Evidence map›Paper›PMID 27378776›Full record

ArticleNucleic acids research2016

Mechanism of endonuclease cleavage by the HigB toxin.

Marc A Schureck, Adrienne Repack, Stacey J Miles, Jhomar Marquez, Christine M Dunham

Abstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

  1. Article
  2. Very high CONAR genomics and bioinformatics · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. TheApplied and environmental microbiology · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Characterisation of Early PositiveAntibiotics (Basel, Switzerland) · 2021
    Article
  17. Article
  18. A YoeB toxin cleaves both RNA and DNA.Scientific reports · 2021
    Article
  19. Review
  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.

Marc A SchureckEmory University School of Medicine, Department of Biochemistry, 1510 Clifton Road NE, Atlanta, GA 30322, USA.
Adrienne RepackEmory University School of Medicine, Department of Biochemistry, 1510 Clifton Road NE, Atlanta, GA 30322, USA.
Stacey J MilesEmory University School of Medicine, Department of Biochemistry, 1510 Clifton Road NE, Atlanta, GA 30322, USA.
Jhomar MarquezEmory University School of Medicine, Department of Biochemistry, 1510 Clifton Road NE, Atlanta, GA 30322, USA.
Christine M DunhamEmory University School of Medicine, Department of Biochemistry, 1510 Clifton Road NE, Atlanta, GA 30322, USA christine.m.dunham@emory.edu.

Funding

Training Program in Biochemistry, Cell and Molecular BiologyT32GM008367 · NIGMS · EMORY UNIVERSITY · PI BOISE, LAWRENCE H., CORBETT, ANITA H. · 1990 to 2019
$5.6M
Structural Studies of Ribosome RegulationR01GM093278 · NIGMS · EMORY UNIVERSITY · PI DUNHAM, CHRISTINE M · 2010 to 2022
$4.6M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
Mechanism of HigB-mediated ribosome-dependent mRNA degradationF31GM108351 · NIGMS · EMORY UNIVERSITY · PI SCHURECK, MARC ANTHONY · 2013 to 2014
$62k
NCRR NIH HHS S10 RR029205NIGMS NIH HHS F31 GM108351NIGMS NIH HHS R01 GM093278NIGMS NIH HHS T32 GM008367
6 · The paper itself

Abstract

Bacteria encode multiple type II toxin-antitoxin modules that cleave ribosome-bound mRNAs in response to stress. All ribosome-dependent toxin family members structurally characterized to date adopt similar microbial RNase architectures despite possessing low sequence identities. Therefore, determining which residues are catalytically important in this specialized RNase family has been a challenge in the field. Structural studies of RelE and YoeB toxins bound to the ribosome provided significant insights but biochemical experiments with RelE were required to clearly demonstrate which residues are critical for acid-base catalysis of mRNA cleavage. Here, we solved an X-ray crystal structure of the wild-type, ribosome-dependent toxin HigB bound to the ribosome revealing potential catalytic residues proximal to the mRNA substrate. Using cell-based and biochemical assays, we further determined that HigB residues His54, Asp90, Tyr91 and His92 are critical for activity in vivo, while HigB H54A and Y91A variants have the largest effect on mRNA cleavage in vitro Comparison of X-ray crystal structures of two catalytically inactive HigB variants with 70S-HigB bound structures reveal that HigB active site residues undergo conformational rearrangements likely required for recognition of its mRNA substrate. These data support the emerging concept that ribosome-dependent toxins have diverse modes of mRNA recognition.

Indexed as

Amino Acid SequenceBacterial ToxinsCrystallography, X-RayEndoribonucleasesEscherichia coliEscherichia coli ProteinsRNA, MessengerRNA StabilityBacterial ToxinsEndoribonucleasesEscherichia coli ProteinsHigB protein, E coliRNA, Messenger

Identifiers

PMID27378776
PMCPMC5027501

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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.