Evidence map›Paper›PMID 40399280›Full record

ArticleNature communications2025

H/ACA snR30 snoRNP guides independent 18S rRNA subdomain formation.

Paulina Fischer, Matthias Thoms, Benjamin Lau, Timo Denk, Maria Kuvshinova, Otto Berninghausen, Dirk Flemming, Ed Hurt, Roland Beckmann

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Interprotomer communication and functional asymmetry in H/ACA snoRNPs.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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

9 authors.

Paulina Fischer *Biochemistry Center, Heidelberg University, Heidelberg, Germany.
Matthias Thoms *Department of Biochemistry, Gene Center, University of Munich, Munich, Germany.
Benjamin LauBiochemistry Center, Heidelberg University, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-7615-1046
Timo DenkDepartment of Biochemistry, Gene Center, University of Munich, Munich, Germany.ORCID http://orcid.org/0000-0002-0761-3294
Maria KuvshinovaBiochemistry Center, Heidelberg University, Heidelberg, Germany.
Otto BerninghausenDepartment of Biochemistry, Gene Center, University of Munich, Munich, Germany.ORCID http://orcid.org/0000-0002-9255-0522
Dirk FlemmingBiochemistry Center, Heidelberg University, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-1528-5032
Ed HurtBiochemistry Center, Heidelberg University, Heidelberg, Germany. ed.hurt@bzh.uni-heidelberg.de.ORCID http://orcid.org/0000-0002-4535-8255
Roland BeckmannDepartment of Biochemistry, Gene Center, University of Munich, Munich, Germany. beckmann@genzentrum.lmu.de.ORCID http://orcid.org/0000-0003-4291-3898

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) HU363/12-1EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) ADG 741781EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) ADG 885711
6 · The paper itself

Abstract

Ribosome biogenesis follows a cascade of pre-rRNA folding and processing steps, coordinated with ribosomal protein incorporation. Nucleolar 90S pre-ribosomes are well-described stable intermediates, composed of pre-18S rRNA, ribosomal S-proteins, U3 snoRNA, and ~70 assembly factors. However, how numerous snoRNAs control pre-rRNA modification and folding during early maturation events remains unclear. We identify snR30 (human U17), the only essential H/ACA snoRNA in yeast, which binds with Cbf5-Gar1-Nop10-Nhp2 to a pre-18S rRNA subdomain containing platform helices and ES6 of the 40S central domain. Integration into the 90S is blocked by RNA hybridization with snR30. The snoRNP complex coordinates the recruitment of early assembly factors Krr1-Utp23-Kri1 and ribosomal proteins uS11-uS15, enabling isolated subdomain assembly. Krr1-dependent release of snR30 culminates in integration of the platform into the 90S. Our study reveals the essential role of snR30 in chaperoning central domain formation as a discrete assembly unit externalized from the pre-ribosomal core.

Indexed as

Ribonucleoproteins, Small NucleolarRNA, Ribosomal, 18SRNA, Small NucleolarSaccharomyces cerevisiaeHumansProtein BindingRibosomal ProteinsRibosomesRNA PrecursorsSaccharomyces cerevisiae ProteinsRibonucleoproteins, Small NucleolarRibosomal ProteinsRNA PrecursorsRNA, Ribosomal, 18SRNA, Small NucleolarSaccharomyces cerevisiae Proteins

Identifiers

PMID40399280
PMCPMC12095548

What OpenQuestion holds

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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.