Evidence map›Paper›PMID 12682022›Full record

ArticleThe EMBO journal2003

Ribosomal protein S15 represses its own translation via adaptation of an rRNA-like fold within its mRNA.

Alexander Serganov, Ann Polonskaia, Bernard Ehresmann, Chantal Ehresmann, Dinshaw J Patel

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

29 citing papers in PubMed, 62 citations in OpenAlex.

  1. Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024
    Review
  2. Article
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  5. Rerouting of ribosomal proteins into splicing in plant organelles.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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  8. Review
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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 1 country.

Alexander SerganovCellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
Ann Polonskaia
Bernard Ehresmann
Chantal Ehresmann
Dinshaw J Patel
Memorial Sloan Kettering Cancer Center · US

Funding

DNA COMPLEXES--ANTITUMOR DRUGS AND CHEMOTHERAPYR01CA046778 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI PATEL, DINSHAW J · 1988 to 2002
$832k
NCI NIH HHS CA46778
6 · The paper itself

Abstract

The 16S rRNA-binding ribosomal protein S15 is a key component in the assembly of the small ribosomal subunit in bacteria. We have shown that S15 from the extreme thermophile Thermus thermophilus represses the translation of its own mRNA in vitro, by interacting with the leader segment of its mRNA. The S15 mRNA-binding site was characterized by footprinting experiments, deletion analysis and site-directed mutagenesis. S15 binding triggers a conformational rearrangement of its mRNA into a fold that mimics the conserved three-way junction of the S15 rRNA-binding site. This conformational change masks the ribosome entry site, as demonstrated by direct competition between the ribosomal subunit and S15 for mRNA binding. A comparison of the T.thermophilus and Escherichia coli regulation systems reveals that the two regulatory mRNA targets do not share any similarity and that the mechanisms of translational inhibition are different. Our results highlight an astonishing plasticity of mRNA in its ability to adapt to evolutionary constraints, that contrasts with the extreme conservation of the rRNA-binding site.

Indexed as

Nucleic Acid ConformationProtein BiosynthesisBacterial ProteinsBinding SitesProtein BindingProtein FootprintingRepressor ProteinsRibosomal ProteinsRibosomesRNA, MessengerThermus thermophilusBacterial ProteinsRepressor ProteinsRibosomal Proteinsribosomal protein S15RNA, Messenger

Identifiers

PMID12682022
PMCPMC154462
OpenAlexW2053649551

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.