Evidence map›Paper›PMID 24152548›Full record

ArticleRNA (New York, N.Y.)2013

The central role of protein S12 in organizing the structure of the decoding site of the ribosome.

Hasan Demirci, Leyi Wang, Frank V Murphy, Eileen L Murphy, Jennifer F Carr, Scott C Blanchard, Gerwald Jogl, Albert E Dahlberg, Steven T Gregory

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

34 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
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  15. Computational and structural biotechnology journal · 2023
    Article
  16. Review
  17. Article
  18. Improving the Methanol Tolerance of anFrontiers in microbiology · 2021
    Article
  19. Tiamulin-Resistant Mutants of the Thermophilic BacteriumAntibiotics (Basel, Switzerland) · 2020
    Article
  20. Light-inducible expression of translation factor EF-Tu during acclimation to strong light enhances the repair of photosystem II.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

9 authors at 3 institutions in 1 country.

Hasan Demirci
Leyi Wang
Frank V Murphy
Eileen L Murphy
Jennifer F Carr
Scott C Blanchard
Gerwald Jogl
Albert E Dahlberg
Steven T Gregory
Brown University · USCornell University · USArgonne National Laboratory · US

Funding

Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI RAO, ANJANA · 2001 to 2011
$28.2M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
POLYSOMES &SUBUNITS: STRUCTURE-FUNCTION RELATIONSHIPSR01GM019756 · NIGMS · BROWN UNIVERSITY · PI DAHLBERG, ALBERT E · 1985 to 2013
$8.5M
Imaging Protein Synthesis on the Ribosome using Single-Molecule FRETR01GM079238 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI BLANCHARD, SCOTT C · 2006 to 2023
$7.0M
Structural Robustness of Ribosome Functional CentersR01GM094157 · NIGMS · BROWN UNIVERSITY · PI GREGORY, STEVEN, JOGL, GERWALD · 2010 to 2024
$4.4M
INDENTATION WITH ATOMIC FORCE MICROSCOPYF32GM019756 · NIGMS · BARNES-JEWISH HOSPITAL · PI COSTA, KEVIN D · 1998 to 1998
–
NCRR NIH HHS 5P41RR015301-10NCRR NIH HHS P41 RR015301NIGMS NIH HHS 8 P41 GM103403-10NIGMS NIH HHS F32 GM019756NIGMS NIH HHS GM019756NIGMS NIH HHS GM019756-37S1NIGMS NIH HHS GM079238NIGMS NIH HHS GM094157NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM019756NIGMS NIH HHS R01 GM079238NIGMS NIH HHS R01 GM094157
6 · The paper itself

Abstract

The ribosome decodes mRNA by monitoring the geometry of codon-anticodon base-pairing using a set of universally conserved 16S rRNA nucleotides within the conformationally dynamic decoding site. By applying single-molecule FRET and X-ray crystallography, we have determined that conditional-lethal, streptomycin-dependence mutations in ribosomal protein S12 interfere with tRNA selection by allowing conformational distortions of the decoding site that impair GTPase activation of EF-Tu during the tRNA selection process. Distortions in the decoding site are reversed by streptomycin or by a second-site suppressor mutation in 16S rRNA. These observations encourage a refinement of the current model for decoding, wherein ribosomal protein S12 and the decoding site collaborate to optimize codon recognition and substrate discrimination during the early stages of the tRNA selection process.

Indexed as

Amino Acid SubstitutionBacterial ProteinsBinding SitesCrystallography, X-RayEscherichia coliModels, MolecularNucleic Acid ConformationPoint MutationProtein BindingProtein SubunitsRibosomal ProteinsRibosomesRNA, Transfer, PheThermus thermophilusBacterial ProteinsProtein SubunitsRibosomal ProteinsRNA, Transfer, PhedecodingribosomerRNAsingle-molecule FRETX-ray crystallography

Identifiers

PMID24152548
PMCPMC3884664
OpenAlexW2100394868

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.