Evidence map›Paper›PMID 26961432›Full record

ArticleNature communications2016

Unmasking the ancestral activity of integron integrases reveals a smooth evolutionary transition during functional innovation.

Jose Antonio Escudero, Celine Loot, Vincent Parissi, Aleksandra Nivina, Christiane Bouchier, Didier Mazel

Abstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Coexistence of tet(A) and blaEuropean journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2023
    Article
  10. Article
  11. Mechanisms of protein evolution.Protein science : a publication of the Protein Society · 2022
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Characterization of Novel Integrons, InFrontiers in microbiology · 2017
    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.

Jose Antonio EscuderoInstitut Pasteur, Unité de Plasticité du Génome Bactérien, Département Génomes et Génétique, 28 Rue du Dr Roux, 75015 Paris, France.ORCID http://orcid.org/0000-0001-8552-2956
Celine LootInstitut Pasteur, Unité de Plasticité du Génome Bactérien, Département Génomes et Génétique, 28 Rue du Dr Roux, 75015 Paris, France.
Vincent ParissiLaboratoire de Microbiologie Fondamentale et Pathogénicité UMR-CNRS 5234. Bat 3A 3ème étage, 146 rue Léo Saignat, 33076 Bordeaux, France.
Aleksandra NivinaInstitut Pasteur, Unité de Plasticité du Génome Bactérien, Département Génomes et Génétique, 28 Rue du Dr Roux, 75015 Paris, France.ORCID http://orcid.org/0000-0002-1802-3724
Christiane BouchierInstitut Pasteur, Genomic Platform, 28 Rue du Dr Roux, 75015 Paris, France.
Didier MazelInstitut Pasteur, Unité de Plasticité du Génome Bactérien, Département Génomes et Génétique, 28 Rue du Dr Roux, 75015 Paris, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tyrosine (Y)-recombinases have evolved to deliver mechanistically different reactions on a variety of substrates, but these evolutionary transitions are poorly understood. Among them, integron integrases are hybrid systems recombining single- and double-stranded DNA partners. These reactions are asymmetric and need a replicative resolution pathway, an exception to the canonical second strand exchange model of Y-recombinases. Integron integrases possess a specific domain for this specialized pathway. Here we show that despite this, integrases are still capable of efficiently operating the ancestral second strand exchange in symmetrical reactions between double-stranded substrates. During these reactions, both strands are reactive and Holliday junction resolution can follow either pathway. A novel deep-sequencing approach allows mapping of the crossover point for the second strand exchange. The persistence of the ancestral activity in integrases illustrates their robustness and shows that innovation towards new recombination substrates and resolution pathways was a smooth evolutionary process.

Indexed as

Bacterial ProteinsBacteriophage lambdaComputer SimulationDNADNA, CruciformDNA, Single-StrandedEscherichia coliEscherichia coli ProteinsEvolution, MolecularIntegrasesIntegronsIn Vitro TechniquesNucleic Acid ConformationProtein Structure, TertiaryVibrio choleraeBacterial ProteinsDNADNA, CruciformDNA, Single-StrandedEscherichia coli ProteinsIntegrases

Identifiers

PMID26961432
PMCPMC4792948

What OpenQuestion holds

Textmetadata
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.