Evidence map›Paper›PMID 29237037›Full record

ArticleNucleic acids research2018

Insights into the evolutionary conserved regulation of Rio ATPase activity.

Robert Knüppel, Regitse H Christensen, Fiona C Gray, Dominik Esser, Daniela Strauß, Jan Medenbach, Bettina Siebers, Stuart A MacNeill, Nicole LaRonde, Sébastien Ferreira-Cerca

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

26 citing papers in PubMed, 45 citations in OpenAlex.

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  12. Ribosome Biogenesis in Archaea.Frontiers in microbiology · 2021
    Review
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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

10 authors at 4 institutions in 4 countries.

Robert KnüppelBiochemistry III - Institute for Biochemistry, Genetics and Microbiology, University of Regensburg, Universitätsstraße 31, 93053 Regensburg, Germany.
Regitse H ChristensenDepartment of Biology, University of Copenhagen, Copenhagen Biocenter, University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen N, Denmark.
Fiona C GrayDepartment of Biology, University of Copenhagen, Copenhagen Biocenter, University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen N, Denmark.
Dominik EsserMolecular Enzyme Technology and Biochemistry, Biofilm Centre, Faculty of Chemistry, University of Duisburg-Essen, Universitätsstraße 5, 45141 Essen, Germany.
Daniela StraußBiochemistry I - Institute for Biochemistry, Genetics and Microbiology, University of Regensburg, Universitätsstraße 31, 93053 Regensburg, Germany.
Jan MedenbachBiochemistry I - Institute for Biochemistry, Genetics and Microbiology, University of Regensburg, Universitätsstraße 31, 93053 Regensburg, Germany.
Bettina SiebersMolecular Enzyme Technology and Biochemistry, Biofilm Centre, Faculty of Chemistry, University of Duisburg-Essen, Universitätsstraße 5, 45141 Essen, Germany.
Stuart A MacNeillDepartment of Biology, University of Copenhagen, Copenhagen Biocenter, University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen N, Denmark.
Nicole LaRondeDepartment of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA University of Maryland Marlene and Stewart Greenebaum Cancer Center, Baltimore, MD 21201, USA.
Sébastien Ferreira-CercaBiochemistry III - Institute for Biochemistry, Genetics and Microbiology, University of Regensburg, Universitätsstraße 31, 93053 Regensburg, Germany.
University of Regensburg · DEUniversity of Copenhagen · DKUniversity of Duisburg-Essen · DEUniversity of Maryland, Baltimore · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic ribosome biogenesis is a complex dynamic process which requires the action of numerous ribosome assembly factors. Among them, the eukaryotic Rio protein family members (Rio1, Rio2 and Rio3) belong to an ancient conserved atypical protein kinase/ ATPase family required for the maturation of the small ribosomal subunit (SSU). Recent structure-function analyses suggested an ATPase-dependent role of the Rio proteins to regulate their dynamic association with the nascent pre-SSU. However, the evolutionary origin of this feature and the detailed molecular mechanism that allows controlled activation of the catalytic activity remained to be determined. In this work we provide functional evidence showing a conserved role of the archaeal Rio proteins for the synthesis of the SSU in archaea. Moreover, we unravel a conserved RNA-dependent regulation of the Rio ATPases, which in the case of Rio2 involves, at least, helix 30 of the SSU rRNA and the P-loop lysine within the shared RIO domain. Together, our study suggests a ribosomal RNA-mediated regulatory mechanism enabling the appropriate stimulation of Rio2 catalytic activity and subsequent release of Rio2 from the nascent pre-40S particle. Based on our findings we propose a unified release mechanism for the Rio proteins.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateArchaeal ProteinsBinding SitesCloning, MolecularConserved SequenceEscherichia coliEvolution, MolecularGene ExpressionGenetic VectorsHaloferax volcaniiIsoenzymesKineticsModels, MolecularNucleic Acid ConformationProtein BindingAdenosine TriphosphatasesAdenosine TriphosphateArchaeal ProteinsIsoenzymesProtein Serine-Threonine KinasesRecombinant ProteinsRio1 protein, S cerevisiaeRNA, Ribosomal, 18SSaccharomyces cerevisiae Proteins

Identifiers

PMID29237037
PMCPMC5815136
OpenAlexW2773879419

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

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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.