Evidence map›Paper›PMID 24837292›Full record

ArticleJournal of bacteriology2014

Control of natural transformation in salivarius Streptococci through specific degradation of σX by the MecA-ClpCP protease complex.

Astrid Wahl, Florence Servais, Anne-Sophie Drucbert, Catherine Foulon, Laetitia Fontaine, Pascal Hols

Abstract read
In one paragraph

Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

  1. Fluoride triggers lysis inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Review
  3. MecA inmSphere · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. The transcription regulator BrsR serves as a network hub of natural competence protein-protein interactions inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Article
  13. Deficiency of MecA inFrontiers in microbiology · 2018
    Article
  14. Article
  15. Article
  16. Stress Physiology of Lactic Acid Bacteria.Microbiology and molecular biology reviews : MMBR · 2016
    Review
  17. Article
  18. Article
  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

6 authors.

Astrid WahlInstitut des Sciences de la Vie, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.
Florence ServaisInstitut des Sciences de la Vie, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.
Anne-Sophie DrucbertUniversité Lille Nord de France and UDSL, Plate-Forme d'Interactions Moléculaires, IMPRT, IFR 114, Faculté de Médecine, Lille, France.
Catherine FoulonUniversité Lille Nord de France and UDSL, EA-4481, UFR Pharmacie, Lille, France.
Laetitia FontaineInstitut des Sciences de la Vie, Université Catholique de Louvain, Louvain-la-Neuve, Belgium laetitia.fontaine@uclouvain.be pascal.hols@uclouvain.be.
Pascal HolsInstitut des Sciences de la Vie, Université Catholique de Louvain, Louvain-la-Neuve, Belgium laetitia.fontaine@uclouvain.be pascal.hols@uclouvain.be.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Competence for natural DNA transformation is a tightly controlled developmental process in streptococci. In mutans and salivarius species, the abundance of the central competence regulator σ(X) is regulated at two levels: transcriptional, by the ComRS signaling system via the σ(X)/ComX/SigX-inducing peptide (XIP), and posttranscriptional, by the adaptor protein MecA and its associated Clp ATPase, ClpC. In this study, we further investigated the mechanism and function of the MecA-ClpC control system in the salivarius species Streptococcus thermophilus. Using in vitro approaches, we showed that MecA specifically interacts with both σ(X) and ClpC, suggesting the formation of a ternary σ(X)-MecA-ClpC complex. Moreover, we demonstrated that MecA ultimately targets σ(X) for its degradation by the ClpCP protease in an ATP-dependent manner. We also identify a short sequence (18 amino acids) in the N-terminal domain of σ(X) as essential for the interaction with MecA and subsequent σ(X) degradation. Finally, increased transformability of a MecA-deficient strain in the presence of subinducing XIP concentrations suggests that the MecA-ClpCP proteolytic complex acts as an additional locking device to prevent competence under inappropriate conditions. A model of the interplay between ComRS and MecA-ClpCP in the control of σ(X) activity is proposed.

Indexed as

Gene Expression Regulation, BacterialAdenosine TriphosphatasesAmino Acid SequenceBacterial ProteinsDNA Transformation CompetenceHeat-Shock ProteinsModels, MolecularMolecular Sequence DataMultienzyme ComplexesProtein Structure, TertiaryProteolysisSigma FactorStreptococcus thermophilusTranscription FactorsTransformation, BacterialAdenosine TriphosphatasesBacterial ProteinsClpC protein, BacteriaClpE protein, bacteriaComX protein, StreptococcusHeat-Shock ProteinsMultienzyme ComplexesSigma FactorTranscription Factors

Identifiers

PMID24837292
PMCPMC4135673

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.