Evidence map›Paper›PMID 22334680›Full record

ArticleThe Journal of biological chemistry2012

Molecular structure and function of the novel BrnT/BrnA toxin-antitoxin system of Brucella abortus.

Brook E Heaton, Julien Herrou, Anne E Blackwell, Vicki H Wysocki, Sean Crosson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
2.9field-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

51 citing papers in PubMed, 78 citations in OpenAlex.

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  9. Genomic analysis of prophages in 44 clinical strains ofFrontiers in cellular and infection microbiology · 2025
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  18. Ribonuclease T2 represents a distinct circularly permutated version of the BECR RNases.Protein science : a publication of the Protein Society · 2023
    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

5 authors at 3 institutions in 1 country.

Brook E HeatonCommittee on Microbiology, University of Chicago, Chicago, Illinois 60637, USA.
Julien Herrou
Anne E Blackwell
Vicki H Wysocki
Sean Crosson
University of Arizona · USUniversity of Chicago · USArgonne National Laboratory · US

Funding

Vaccines and Diagnostics TrialsU54AI065359 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI BARBOUR, ALAN G. · 2005 to 2013
$88.8M
Vaccines and Therapies Against BotulismU54AI057153 · NIAID · UNIVERSITY OF CHICAGO · PI SHUMAN, HOWARD A · 2003 to 2013
$87.6M
NIAID NIH HHS 1-U54-AI-057153NIAID NIH HHS 1U54-AI-065359NIAID NIH HHS U54 AI057153NIAID NIH HHS U54 AI065359
6 · The paper itself

Abstract

Type II toxin-antitoxin (TA) systems are expressed from two-gene operons that encode a cytoplasmic protein toxin and its cognate protein antitoxin. These gene cassettes are often present in multiple copies on bacterial chromosomes, where they have been reported to regulate stress adaptation and persistence during antimicrobial treatment. We have identified a novel type II TA cassette in the intracellular pathogen Brucella abortus that consists of the toxin gene, brnT, and its antitoxin, brnA. BrnT is coexpressed and forms a 2:2 tetrameric complex with BrnA, which neutralizes BrnT toxicity. The BrnT(2)-BrnA(2) tetramer binds its own promoter via BrnA, and autorepresses its expression; its transcription is strongly induced in B. abortus by various stressors encountered by the bacterial cell during infection of a mammalian host. Although highly divergent at the primary sequence level, an atomic resolution (1.1 Å) crystal structure of BrnT reveals a secondary topology related to the RelE family of type II ribonuclease toxins. However, overall tertiary structural homology to other RelE family toxins is low. A functional characterization of BrnT by site-directed mutagenesis demonstrates a correspondence between its in vitro activity as a ribonuclease and control of bacteriostasis in vivo. We further present an analysis of the conserved and variable features of structure required for RNA scission in BrnT and the RelE toxin family. This structural investigation informs a model of the RelE-fold as an evolutionarily flexible scaffold that has been selected to bind structurally disparate antitoxins, and exhibit distinct toxin activities including RNA scission and DNA gyrase inhibition.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionBacterial ProteinsBacterial ToxinsBrucella abortusCrystallography, X-RayEscherichia coliGene Expression Regulation, BacterialMicrobial ViabilityModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedOperonProtein BindingProtein Structure, QuaternaryProtein Structure, SecondaryBacterial ProteinsBacterial ToxinsRecombinant ProteinsRibonucleases

Identifiers

PMID22334680
PMCPMC3320955
OpenAlexW2040558557

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.