Evidence map›Paper›PMID 33637717›Full record

ArticleNature communications2021

The TUTase URT1 connects decapping activators and prevents the accumulation of excessively deadenylated mRNAs to avoid siRNA biogenesis.

Hélène Scheer, Caroline de Almeida, Emilie Ferrier, Quentin Simonnot, Laure Poirier, David Pflieger, François M Sement, Sandrine Koechler, Christina Piermaria, Paweł Krawczyk and 7 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

35 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. TheProceedings of the National Academy of Sciences of the United States of America · 2026
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  8. Epigenetics in the modern era of crop improvements.Science China. Life sciences · 2025
    Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. The plant siRNA landscape.The Plant cell · 2024
    Review
  17. Article
  18. Article
  19. 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

17 authors at 2 institutions in 2 countries.

Hélène Scheer *Institut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France.
Caroline de Almeida *Institut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France.
Emilie FerrierInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France.
Quentin SimonnotInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France.
Laure PoirierInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France.
David PfliegerInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France.
François M SementInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France.
Sandrine KoechlerInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France.
Christina PiermariaPlateforme Protéomique Strasbourg Esplanade du CNRS, Université de Strasbourg, Strasbourg, France.ORCID 0000-0001-6873-4113
Paweł KrawczykLaboratory of RNA Biology, International Institute of Molecular and Cell Biology, Warsaw, Poland.ORCID 0000-0001-9531-1298
Seweryn MroczekLaboratory of RNA Biology, International Institute of Molecular and Cell Biology, Warsaw, Poland.ORCID 0000-0001-5026-1741
Johana ChicherPlateforme Protéomique Strasbourg Esplanade du CNRS, Université de Strasbourg, Strasbourg, France.ORCID 0000-0002-4403-7484
Lauriane KuhnPlateforme Protéomique Strasbourg Esplanade du CNRS, Université de Strasbourg, Strasbourg, France.ORCID 0000-0002-2637-1024
Andrzej DziembowskiLaboratory of RNA Biology, International Institute of Molecular and Cell Biology, Warsaw, Poland.
Philippe HammannPlateforme Protéomique Strasbourg Esplanade du CNRS, Université de Strasbourg, Strasbourg, France.
Hélène ZuberInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France. helene.zuber@ibmp-cnrs.unistra.fr.ORCID 0000-0002-2132-4536
Dominique GagliardiInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France. dominique.gagliardi@ibmp-cnrs.unistra.fr.ORCID 0000-0002-5871-7544
Centre National de la Recherche Scientifique · FRInternational Institute of Molecular and Cell Biology · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Uridylation is a widespread modification destabilizing eukaryotic mRNAs. Yet, molecular mechanisms underlying TUTase-mediated mRNA degradation remain mostly unresolved. Here, we report that the Arabidopsis TUTase URT1 participates in a molecular network connecting several translational repressors/decapping activators. URT1 directly interacts with DECAPPING 5 (DCP5), the Arabidopsis ortholog of human LSM14 and yeast Scd6, and this interaction connects URT1 to additional decay factors like DDX6/Dhh1-like RNA helicases. Nanopore direct RNA sequencing reveals a global role of URT1 in shaping poly(A) tail length, notably by preventing the accumulation of excessively deadenylated mRNAs. Based on in vitro and in planta data, we propose a model that explains how URT1 could reduce the accumulation of oligo(A)-tailed mRNAs both by favoring their degradation and because 3' terminal uridines intrinsically hinder deadenylation. Importantly, preventing the accumulation of excessively deadenylated mRNAs avoids the biogenesis of illegitimate siRNAs that silence endogenous mRNAs and perturb Arabidopsis growth and development.

Indexed as

ArabidopsisArabidopsis ProteinsCo-Repressor ProteinsDEAD-box RNA HelicasesGene Expression Regulation, PlantHumansNicotianaProto-Oncogene ProteinsRibonucleoproteinsRNA, MessengerRNA NucleotidyltransferasesRNA, Small InterferingRNA StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscriptomeArabidopsis ProteinsCo-Repressor ProteinsDCP5 protein, ArabidopsisDDX6 protein, humanDEAD-box RNA HelicasesDHH1 protein, S cerevisiaeProto-Oncogene ProteinsRibonucleoproteinsRNA-associated protein 55, humanRNA, MessengerRNA NucleotidyltransferasesRNA, Small InterferingSaccharomyces cerevisiae ProteinsScd6 protein, S cerevisiaeUridineURT1 protein, Arabidopsis

Identifiers

PMID33637717
PMCPMC7910438
OpenAlexW3129539500

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.