Evidence map›Paper›PMID 27159580›Full record

ArticleNature chemical biology2016

An intrinsically disordered entropic switch determines allostery in Phd-Doc regulation.

Abel Garcia-Pino, Steven De Gieter, Ariel Talavera, Henri De Greve, Rouslan G Efremov, Remy Loris

Abstract read
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In one paragraph

Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
6.0field-weighted citation impact, top 4% 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

27 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
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  8. Biochemical and X-ray analyses of the players involved in the faRel2/aTfaRel2 toxin-antitoxin operon.Acta crystallographica. Section F, Structural biology communications · 2023
    Article
  9. Article
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  11. Review
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  13. Entropic pressure controls the oligomerization of the Vibrio cholerae ParD2 antitoxin.Acta crystallographica. Section D, Structural biology · 2021
    Article
  14. Prokaryote toxin-antitoxin modules: Complex regulation of an unclear function.Protein science : a publication of the Protein Society · 2021
    Review
  15. Article
  16. Article
  17. The Rel stringent factor from Thermus thermophilus: crystallization and X-ray analysis.Acta crystallographica. Section F, Structural biology communications · 2019
    Article
  18. Article
  19. Article
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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 2 institutions in 1 country.

Abel Garcia-PinoStructural Biology Brussels, Department of Biotechnology, Vrije Universiteit Brussel (VUB), Brussels, Belgium.
Steven De GieterStructural Biology Brussels, Department of Biotechnology, Vrije Universiteit Brussel (VUB), Brussels, Belgium.
Ariel TalaveraStructural Biology Brussels, Department of Biotechnology, Vrije Universiteit Brussel (VUB), Brussels, Belgium.
Henri De GreveStructural Biology Brussels, Department of Biotechnology, Vrije Universiteit Brussel (VUB), Brussels, Belgium.
Rouslan G EfremovStructural Biology Brussels, Department of Biotechnology, Vrije Universiteit Brussel (VUB), Brussels, Belgium.
Remy LorisStructural Biology Brussels, Department of Biotechnology, Vrije Universiteit Brussel (VUB), Brussels, Belgium.
Vrije Universiteit Brussel · BEVIB-VUB Center for Structural Biology · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Conditional cooperativity is a common mechanism involved in transcriptional regulation of prokaryotic type II toxin-antitoxin operons and is intricately related to bacterial persistence. It allows the toxin component of a toxin-antitoxin module to act as a co-repressor at low doses of toxin as compared to antitoxin. When toxin level exceeds a certain threshold, however, the toxin becomes a de-repressor. Most antitoxins contain an intrinsically disordered region (IDR) that typically is involved in toxin neutralization and repressor complex formation. To address how the antitoxin IDR is involved in transcription regulation, we studied the phd-doc operon from bacteriophage P1. We provide evidence that the IDR of Phd provides an entropic barrier precluding full operon repression in the absence of Doc. Binding of Doc results in a cooperativity switch and consequent strong operon repression, enabling context-specific modulation of the regulatory process. Variations of this theme are likely to be a common mechanism in the autoregulation of bacterial operons that involve intrinsically disordered regions.

Indexed as

EntropyAllosteric RegulationAntitoxinsBacteriophage P1OperonAntitoxins

Identifiers

PMID27159580
OpenAlexW2345986058

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.