Evidence map›Paper›PMID 31909713›Full record

ArticleeLife2020

The GTPase Nog1 co-ordinates the assembly, maturation and quality control of distant ribosomal functional centers.

Purnima Klingauf-Nerurkar, Ludovic C Gillet, Daniela Portugal-Calisto, Michaela Oborská-Oplová, Martin Jäger, Olga T Schubert, Agnese Pisano, Cohue Peña, Sanjana Rao, Martin Altvater and 3 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 46 citations in OpenAlex.

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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

13 authors at 3 institutions in 2 countries.

Purnima Klingauf-Nerurkar *Institute of Medical Microbiology, University of Zurich, Zurich, Switzerland.
Ludovic C Gillet *Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.ORCID 0000-0002-1001-3265
Daniela Portugal-CalistoInstitute of Medical Microbiology, University of Zurich, Zurich, Switzerland.ORCID 0000-0003-1591-5812
Michaela Oborská-OplováInstitute of Medical Microbiology, University of Zurich, Zurich, Switzerland.ORCID 0000-0003-0976-4341
Martin JägerInstitute of Biochemistry, ETH Zurich, Zurich, Switzerland.
Olga T SchubertInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.ORCID 0000-0002-2613-0714
Agnese PisanoInstitute of Medical Microbiology, University of Zurich, Zurich, Switzerland.
Cohue PeñaInstitute of Medical Microbiology, University of Zurich, Zurich, Switzerland.
Sanjana RaoInstitute of Medical Microbiology, University of Zurich, Zurich, Switzerland.
Martin AltvaterInstitute of Biochemistry, ETH Zurich, Zurich, Switzerland.
Yiming ChangInstitute of Biochemistry, ETH Zurich, Zurich, Switzerland.
Ruedi AebersoldInstitute of Medical Microbiology, University of Zurich, Zurich, Switzerland.
Vikram G PanseInstitute of Medical Microbiology, University of Zurich, Zurich, Switzerland.ORCID 0000-0001-7950-5746
University of Zurich · CHETH Zurich · CHUniversity of California, Los Angeles · US

Funding

H2020 European Research Council EURIBIO
6 · The paper itself

Abstract

Eukaryotic ribosome precursors acquire translation competence in the cytoplasm through stepwise release of bound assembly factors, and proofreading of their functional centers. In case of the pre-60S, these steps include removal of placeholders Rlp24, Arx1 and Mrt4 that prevent premature loading of the ribosomal protein eL24, the protein-folding machinery at the polypeptide exit tunnel (PET), and the ribosomal stalk, respectively. Here, we reveal that sequential ATPase and GTPase activities license release factors Rei1 and Yvh1 to trigger Arx1 and Mrt4 removal. Drg1-ATPase activity removes Rlp24 from the GTPase Nog1 on the pre-60S; consequently, the C-terminal tail of Nog1 is extracted from the PET. These events enable Rei1 to probe PET integrity and catalyze Arx1 release. Concomitantly, Nog1 eviction from the pre-60S permits peptidyl transferase center maturation, and allows Yvh1 to mediate Mrt4 release for stalk assembly. Thus, Nog1 co-ordinates the assembly, maturation and quality control of distant functional centers during ribosome formation.

Indexed as

GTP-Binding ProteinsNuclear ProteinsRibosomal ProteinsRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsGTP-Binding ProteinsNOG1 protein, S cerevisiaeNuclear ProteinsRibosomal ProteinsSaccharomyces cerevisiae Proteinsbiochemistrychemical biologycytoplasmic maturationribosome assemblyribosome quality controlS. cerevisiae

Identifiers

PMID31909713
PMCPMC6968927
OpenAlexW3000744971

What OpenQuestion holds

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LicenceCC BY
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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.