Evidence map›Paper›PMID 21460219›Full record

ArticleThe Journal of biological chemistry2011

RNA binding targets aminoacyl-tRNA synthetases to translating ribosomes.

Alexandre David, Nir Netzer, Michael Brad Strader, Suman R Das, Cai Yun Chen, James Gibbs, Philippe Pierre, Jack R Bennink, Jonathan W Yewdell

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing 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

57 citing papers in PubMed.

  1. Review
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  3. Article
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  5. Review
  6. Article
  7. Multimodal cotranslational interactions direct assembly of the human multi-tRNA synthetase complex.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Local translation in nuclear condensate amyloid bodies.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Emerging translation strategies during virus-host interaction.Wiley interdisciplinary reviews. RNA · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Review
  19. The GAIT translational control system.Wiley interdisciplinary reviews. RNA · 2018
    Review
  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

9 authors.

Alexandre DavidLaboratory of Viral Diseases, NIAID, National Institutes of Health, Bethesda, Maryland 20892, USA.
Nir Netzer
Michael Brad Strader
Suman R Das
Cai Yun Chen
James Gibbs
Philippe Pierre
Jack R Bennink
Jonathan W Yewdell

Funding

Processing Of Viral Proteins For T Cell RecognitionZIAAI000542 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI YEWDELL, JONATHAN W · 2009 to 2015
$2.8M
Intramural NIH HHS
6 · The paper itself

Abstract

Here, we examine tRNA-aminoacyl synthetase (ARS) localization in protein synthesis. Proteomics reveals that ten of the twenty cytosolic ARSs associate with ribosomes in sucrose gradients: phenylalanyl-RS (FRS), and the 9 ARSs that form the multi-ARS complex (MSC). Using the ribopuromycylation method (RPM) for localizing intracellular translation, we show that FRS and the MSC, and to a lesser extent other ARSs, localize to translating ribosomes, most strikingly when translation is restricted to poxvirus or alphavirus factories in infected cells. Immunoproximity fluorescence indicates close proximity between MSC and the ribosome. Stress induced-translational shutdown recruits the MSC to stress-granules, a depot for mRNA and translation components. MSC binding to mRNA provides a facile explanation for its delivery to translating ribosomes and stress granules. These findings, along with the abundance of the MSC (9 × 10(6) copies per cell, roughly equimolar with ribosomes), is consistent with the idea that MSC specificity, recently reported to vary with cellular stress (Netzer, N., Goodenbour, J. M., David, A., Dittmar, K. A., Jones, R. B., Schneider, J. R., Boone, D., Eves, E. M., Rosner, M. R., Gibbs, J. S., Embry, A., Dolan, B., Das, S., Hickman, H. D., Berglund, P., Bennink, J. R., Yewdell, J. W., and Pan, T. (2009) Nature 462, 522-526) can be modulated at the level of individual mRNAs to modify decoding of specific gene products.

Indexed as

AlphavirusAlphavirus InfectionsAmino Acyl-tRNA SynthetasesHEK293 CellsHeLa CellsHumansPoxviridaePoxviridae InfectionsProtein BiosynthesisRibosomesRNA, MessengerAmino Acyl-tRNA SynthetasesRNA, Messenger

Identifiers

PMID21460219
PMCPMC3121505

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.