Evidence map›Paper›PMID 30475795›Full record

ArticlePLoS genetics2018

Interactions between the mRNA and Rps3/uS3 at the entry tunnel of the ribosomal small subunit are important for no-go decay.

Carrie L Simms, Kyusik Q Kim, Liewei L Yan, Jessica Qiu, Hani S Zaher

Abstract 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
–field-weighted citation impact
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.

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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.

Carrie L SimmsDepartment of Biology, Washington University in St. Louis, St. Louis, Missouri, United States of America.
Kyusik Q KimDepartment of Biology, Washington University in St. Louis, St. Louis, Missouri, United States of America.ORCID 0000-0002-1832-2070
Liewei L YanDepartment of Biology, Washington University in St. Louis, St. Louis, Missouri, United States of America.ORCID 0000-0002-3692-0621
Jessica QiuDepartment of Biology, Washington University in St. Louis, St. Louis, Missouri, United States of America.ORCID 0000-0001-8626-7651
Hani S ZaherDepartment of Biology, Washington University in St. Louis, St. Louis, Missouri, United States of America.ORCID 0000-0002-7424-3617

Funding

THE ROLE OF THE RIBOSOME IN DETERMINING THE FATE OF DAMAGED MRNA-SupplementR01GM112641 · NIGMS · WASHINGTON UNIVERSITY · PI ZAHER, HANI · 2015 to 2024
$3.1M
NIGMS NIH HHS R01 GM112641
6 · The paper itself

Abstract

No-go Decay (NGD) is a process that has evolved to deal with stalled ribosomes resulting from structural blocks or aberrant mRNAs. The process is distinguished by an endonucleolytic cleavage prior to degradation of the transcript. While many of the details of the pathway have been described, the identity of the endonuclease remains unknown. Here we identify residues of the small subunit ribosomal protein Rps3 that are important for NGD by affecting the cleavage reaction. Mutation of residues within the ribosomal entry tunnel that contact the incoming mRNA leads to significantly reduced accumulation of cleavage products, independent of the type of stall sequence, and renders cells sensitive to damaging agents thought to trigger NGD. These phenotypes are distinct from those seen in combination with other NGD factors, suggesting a separate role for Rps3 in NGD. Conversely, ribosomal proteins ubiquitination is not affected by rps3 mutations, indicating that upstream ribosome quality control (RQC) events are not dependent on these residues. Together, these results suggest that Rps3 is important for quality control on the ribosome and strongly supports the notion that the ribosome itself plays a central role in the endonucleolytic cleavage reaction during NGD.

Indexed as

RNA StabilityAdaptor Proteins, Signal TransducingAmino Acid SequenceAmino Acid SubstitutionCell Cycle ProteinsEndoribonucleasesGenes, FungalGTP-Binding ProteinsModels, MolecularMutagenesis, Site-DirectedMutationPeptide Chain Elongation, TranslationalProtein ConformationRibosomal ProteinsRibosome Subunits, SmallRNA, FungalAdaptor Proteins, Signal TransducingASC1 protein, S cerevisiaeCell Cycle ProteinsDom34 protein, S cerevisiaeEndoribonucleasesGTP-Binding ProteinsRibosomal ProteinsRNA, FungalRNA, MessengerRPS3 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID30475795
PMCPMC6283612

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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.