Evidence map›Paper›PMID 31913314›Full record

ArticleNature communications2020

No-Go Decay mRNA cleavage in the ribosome exit tunnel produces 5'-OH ends phosphorylated by Trl1.

Albertas Navickas, Sébastien Chamois, Rénette Saint-Fort, Julien Henri, Claire Torchet, Lionel Benard

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

34 citing papers in PubMed, 58 citations in OpenAlex.

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  8. Pelota-mediated ribosome-associated quality control counteracts aging and age-associated pathologies across species.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

6 authors at 1 institution in 1 country.

Albertas NavickasInstitut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, Laboratoire de Biologie moléculaire et Cellulaire des Eucaryotes, Paris, France.ORCID http://orcid.org/0000-0003-0016-2643
Sébastien ChamoisInstitut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, Laboratoire de Biologie moléculaire et Cellulaire des Eucaryotes, Paris, France.ORCID http://orcid.org/0000-0003-3816-3748
Rénette Saint-FortInstitut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, Laboratoire de Biologie moléculaire et Cellulaire des Eucaryotes, Paris, France.
Julien HenriInstitut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, Laboratoire de Biologie moléculaire et Cellulaire des Eucaryotes, Paris, France.
Claire TorchetInstitut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, Laboratoire de Biologie moléculaire et Cellulaire des Eucaryotes, Paris, France.ORCID http://orcid.org/0000-0002-6583-823X
Lionel BenardInstitut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, Laboratoire de Biologie moléculaire et Cellulaire des Eucaryotes, Paris, France. lionel.benard@ibpc.fr.ORCID http://orcid.org/0000-0003-1745-1361
Université Claude Bernard Lyon 1 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The No-Go Decay (NGD) mRNA surveillance pathway degrades mRNAs containing stacks of stalled ribosomes. Although an endoribonuclease has been proposed to initiate cleavages upstream of the stall sequence, the production of two RNA fragments resulting from a unique cleavage has never been demonstrated. Here we use mRNAs expressing a 3'-ribozyme to produce truncated transcripts in vivo to mimic naturally occurring truncated mRNAs known to trigger NGD. This technique allows us to analyse endonucleolytic cleavage events at single-nucleotide resolution starting at the third collided ribosome, which we show to be Hel2-dependent. These cleavages map precisely in the mRNA exit tunnel of the ribosome, 8 nucleotides upstream of the first P-site residue and release 5'-hydroxylated RNA fragments requiring 5'-phosphorylation prior to digestion by the exoribonuclease Xrn1, or alternatively by Dxo1. Finally, we identify the RNA kinase Trl1, alias Rlg1, as an essential player in the degradation of NGD RNAs.

Indexed as

ExoribonucleasesPhosphorylationRibosomesRNA, FungalRNA Ligase (ATP)RNA, MessengerRNA StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsExoribonucleasesRNA, FungalRNA Ligase (ATP)RNA, MessengerSaccharomyces cerevisiae ProteinsTrl1 protein, S cerevisiaeXRN1 protein, S cerevisiae

Identifiers

PMID31913314
PMCPMC6949252
OpenAlexW2999248361

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.