Evidence map›Paper›PMID 24706739›Full record

ReviewJournal of bacteriology2014

Resolving nonstop translation complexes is a matter of life or death.

Kenneth C Keiler, Heather A Feaga

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

52 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Collided ribosomes are rescued by the endonuclease Rae1 andbioRxiv : the preprint server for biology · 2026
    Article
  3. Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. A cascade of structural rearrangements positions peptide release factor 2 for polypeptide hydrolysis on the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Cooperative and Independent Functionality of tmRNA and SmpB inInternational journal of molecular sciences · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Toxin-based screening of C-terminal tags inbioRxiv : the preprint server for biology · 2024
    Article
  14. Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024
    Review
  15. Article
  16. Article
  17. Degron-controlled protein degradation inbioRxiv : the preprint server for biology · 2023
    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

2 authors at 1 institution in 1 country.

Kenneth C KeilerThe Pennsylvania State University, Department of Biochemistry & Molecular Biology, University Park, Pennsylvania, USA kkeiler@psu.edu.
Heather A FeagaThe Pennsylvania State University, Department of Biochemistry & Molecular Biology, University Park, Pennsylvania, USA.
Pennsylvania State University · US

Funding

The Role of tmRNA in development of C. crescentusR01GM068720 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI KEILER, KENNETH C · 2004 to 2014
$2.3M
NIGMS NIH HHS GM68720NIGMS NIH HHS R01 GM068720
6 · The paper itself

Abstract

Problems during gene expression can result in a ribosome that has translated to the 3' end of an mRNA without terminating at a stop codon, forming a nonstop translation complex. The nonstop translation complex contains a ribosome with the mRNA and peptidyl-tRNA engaged, but because there is no codon in the A site, the ribosome cannot elongate or terminate the nascent chain. Recent work has illuminated the importance of resolving these nonstop complexes in bacteria. Transfer-messenger RNA (tmRNA)-SmpB specifically recognizes and resolves nonstop translation complexes in a reaction known as trans-translation. trans-Translation releases the ribosome and promotes degradation of the incomplete nascent polypeptide and problematic mRNA. tmRNA and SmpB have been found in all bacteria and are essential in some species. However, other bacteria can live without trans-translation because they have one of the alternative release factors, ArfA or ArfB. ArfA recruits RF2 to nonstop translation complexes to promote hydrolysis of the peptidyl-tRNAs. ArfB recognizes nonstop translation complexes in a manner similar to tmRNA-SmpB recognition and directly hydrolyzes the peptidyl-tRNAs to release the stalled ribosomes. Genetic studies indicate that most or all species require at least one mechanism to resolve nonstop translation complexes. Consistent with such a requirement, small molecules that inhibit resolution of nonstop translation complexes have broad-spectrum antibacterial activity. These results suggest that resolving nonstop translation complexes is a matter of life or death for bacteria.

Indexed as

Bacterial ProteinsGene Expression Regulation, BacterialPeptide Chain Termination, TranslationalRNA, BacterialRNA, MessengerBacterial ProteinsRNA, BacterialRNA, Messenger

Identifiers

PMID24706739
PMCPMC4054194
OpenAlexW2144547581

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.