Iris EckertBioinformatics Group, Department of Computer Science and Interdisciplinary Centre for Bioinformatics, Leipzig University, Härtelstraße 16-18, 04107 Leipzig, Germany.
Jörg S HartigDepartment of Chemistry, University of Konstanz, Universitätsstraße 10, 78457 Konstanz, Germany.
Zasha WeinbergBioinformatics Group, Department of Computer Science and Interdisciplinary Centre for Bioinformatics, Leipzig University, Härtelstraße 16-18, 04107 Leipzig, Germany.
Leipzig University · DEUniversity of Konstanz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Riboswitches are RNAs that specifically sense a small molecule and regulate genes accordingly. The recent discovery of guanidine-binding riboswitches revealed the biological significance of this compound, and uncovered genes related to its biology. For example, certain sugE genes encode guanidine exporters and are activated by the riboswitches to reduce toxic levels of guanidine in the cell. In order to study guanidine biology and riboswitches, we applied a bioinformatics strategy for discovering additional guanidine riboswitches by searching for new candidate motifs associated with sugE genes. Based on in vitro and in vivo experiments, we determined that one of our six best candidates is a new structural class of guanidine riboswitches. The expression of a genetic reporter was induced 80-fold in response to addition of 5 mM guanidine in Staphylococcus aureus. This new class, called the guanidine-IV riboswitch, reveals additional guanidine-associated protein domains that are extremely rarely or never associated with previously established guanidine riboswitches. Among these protein domains are two transporter families that are structurally distinct from SugE, and could represent novel types of guanidine exporters. These results establish a new metabolite-binding RNA, further validate a bioinformatics method for finding riboswitches and suggest substrate specificities for as-yet uncharacterized transporter proteins.

Indexed as

Computational BiologyEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialGuanidineMembrane ProteinsMembrane Transport ProteinsMolecular ChaperonesNucleic Acid ConformationProtein DomainsRiboswitchRNARNA, BacterialStaphylococcus aureusEscherichia coli ProteinsGuanidineMembrane ProteinsMembrane Transport ProteinsMolecular ChaperonesRiboswitchRNARNA, BacterialsugE protein, E coli

Identifiers

PMID33237283
PMCPMC7736828
OpenAlexW3108381361

What OpenQuestion holds

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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.