Evidence map›Paper›PMID 29263326›Full record

ArticleNature communications2017

Interdependent action of KH domain proteins Krr1 and Dim2 drive the 40S platform assembly.

Miriam Sturm, Jingdong Cheng, Jochen Baßler, Roland Beckmann, Ed Hurt

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

24 citing papers in PubMed, 43 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

5 authors at 2 institutions in 1 country.

Miriam SturmBiochemistry Centre, University of Heidelberg, Heidelberg, 69221, Germany.
Jingdong ChengDepartment of Biochemistry, Gene Center, Center for integrated Protein Science - Munich (CiPS-M), Ludwig-Maximillian University, Munich, 81377, Germany.ORCID http://orcid.org/0000-0003-4442-377X
Jochen BaßlerBiochemistry Centre, University of Heidelberg, Heidelberg, 69221, Germany.ORCID http://orcid.org/0000-0002-7441-7867
Roland BeckmannDepartment of Biochemistry, Gene Center, Center for integrated Protein Science - Munich (CiPS-M), Ludwig-Maximillian University, Munich, 81377, Germany.
Ed HurtBiochemistry Centre, University of Heidelberg, Heidelberg, 69221, Germany. ed.hurt@bzh.uni-heidelberg.de.ORCID http://orcid.org/0000-0002-4535-8255
Heidelberg University · DECenter for Integrated Protein Science Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribosome biogenesis begins in the nucleolus with the formation of 90S pre-ribosomes, from which pre-40S and pre-60S particles arise that subsequently follow separate maturation pathways. Here, we show how structurally related assembly factors, the KH domain proteins Krr1 and Dim2, participate in ribosome assembly. Initially, Dim2 (Pno1) orchestrates an early step in small subunit biogenesis through its binding to a distinct region of the 90S pre-ribosome. This involves Utp1 of the UTP-B module, and Utp14, an activator of the DEAH-box helicase Dhr1 that catalyzes the removal of U3 snoRNP from the 90S. Following this dismantling reaction, the pre-40S subunit emerges, but Dim2 relocates to the pre-40S platform domain, previously occupied in the 90S by the other KH factor Krr1 through its interaction with Rps14 and the UTP-C module. Our findings show how the structurally related Krr1 and Dim2 can control stepwise ribosome assembly during the 90S-to-pre-40S subunit transition.

Indexed as

Organelle BiogenesisCell NucleolusDEAD-box RNA HelicasesEscherichia coliRibonucleoproteins, Small NucleolarRibosomal ProteinsRibosomesRibosome Subunits, Large, EukaryoticRibosome Subunits, Small, EukaryoticRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDEAD-box RNA HelicasesDIM2 protein, S cerevisiaeECM16 protein, S cerevisiaeKRR1 protein, S cerevisiaeRibonucleoproteins, Small Nucleolarribonucleoprotein, U3 small nucleolarRibosomal Proteinsribosomal protein S14RNA-Binding ProteinsSaccharomyces cerevisiae ProteinsUtp14 protein, S cerevisiaeUtp1 protein, S cerevisiae

Identifiers

PMID29263326
PMCPMC5738357
OpenAlexW2772909853

What OpenQuestion holds

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LicenceCC BY
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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.