Evidence map›Paper›PMID 26508639›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Defining the mRNA recognition signature of a bacterial toxin protein.

Marc A Schureck, Jack A Dunkle, Tatsuya Maehigashi, Stacey J Miles, Christine M Dunham

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.5field-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

26 citing papers in PubMed, 32 citations in OpenAlex.

  1. Interplay of the ribosome A and CAR sites.NAR genomics and bioinformatics · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. The DisorderedMicroorganisms · 2021
    Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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 1 institution in 1 country.

Marc A SchureckDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322.
Jack A DunkleDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322.
Tatsuya MaehigashiDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322.
Stacey J MilesDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322.
Christine M DunhamDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322 christine.m.dunham@emory.edu.
Emory University · US

Funding

Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI EISENBERG, DAVID · 2001 to 2011
$28.2M
Training Program in Biochemistry, Cell and Molecular BiologyT32GM008367 · NIGMS · EMORY UNIVERSITY · PI BOISE, LAWRENCE H., CORBETT, ANITA H. · 1990 to 2019
$5.6M
Mechanism of HigB-mediated ribosome-dependent mRNA degradationF31GM108351 · NIGMS · EMORY UNIVERSITY · PI SCHURECK, MARC ANTHONY · 2013 to 2014
$62k
NCRR NIH HHS P41 RR015301NCRR NIH HHS RR-15301NIGMS NIH HHS 5T32GM8367NIGMS NIH HHS F31 GM108351NIGMS NIH HHS GM108351NIGMS NIH HHS T32 GM008367
6 · The paper itself

Abstract

Bacteria contain multiple type II toxins that selectively degrade mRNAs bound to the ribosome to regulate translation and growth and facilitate survival during the stringent response. Ribosome-dependent toxins recognize a variety of three-nucleotide codons within the aminoacyl (A) site, but how these endonucleases achieve substrate specificity remains poorly understood. Here, we identify the critical features for how the host inhibition of growth B (HigB) toxin recognizes each of the three A-site nucleotides for cleavage. X-ray crystal structures of HigB bound to two different codons on the ribosome illustrate how HigB uses a microbial RNase-like nucleotide recognition loop to recognize either cytosine or adenosine at the second A-site position. Strikingly, a single HigB residue and 16S rRNA residue C1054 form an adenosine-specific pocket at the third A-site nucleotide, in contrast to how tRNAs decode mRNA. Our results demonstrate that the most important determinant for mRNA cleavage by ribosome-dependent toxins is interaction with the third A-site nucleotide.

Indexed as

Bacterial ToxinsBinding SitesCodonNucleotidesRNA, MessengerBacterial ToxinsCodonNucleotidesRNA, Messengerprotein synthesisribosomeRNasesstringent responsetoxin–antitoxin systems

Identifiers

PMID26508639
PMCPMC4653167
OpenAlexW2170702959

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.