Evidence map›Paper›PMID 23824292›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Blasticidin S inhibits translation by trapping deformed tRNA on the ribosome.

Egor Svidritskiy, Clarence Ling, Dmitri N Ermolenko, Andrei A Korostelev

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
3.4field-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

62 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Article
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  4. Article
  5. Article
  6. Article
  7. Microbial production of 5-Applied and environmental microbiology · 2024
    Article
  8. Article
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  10. Hibernating ribosomes as drug targets?Frontiers in microbiology · 2024
    Review
  11. Biosynthesis and Genome Mining Potentials of Nucleoside Natural Products.Chembiochem : a European journal of chemical biology · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. RadicalJournal of the American Chemical Society · 2022
    Article
  20. Article

2 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 1 country.

Egor SvidritskiyRNA Therapeutics Institute, Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Clarence Ling
Dmitri N Ermolenko
Andrei A Korostelev
University of Massachusetts Chan Medical School · USUniversity of Rochester · US

Funding

Training in Cellular, Biochemical and Molecular SciencesT32GM068411 · NIGMS · UNIVERSITY OF ROCHESTER · PI MAQUAT, LYNNE E · 2005 to 2019
$3.9M
Structural Dynamics of TranslationR01GM099719 · NIGMS · UNIVERSITY OF ROCHESTER · PI ERMOLENKO, DMITRI · 2012 to 2020
$2.8M
Faculty Recruitment for the University of Rochester Center for RNA Biology CoreP30GM092424 · NIGMS · UNIVERSITY OF ROCHESTER · PI MAQUAT, LYNNE E · 2009 to 2010
$767k
NIGMS NIH HHS GM-099719NIGMS NIH HHS P30 GM092424NIGMS NIH HHS R01 GM099719NIGMS NIH HHS T32 GM068411
6 · The paper itself

Abstract

The antibiotic blasticidin S (BlaS) is a potent inhibitor of protein synthesis in bacteria and eukaryotes. We have determined a 3.4-Å crystal structure of BlaS bound to a 70S⋅tRNA ribosome complex and performed biochemical and single-molecule FRET experiments to determine the mechanism of action of the antibiotic. We find that BlaS enhances tRNA binding to the P site of the large ribosomal subunit and slows down spontaneous intersubunit rotation in pretranslocation ribosomes. However, the antibiotic has negligible effect on elongation factor G catalyzed translocation of tRNA and mRNA. The crystal structure of the antibiotic-ribosome complex reveals that BlaS impedes protein synthesis through a unique mechanism by bending the 3' terminus of the P-site tRNA toward the A site of the large ribosomal subunit. Biochemical experiments demonstrate that stabilization of the deformed conformation of the P-site tRNA by BlaS strongly inhibits peptidyl-tRNA hydrolysis by release factors and, to a lesser extent, peptide bond formation.

Indexed as

Crystallography, X-RayFluorescence Resonance Energy TransferModels, MolecularNucleosidesProtein BiosynthesisRibosomesRNA, TransferThermus thermophilusblasticidin SNucleosidesRNA, Transferpeptidyl transferribosome crystal structuretermination inhibitortranslation inhibitortranslation termination

Identifiers

PMID23824292
PMCPMC3725078
OpenAlexW2063647838

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.