Evidence map›Paper›PMID 27899648›Full record

ArticleNucleic acids research2017

Genetic selection for mistranslation rescues a defective co-chaperone in yeast.

Kyle S Hoffman, Matthew D Berg, Brian H Shilton, Christopher J Brandl, Patrick O'Donoghue

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

36 citing papers in PubMed, 49 citations in OpenAlex.

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  5. Mistranslating tRNA variants impact the proteome and phosphoproteome ofbioRxiv : the preprint server for biology · 2025
    Article
  6. Natural human tRNARNA (New York, N.Y.) · 2025
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  9. Review
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  11. Perseverance of protein homeostasis despite mistranslation of glycine codons with alanine.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
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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

5 authors at 1 institution in 1 country.

Kyle S HoffmanDepartment of Biochemistry, The University of Western Ontario, London, ON N6A 5C1, Canada.
Matthew D BergDepartment of Biochemistry, The University of Western Ontario, London, ON N6A 5C1, Canada.
Brian H ShiltonDepartment of Biochemistry, The University of Western Ontario, London, ON N6A 5C1, Canada.
Christopher J BrandlDepartment of Biochemistry, The University of Western Ontario, London, ON N6A 5C1, Canada.
Patrick O'DonoghueDepartment of Biochemistry, The University of Western Ontario, London, ON N6A 5C1, Canada.
Western University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite the general requirement for translation fidelity, mistranslation can be an adaptive response. We selected spontaneous second site mutations that suppress the stress sensitivity caused by a Saccharomyces cerevisiae tti2 allele with a Leu to Pro mutation at residue 187, identifying a single nucleotide mutation at the same position (C70U) in four tRNAProUGG genes. Linkage analysis and suppression by SUF9G3:U70 expressed from a centromeric plasmid confirmed the causative nature of the suppressor mutation. Since the mutation incorporates the G3:U70 identity element for alanyl-tRNA synthetase into tRNAPro, we hypothesized that suppression results from mistranslation of Pro187 in Tti2L187P as Ala. A strain expressing Tti2L187A was not stress sensitive. In vitro, tRNAProUGG (C70U) was mis-aminoacylated with alanine by alanyl-tRNA synthetase, but was not a substrate for prolyl-tRNA synthetase. Mass spectrometry from protein expressed in vivo and a novel GFP reporter for mistranslation confirmed substitution of alanine for proline at a rate of ∼6%. Mistranslating cells expressing SUF9G3:U70 induce a partial heat shock response but grow nearly identically to wild-type. Introducing the same G3:U70 mutation in SUF2 (tRNAProAGG) suppressed a second tti2 allele (tti2L50P). We have thus identified a strategy that allows mistranslation to suppress deleterious missense Pro mutations in Tti2.

Indexed as

Amino Acid SubstitutionProtein BiosynthesisSuppression, GeneticAllelesIntronsMolecular ChaperonesRNA, Transfer, ProSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSelection, GeneticMolecular ChaperonesRNA, Transfer, ProSaccharomyces cerevisiae ProteinsTti2 protein, S cerevisiae

Identifiers

PMID27899648
PMCPMC5389508
OpenAlexW2559018695

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.