Evidence map›Paper›PMID 30059503›Full record

ArticlePLoS genetics2018

The Lsm1-7/Pat1 complex binds to stress-activated mRNAs and modulates the response to hyperosmotic shock.

Elena Garre, Vicent Pelechano, Manuel Sánchez Del Pino, Paula Alepuz, Per Sunnerhagen

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

20 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  11. Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022
    Review
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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 3 institutions in 2 countries.

Elena GarreDepartment of Chemistry and Molecular Biology, University of Gothenburg, Göteborg, Sweden.ORCID 0000-0002-3827-4977
Vicent PelechanoSciLifeLab, Department of Microbiology, Tumor, and Cell Biology, Karolinska Institute, Stockholm, Sweden.ORCID 0000-0002-9415-788X
Manuel Sánchez Del PinoDepartamento de Bioquímica y Biología Molecular, Universitat de València, Burjassot, Valencia, Spain.ORCID 0000-0001-9696-7600
Paula AlepuzDepartamento de Bioquímica y Biología Molecular, Universitat de València, Burjassot, Valencia, Spain.
Per SunnerhagenDepartment of Chemistry and Molecular Biology, University of Gothenburg, Göteborg, Sweden.ORCID 0000-0002-0967-8729
Universitat de València · ESUniversity of Gothenburg · SEScience for Life Laboratory · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA-binding proteins (RBPs) establish the cellular fate of a transcript, but an understanding of these processes has been limited by a lack of identified specific interactions between RNA and protein molecules. Using MS2 RNA tagging, we have purified proteins associated with individual mRNA species induced by osmotic stress, STL1 and GPD1. We found members of the Lsm1-7/Pat1 RBP complex to preferentially bind these mRNAs, relative to the non-stress induced mRNAs, HYP2 and ASH1. To assess the functional importance, we mutated components of the Lsm1-7/Pat1 RBP complex and analyzed the impact on expression of osmostress gene products. We observed a defect in global translation inhibition under osmotic stress in pat1 and lsm1 mutants, which correlated with an abnormally high association of both non-stress and stress-induced mRNAs to translationally active polysomes. Additionally, for stress-induced proteins normally triggered only by moderate or high osmostress, in the mutants the protein levels rose high already at weak hyperosmosis. Analysis of ribosome passage on mRNAs through co-translational decay from the 5' end (5P-Seq) showed increased ribosome accumulation in lsm1 and pat1 mutants upstream of the start codon. This effect was particularly strong for mRNAs induced under osmostress. Thus, our results indicate that, in addition to its role in degradation, the Lsm1-7/Pat1 complex acts as a selective translational repressor, having stronger effect over the translation initiation of heavily expressed mRNAs. Binding of the Lsm1-7/Pat1p complex to osmostress-induced mRNAs mitigates their translation, suppressing it in conditions of weak or no stress, and avoiding a hyperresponse when triggered.

Indexed as

Glycerol-3-Phosphate Dehydrogenase (NAD+)Membrane Transport ProteinsOsmotic PressureProtein BindingProtein BiosynthesisRepressor ProteinsRNA-Binding ProteinsRNA Cap-Binding ProteinsRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsASH1 protein, S cerevisiaeGlycerol-3-Phosphate Dehydrogenase (NAD+)GPD1 protein, S cerevisiaeLSM1 protein, S cerevisiaeMembrane Transport ProteinsPAT1 protein, S cerevisiaeRepressor ProteinsRNA-Binding ProteinsRNA Cap-Binding ProteinsRNA, MessengerSaccharomyces cerevisiae ProteinsSTL1 protein, S cerevisiae

Identifiers

PMID30059503
PMCPMC6085073
OpenAlexW2883978003

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.