Evidence map›Paper›PMID 25404745›Full record

ArticleThe Journal of cell biology2014

A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation.

Jochen Baßler, Helge Paternoga, Iris Holdermann, Matthias Thoms, Sander Granneman, Clara Barrio-Garcia, Afua Nyarko, Woonghee Lee, Gunter Stier, Sarah A Clark and 7 more

Erratum issuedAbstract read
In one paragraph

Article in The Journal of cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing 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

38 citing papers in PubMed.

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  20. Interaction network of the ribosome assembly machinery from a eukaryotic thermophile.Protein science : a publication of the Protein Society · 2017
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

17 authors.

Jochen BaßlerBiochemistry Center of Heidelberg University, INF328, D-69120 Heidelberg, Germany.
Helge PaternogaBiochemistry Center of Heidelberg University, INF328, D-69120 Heidelberg, Germany.
Iris HoldermannBiochemistry Center of Heidelberg University, INF328, D-69120 Heidelberg, Germany.
Matthias ThomsBiochemistry Center of Heidelberg University, INF328, D-69120 Heidelberg, Germany.
Sander GrannemanCentre for Synthetic and Systems Biology (SynthSys) and Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh EH9 3BF, Scotland, UK.
Clara Barrio-GarciaGene Center, Department of Chemistry and Biochemistry, University of Munich, 80539 Munich, Germany.
Afua NyarkoDepartment of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331.
Woonghee LeeNational Magnetic Resonance Facility; Biochemistry Department, University of Wisconsin-Madison, Madison, WI 53706.
Gunter StierBiochemistry Center of Heidelberg University, INF328, D-69120 Heidelberg, Germany.
Sarah A ClarkDepartment of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331.
Daniel SchraivogelBiochemistry Center of Heidelberg University, INF328, D-69120 Heidelberg, Germany.
Martina KallasBiochemistry Center of Heidelberg University, INF328, D-69120 Heidelberg, Germany.
Roland BeckmannGene Center, Department of Chemistry and Biochemistry, University of Munich, 80539 Munich, Germany.
David TollerveyCentre for Synthetic and Systems Biology (SynthSys) and Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh EH9 3BF, Scotland, UK.
Elisar BarbarDepartment of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331 ed.hurt@bzh.uni-heidelberg.de irmi.sinning@bzh.uni-heidelberg.de barbare@science.oregonstate.edu.
Irmi SinningBiochemistry Center of Heidelberg University, INF328, D-69120 Heidelberg, Germany ed.hurt@bzh.uni-heidelberg.de irmi.sinning@bzh.uni-heidelberg.de barbare@science.oregonstate.edu.
Ed HurtBiochemistry Center of Heidelberg University, INF328, D-69120 Heidelberg, Germany ed.hurt@bzh.uni-heidelberg.de irmi.sinning@bzh.uni-heidelberg.de barbare@science.oregonstate.edu.

Funding

Dynein light chain as a dimerization hub for natively disordered proteinsR01GM084276 · NIGMS · OREGON STATE UNIVERSITY · PI BARBAR, ELISAR J · 2009 to 2013
$1.5M
NIGMS NIH HHS R01 GM084276Wellcome Trust 077248Wellcome Trust 092076
6 · The paper itself

Abstract

Eukaryotic ribosome biogenesis involves ∼200 assembly factors, but how these contribute to ribosome maturation is poorly understood. Here, we identify a network of factors on the nascent 60S subunit that actively remodels preribosome structure. At its hub is Rsa4, a direct substrate of the force-generating ATPase Rea1. We show that Rsa4 is connected to the central protuberance by binding to Rpl5 and to ribosomal RNA (rRNA) helix 89 of the nascent peptidyl transferase center (PTC) through Nsa2. Importantly, Nsa2 binds to helix 89 before relocation of helix 89 to the PTC. Structure-based mutations of these factors reveal the functional importance of their interactions for ribosome assembly. Thus, Rsa4 is held tightly in the preribosome and can serve as a "distribution box," transmitting remodeling energy from Rea1 into the developing ribosome. We suggest that a relay-like factor network coupled to a mechano-enzyme is strategically positioned to relocate rRNA elements during ribosome maturation.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceATPases Associated with Diverse Cellular ActivitiesCrystallography, X-RayEscherichia coliMolecular Sequence DataProtein Structure, TertiaryRecombinant Fusion ProteinsRibosomal ProteinsRibosome Subunits, Large, EukaryoticRNA-Binding ProteinsRNA, RibosomalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesMDN1 protein, S cerevisiaeNsa2 protein, S cerevisiaeRecombinant Fusion Proteinsribosomal protein L25Ribosomal ProteinsRNA-Binding ProteinsRNA, RibosomalRPL5 protein, S cerevisiaeRsa4 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID25404745
PMCPMC4242840

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.