Evidence map›Paper›PMID 27837019›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Two proofreading steps amplify the accuracy of genetic code translation.

Ka-Weng Ieong, Ülkü Uzun, Maria Selmer, Måns Ehrenberg

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Article
  2. Translation fidelity mechanisms and their changes in aging.bioRxiv : the preprint server for biology · 2026
    Article
  3. RNAViruses · 2026
    Review
  4. Article
  5. Article
  6. Unchecked growth: Pushing the limits on RNA virus genome size in the absence of known proofreading.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. The Structural Dynamics of Translation.Annual review of biochemistry · 2022
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Elongation factor-Tu can repetitively engage aminoacyl-tRNA within the ribosome during the proofreading stage of tRNA selection.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Allostery and Kinetic Proofreading.The journal of physical chemistry. B · 2019
    Article
  19. Article
  20. Ribosome Structure, Function, and Early Evolution.International journal of molecular sciences · 2018
    Review
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.

Ka-Weng IeongDepartment of Cell and Molecular Biology, Uppsala University, Uppsala 75124, Sweden.ORCID 0000-0003-4518-0618
Ülkü UzunDepartment of Cell and Molecular Biology, Uppsala University, Uppsala 75124, Sweden.
Maria SelmerDepartment of Cell and Molecular Biology, Uppsala University, Uppsala 75124, Sweden.
Måns EhrenbergDepartment of Cell and Molecular Biology, Uppsala University, Uppsala 75124, Sweden ehrenberg@xray.bmc.uu.se.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aminoacyl-tRNAs (aa-tRNAs) are selected by the messenger RNA programmed ribosome in ternary complex with elongation factor Tu (EF-Tu) and GTP and then, again, in a proofreading step after GTP hydrolysis on EF-Tu. We use tRNA mutants with different affinities for EF-Tu to demonstrate that proofreading of aa-tRNAs occurs in two consecutive steps. First, aa-tRNAs in ternary complex with EF-Tu·GDP are selected in a step where the accuracy increases linearly with increasing aa-tRNA affinity to EF-Tu. Then, following dissociation of EF-Tu·GDP from the ribosome, the accuracy is further increased in a second and apparently EF-Tu-independent step. Our findings identify the molecular basis of proofreading in bacteria, highlight the pivotal role of EF-Tu for fast and accurate protein synthesis, and illustrate the importance of multistep substrate selection in intracellular processing of genetic information.

Indexed as

Protein BiosynthesisAmino Acyl-tRNA SynthetasesGenetic CodeGuanosine DiphosphateMutationNucleic Acid ConformationPeptide Elongation Factor TuRibosomesRNA, MessengerRNA, TransferTernary Complex FactorsAmino Acyl-tRNA SynthetasesGuanosine DiphosphatePeptide Elongation Factor TuRNA, MessengerRNA, TransferTernary Complex FactorsEF-Tuerror correctionfidelityribosometernary complex

Identifiers

PMID27837019
PMCPMC5137768

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.