Evidence map›Paper›PMID 12738792›Full record

ArticleThe Journal of biological chemistry2003

RNA-structural mimicry in Escherichia coli ribosomal protein L4-dependent regulation of the S10 operon.

Ulrich Stelzl, Janice M Zengel, Marina Tovbina, Marquis Walker, Knud H Nierhaus, Lasse Lindahl, Dinshaw J Patel

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

18 citing papers in PubMed, 37 citations in OpenAlex.

  1. Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024
    Review
  2. Article
  3. Rerouting of ribosomal proteins into splicing in plant organelles.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  4. Posttranscriptional Regulation ofJournal of bacteriology · 2020
    Article
  5. Review
  6. Article
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  10. Review
  11. 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

7 authors at 3 institutions in 2 countries.

Ulrich StelzlMemorial Sloan Kettering Cancer Center, Cellular Biochemistry and Biophysics Program, New York, New York 10021, USA. u.stelzl@mdc-berlin.de
Janice M Zengel
Marina Tovbina
Marquis Walker
Knud H Nierhaus
Lasse Lindahl
Dinshaw J Patel
Memorial Sloan Kettering Cancer Center · USUniversity of Maryland, Baltimore County · USMax Planck Institute for Molecular Genetics · DE

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Elisa de Stanchina · 1985 to 2026
$347.4M
DNA COMPLEXES--ANTITUMOR DRUGS AND CHEMOTHERAPYR01CA046778 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI PATEL, DINSHAW J · 1988 to 2002
$832k
COORDINATION OF BACTERIAL RIBOSOMAL PROTEIN SYNTHESISR01GM054876 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE · PI LINDAHL, LASSE A · 1996 to 2001
$108k
NCI NIH HHS CA46778NCI NIH HHS P30 CA008748NIGMS NIH HHS GM54876
6 · The paper itself

Abstract

Ribosomal protein L4 regulates the 11-gene S10 operon in Escherichia coli by acting, in concert with transcription factor NusA, to cause premature transcription termination at a Rho-independent termination site in the leader sequence. This process presumably involves L4 interaction with the leader mRNA. Here, we report direct, specific, and independent binding of ribosomal protein L4 to the S10 mRNA leader in vitro. Most of the binding energy is contributed by a small hairpin structure within the leader region, but a 64-nucleotide sequence is required for the bona fide interaction. Binding to the S10 leader mRNA is competed by the 23 S rRNA L4 binding site. Although the secondary structures of the mRNA and rRNA binding sites appear different, phosphorothioate footprinting of the L4-RNA complexes reveals close structural similarity in three dimensions. Mutational analysis of the mRNA binding site is compatible with the structural model. In vitro binding of L4 induces structural changes of the S10 leader RNA, providing a first clue for how protein L4 may provoke transcription termination.

Indexed as

Gene Expression Regulation, Enzymologic5' Untranslated RegionsAmino Acid SequenceBase SequenceBinding, CompetitiveBinding SitesCollodionDNA Mutational AnalysisDose-Response Relationship, DrugEscherichia coliIodineModels, MolecularMolecular Sequence DataNucleic Acid ConformationPhylogenyProtein Binding5' Untranslated RegionsCollodionIodineribosomal protein L4Ribosomal ProteinsRNA, MessengerRNA, Ribosomal, 23S

Identifiers

PMID12738792
PMCPMC4692380
OpenAlexW2051027524

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.