Evidence map›Paper›PMID 30911188›Full record

ArticleNature structural & molecular biology2019

Structure of the 80S ribosome-Xrn1 nuclease complex.

Petr Tesina, Elisabeth Heckel, Jingdong Cheng, Micheline Fromont-Racine, Robert Buschauer, Lukas Kater, Birgitta Beatrix, Otto Berninghausen, Alain Jacquier, Thomas Becker and 1 more

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

53 citing papers in PubMed, 93 citations in OpenAlex.

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  18. Quantification of gallium cryo-FIB milling damage in biological lamellae.Proceedings of the National Academy of Sciences of the United States of America · 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

11 authors at 2 institutions in 2 countries.

Petr TesinaGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.ORCID http://orcid.org/0000-0002-5227-1799
Elisabeth HeckelGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Jingdong ChengGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.ORCID http://orcid.org/0000-0003-4442-377X
Micheline Fromont-RacineInstitut Pasteur, Génétique des Interactions Macromoléculaires, Centre National de la Recherche Scientifique, Unité Mixte de Recherche, Paris, France.
Robert BuschauerGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Lukas KaterGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Birgitta BeatrixGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.ORCID http://orcid.org/0000-0001-5568-8533
Otto BerninghausenGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.ORCID http://orcid.org/0000-0002-9255-0522
Alain JacquierInstitut Pasteur, Génétique des Interactions Macromoléculaires, Centre National de la Recherche Scientifique, Unité Mixte de Recherche, Paris, France. alain.jacquier@pasteur.fr.ORCID http://orcid.org/0000-0001-5707-9184
Thomas BeckerGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany. becker@genzentrum.lmu.de.ORCID http://orcid.org/0000-0001-8458-2738
Roland BeckmannGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany. beckmann@genzentrum.lmu.de.ORCID http://orcid.org/0000-0003-4291-3898
Center for Integrated Protein Science Munich · DEInstitut Pasteur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Messenger RNA (mRNA) homeostasis represents an essential part of gene expression, in which the generation of mRNA by RNA polymerase is counter-balanced by its degradation by nucleases. The conserved 5'-to-3' exoribonuclease Xrn1 has a crucial role in eukaryotic mRNA homeostasis by degrading decapped or cleaved mRNAs post-translationally and, more surprisingly, also co-translationally. Here we report that active Xrn1 can directly and specifically interact with the translation machinery. A cryo-electron microscopy structure of a programmed Saccharomyces cerevisiae 80S ribosome-Xrn1 nuclease complex reveals how the conserved core of Xrn1 enables binding at the mRNA exit site of the ribosome. This interface provides a conduit for channelling of the mRNA from the ribosomal decoding site directly into the active center of the nuclease, thus separating mRNA decoding from degradation by only 17 ± 1 nucleotides. These findings explain how rapid 5'-to-3' mRNA degradation is coupled efficiently to its final round of mRNA translation.

Indexed as

Cryoelectron MicroscopyExoribonucleasesRibosomesRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsExoribonucleasesRNA, MessengerSaccharomyces cerevisiae ProteinsXRN1 protein, S cerevisiae

Identifiers

PMID30911188
OpenAlexW2924025784

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.