Evidence map›Paper›PMID 23543711›Full record

ArticleJournal of bacteriology2013

Relaxed cleavage specificity within the RelE toxin family.

Nathalie Goeders, Pierre-Luc Drèze, Laurence Van Melderen

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.9field-weighted citation impact, top 7% 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

25 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
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  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Towards Exploring Toxin-Antitoxin Systems inInternational journal of molecular sciences · 2019
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Wake me when it's over - Bacterial toxin-antitoxin proteins and induced dormancy.Experimental biology and medicine (Maywood, N.J.) · 2016
    Review
  16. Article
  17. Article
  18. Article
  19. Initiation of mRNA decay in bacteria.Cellular and molecular life sciences : CMLS · 2014
    Review
  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

3 authors at 1 institution in 1 country.

Nathalie GoedersLaboratoire de Génétique et Physiologie Bactérienne, IBMM, Faculté des Sciences, Université Libre de Bruxelles (ULB), Gosselies, Belgium.
Pierre-Luc Drèze
Laurence Van Melderen
Université Libre de Bruxelles · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial type II toxin-antitoxin systems are widespread in bacteria. Among them, the RelE toxin family is one of the most abundant. The RelE(K-12) toxin of Escherichia coli K-12 represents the paradigm for this family and has been extensively studied, both in vivo and in vitro. RelE(K-12) is an endoribonuclease that cleaves mRNAs that are translated by the ribosome machinery as these transcripts enter the A site. Earlier in vivo reports showed that RelE(K-12) cleaves preferentially in the 5'-end coding region of the transcripts in a codon-independent manner. To investigate whether the molecular activity as well as the cleavage pattern are conserved within the members of this toxin family, RelE-like sequences were selected in Proteobacteria, Cyanobacteria, Actinobacteria, and Spirochaetes and tested in E. coli. Our results show that these RelE-like sequences are part of toxin-antitoxin gene pairs, and that they inhibit translation in E. coli by cleaving transcripts that are being translated. Primer extension analyses show that these toxins exhibit specific cleavage patterns in vivo, both in terms of frequency and location of cleavage sites. We did not observe codon-dependent cleavage but rather a trend to cleave upstream purines and between the second and third positions of codons, except for the actinobacterial toxin. Our results suggest that RelE-like toxins have evolved to rapidly and efficiently shut down translation in a large spectrum of bacterial species, which correlates with the observation that toxin-antitoxin systems are spreading by horizontal gene transfer.

Indexed as

Amino Acid SequenceBacterial ToxinsCodonConsensus SequenceEscherichia coli K12Escherichia coli ProteinsGenome, BacterialRNA, BacterialRNA CleavageRNA, MessengerSequence AlignmentSubstrate SpecificityBacterial ToxinsCodonEscherichia coli ProteinsRelE protein, E coliRNA, BacterialRNA, Messenger

Identifiers

PMID23543711
PMCPMC3676057
OpenAlexW1985934885

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.