Evidence map›Paper›PMID 34556858›Full record

ArticleNature chemical biology2021

Auxiliary interfaces support the evolution of specific toxin-antitoxin pairing.

Grzegorz J Grabe, Rachel T Giorgio, Alexander M J Hall, Rhodri M L Morgan, Laurent Dubois, Tyler A Sisley, Julian A Rycroft, Stephen A Hare, Sophie Helaine

Abstract read
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Article in Nature chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
3.1field-weighted citation impact, top 10% 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

8 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Evolving complex insulation.Nature chemical biology · 2021
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 2 countries.

Grzegorz J GrabeDepartment of Microbiology, Harvard Medical School, Boston, MA, USA.
Rachel T GiorgioDepartment of Microbiology, Harvard Medical School, Boston, MA, USA.
Alexander M J HallDepartment of Microbiology, Harvard Medical School, Boston, MA, USA.
Rhodri M L MorganDepartment of Life Sciences, Imperial College London, London, UK.ORCID http://orcid.org/0000-0002-9760-3638
Laurent DuboisDepartment of Microbiology, Harvard Medical School, Boston, MA, USA.ORCID http://orcid.org/0000-0003-0963-4029
Tyler A SisleyDepartment of Microbiology, Harvard Medical School, Boston, MA, USA.ORCID http://orcid.org/0000-0002-7711-6234
Julian A RycroftDepartment of Microbiology, Harvard Medical School, Boston, MA, USA.
Stephen A HareSchool of Life Sciences, University of Sussex, Brighton, UK.
Sophie HelaineDepartment of Microbiology, Harvard Medical School, Boston, MA, USA. Sophie_Helaine@hms.harvard.edu.ORCID http://orcid.org/0000-0002-9877-4180
Harvard University · USImperial College London · GBUniversity of Sussex · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D524840/1Medical Research Council MR/M009629/1Wellcome Trust 202926/Z/16/Z
6 · The paper itself

Abstract

Toxin-antitoxin (TA) systems are a large family of genes implicated in the regulation of bacterial growth and its arrest in response to attacks. These systems encode nonsecreted toxins and antitoxins that specifically pair, even when present in several paralogous copies per genome. Salmonella enterica serovar Typhimurium contains three paralogous TacAT systems that block bacterial translation. We determined the crystal structures of the three TacAT complexes to understand the structural basis of specific TA neutralization and the evolution of such specific pairing. In the present study, we show that alteration of a discrete structural add-on element on the toxin drives specific recognition by their cognate antitoxin underpinning insulation of the three pairs. Similar to other TA families, the region supporting TA-specific pairing is key to neutralization. Our work reveals that additional TA interfaces beside the main neutralization interface increase the safe space for evolution of pairing specificity.

Indexed as

Amino Acid SequenceAntitoxinsBacteriaBacterial ToxinsCrystallizationEscherichia coliModels, MolecularProtein BindingProtein ConformationRecombinant ProteinsToxin-Antitoxin SystemsAntitoxinsBacterial ToxinsRecombinant Proteins

Identifiers

PMID34556858
OpenAlexW3201153893

What OpenQuestion holds

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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.