Evidence map›Paper›PMID 32893724›Full record

ArticleRNA biology2021

tRNA-modifying enzyme mutations induce codon-specific mistranslation and protein aggregation in yeast.

Joana F Tavares, Nick K Davis, Ana Poim, Andreia Reis, Stefanie Kellner, Inês Sousa, Ana R Soares, Gabriela M R Moura, Peter C Dedon, Manuel Santos

Open access · bronzeAbstract read
In one paragraph

Article in RNA biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

18 citing papers in PubMed, 29 citations in OpenAlex.

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  9. The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  10. Review
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  12. Review
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  14. Article
  15. Role ofInternational journal of molecular sciences · 2021
    Article
  16. Review
  17. Urm1: A Non-Canonical UBL.Biomolecules · 2021
    Review
  18. tRNA Metabolism and Lung Cancer: Beyond Translation.Frontiers in molecular biosciences · 2021
    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

10 authors at 3 institutions in 3 countries.

Joana F TavaresDepartment of Medical Sciences, Institute of Biomedicine - iBiMED, University of Aveiro, Aveiro, Portugal.ORCID 0000-0001-7083-6266
Nick K DavisDepartment of Biological Engineering, Massachusetts Institute of Technology - MIT, Cambridge, US.
Ana PoimDepartment of Medical Sciences, Institute of Biomedicine - iBiMED, University of Aveiro, Aveiro, Portugal.ORCID 0000-0003-2947-0308
Andreia ReisDepartment of Medical Sciences, Institute of Biomedicine - iBiMED, University of Aveiro, Aveiro, Portugal.
Stefanie KellnerDepartment of Biological Engineering, Massachusetts Institute of Technology - MIT, Cambridge, US.
Inês SousaDepartment of Medical Sciences, Institute of Biomedicine - iBiMED, University of Aveiro, Aveiro, Portugal.ORCID 0000-0001-7062-5346
Ana R SoaresDepartment of Medical Sciences, Institute of Biomedicine - iBiMED, University of Aveiro, Aveiro, Portugal.ORCID 0000-0003-4000-7461
Gabriela M R MouraDepartment of Medical Sciences, Institute of Biomedicine - iBiMED, University of Aveiro, Aveiro, Portugal.
Peter C DedonDepartment of Biological Engineering, Massachusetts Institute of Technology - MIT, Cambridge, US.ORCID 0000-0003-0011-3067
Manuel SantosDepartment of Medical Sciences, Institute of Biomedicine - iBiMED, University of Aveiro, Aveiro, Portugal.
University of Aveiro · PTMassachusetts Institute of Technology · USSingapore-MIT Alliance for Research and Technology · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein synthesis rate and accuracy are tightly controlled by the cell and are essential for proteome homoeostasis (proteostasis); however, the full picture of how mRNA translational factors maintain protein synthesis accuracy and co-translational protein folding are far from being fully understood. To address this question, we evaluated the role of 70 yeast tRNA-modifying enzyme genes on protein aggregation and used mass spectrometry to identify the aggregated proteins. We show that modification of uridine at anticodon position 34 (U34) by the tRNA-modifying enzymes Elp1, Elp3, Sml3 and Trm9 is critical for proteostasis, the mitochondrial tRNA-modifying enzyme Slm3 plays a fundamental role in general proteostasis and that stress response proteins whose genes are enriched in codons decoded by tRNAs lacking mcm

Indexed as

Saccharomyces cerevisiaeCodonEnzymesMutationOrganisms, Genetically ModifiedProtein AggregatesProtein BiosynthesisProteostasisRNA Processing, Post-TranscriptionalRNA, TransferCodonEnzymesProtein AggregatesRNA, Transfer(5-10) tRNA modifying enzymesprotein aggregationproteometRNAyeast

Identifiers

PMID32893724
PMCPMC7971265
OpenAlexW3084186667

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.