Evidence map›Paper›PMID 19285947›Full record

ArticleMolecular cell2009

Resampling and editing of mischarged tRNA prior to translation elongation.

Jiqiang Ling, Byung Ran So, Srujana S Yadavalli, Hervé Roy, Shinichiro Shoji, Kurt Fredrick, Karin Musier-Forsyth, Michael Ibba

Abstract read
In one paragraph

Article in Molecular cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
–field-weighted citation impact
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

54 citing papers in PubMed.

  1. Article
  2. Article
  3. Frontiers in microbiology · 2024
    Article
  4. Review
  5. Article
  6. Article
  7. Study on the Metabonomics Mechanism of Mongolian Medical Andai Therapy on Healthy People.Evidence-based complementary and alternative medicine : eCAM · 2022
    Article
  8. Article
  9. HumanThe Journal of biological chemistry · 2020
    Article
  10. Chiral checkpoints during protein biosynthesis.The Journal of biological chemistry · 2019
    Review
  11. Principles of tRNAACS omega · 2019
    Article
  12. Comparative Proteomic Analysis of Wheat CarryingInternational journal of molecular sciences · 2019
    Article
  13. Article
  14. Distinct ways of G:U recognition by conserved tRNA binding motifs.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

8 authors.

Jiqiang LingOhio State Biochemistry Program, The Ohio State University, Columbus, Ohio 43210, USA.
Byung Ran So
Srujana S Yadavalli
Hervé Roy
Shinichiro Shoji
Kurt Fredrick
Karin Musier-Forsyth
Michael Ibba

Funding

Molecular analysis of accurate ribosomal translocationR01GM072528 · NIGMS · OHIO STATE UNIVERSITY · PI Kurt L Fredrick · 2005 to 2026
$5.8M
CLASS II AMINOACYL-TRNA SYNTHETASE SUBSTRATE RECOGNITIONR01GM049928 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI MUSIER-FORSYTH, KARIN M · 1996 to 2012
$4.0M
CLASS II AMINOACYL-TRNA SYNTHETASE SUBSTRATE RECOGNITIONR29GM049928 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI MUSIER-FORSYTH, KARIN M · 1994 to 1996
–
CLASS II AMINOACYL-TRNA SYNTHETASE SUBSTRATE RECOGNITIONR55GM049928 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI MUSIER-FORSYTH, KARIN M · 1993 to 1993
–
NIGMS NIH HHS GM49928NIGMS NIH HHS GM72528NIGMS NIH HHS R01 GM049928NIGMS NIH HHS R01 GM072528
6 · The paper itself

Abstract

Faithful translation of the genetic code depends on the GTPase EF-Tu delivering correctly charged aminoacyl-tRNAs to the ribosome for pairing with cognate codons. The accurate coupling of cognate amino acids and tRNAs by the aminoacyl-tRNA synthetases is achieved through a combination of substrate specificity and product editing. Once released by aminoacyl-tRNA synthetases, both cognate and near-cognate aminoacyl-tRNAs were considered to be committed to ribosomal protein synthesis through their association with EF-Tu. Here we show instead that aminoacyl-tRNAs in ternary complex with EF-Tu*GTP can readily dissociate and rebind to aminoacyl-tRNA synthetases. For mischarged species, this allows resampling by the product editing pathway, leading to a reduction in the overall error rate of aminoacyl-tRNA synthesis. Resampling of mischarged tRNAs was shown to increase the accuracy of translation over ten fold during in vitro protein synthesis, supporting the presence of an additional quality control step prior to translation elongation.

Indexed as

Peptide Chain Elongation, TranslationalTransfer RNA AminoacylationAmino Acyl-tRNA SynthetasesBinding SitesEscherichia coliEscherichia coli ProteinsGenetic CodeGuanosine TriphosphateKineticsLeucine-tRNA LigaseNucleic Acid ConformationPeptide Elongation Factor TuPeptidesPhenylalanine-tRNA LigaseRNA, BacterialRNA, TransferAmino Acyl-tRNA SynthetasesEscherichia coli ProteinsGuanosine TriphosphateLeucine-tRNA LigasePeptide Elongation Factor TuPeptidesPhenylalanine-tRNA LigasepolyphenylalaninepolytyrosineRNA, BacterialRNA, TransferTyrosine-tRNA Ligase

Identifiers

PMID19285947
PMCPMC2944653

What OpenQuestion holds

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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.