Evidence map›Paper›PMID 17392345›Full record

ArticleNucleic acids research2007

Ribosomal protein S1 influences trans-translation in vitro and in vivo.

Matthieu Saguy, Reynald Gillet, Patricia Skorski, Sylvie Hermann-Le Denmat, Brice Felden

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2007. 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
1.3field-weighted citation impact, top 20% 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, 49 citations in OpenAlex.

  1. Article
  2. Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024
    Review
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  16. Molecular biology of drug resistance in Mycobacterium tuberculosis.Current topics in microbiology and immunology · 2013
    Review
  17. Ribosomal protein S1 unwinds double-stranded RNA in multiple steps.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  18. Article
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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 2 countries.

Matthieu SaguyUniversité de Rennes 1, UPRES 2311, Inserm U835, Biochimie Pharmaceutique, Rennes, France.
Reynald Gillet
Patricia Skorski
Sylvie Hermann-Le Denmat
Brice Felden
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

When the bacterial ribosome stalls on a truncated mRNA, transfer-messenger RNA (tmRNA) acts initially as a transfer RNA (tRNA) and then as a messenger RNA (mRNA) to rescue the ribosome and add a peptide tag to the nascent polypeptide that targets it for degradation. Ribosomal protein S1 binds tmRNA but its functional role in this process has remained elusive. In this report, we demonstrate that, in vitro, S1 is dispensable for the tRNA-like role of tmRNA but is essential for its mRNA function. Increasing or decreasing the amount of protein S1 in vivo reduces the overall amount of trans-translated proteins. Also, a truncated S1 protein impaired for ribosome binding can still trigger protein tagging, suggesting that S1 interacts with tmRNA outside the ribosome to keep it in an active state. Overall, these results demonstrate that S1 has a role in tmRNA-mediated tagging that is distinct from its role during canonical translation.

Indexed as

Protein BiosynthesisCodonEscherichia coliMutationRibosomal ProteinsRibosomesRNA, BacterialRNA, MessengerCodonRibosomal Proteinsribosomal protein S1RNA, BacterialRNA, MessengertmRNA

Identifiers

PMID17392345
PMCPMC1874662
OpenAlexW2157401644

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.