Evidence map›Paper›PMID 41603732›Full record

ArticleNucleic acids research2026

Sni445 recruits box C/D snoRNPs snR4 and snR45 to guide ribosomal RNA acetylation by Kre33.

Jutta Hafner, Ingrid Zierler, Hussein Hamze, Sébastien Favre, Matthias Thoms, Natalia Kunowska, Sarah Rimser, Benjamin Albert, Tomas Caetano, Marion Aguirrebengoa and 5 more

Abstract read
In one paragraph

Article in Nucleic acids research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

15 authors.

Jutta HafnerInstitute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.ORCID 0009-0003-2179-1702
Ingrid ZierlerInstitute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.
Hussein HamzeUniversité de Toulouse, CNRS, UPS, 31062 Toulouse, France.
Sébastien FavreDepartment of Biology, University of Fribourg, 1700Fribourg, Switzerland.
Matthias ThomsGene Center, University of Munich, D-81377Munich, Germany.
Natalia KunowskaInstitute of Pharmaceutical Sciences, Pharmaceutical Chemistry, University of Graz, 8010 Graz, Austria.
Sarah RimserInstitute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.
Benjamin AlbertUniversité de Toulouse, CNRS, UPS, 31062 Toulouse, France.ORCID 0000-0003-2122-6458
Tomas CaetanoUniversité de Toulouse, 31062 Toulouse, France.
Marion AguirrebengoaUniversité de Toulouse, 31062 Toulouse, France.
Roland BeckmannGene Center, University of Munich, D-81377Munich, Germany.ORCID 0000-0003-4291-3898
Ulrich StelzlBioTechMed-Graz, 8010 Graz, Austria.ORCID 0000-0003-2500-3585
Dieter KresslerDepartment of Biology, University of Fribourg, 1700Fribourg, Switzerland.ORCID 0000-0003-4855-3563
Anthony K HenrasUniversité de Toulouse, CNRS, UPS, 31062 Toulouse, France.
Brigitte PertschyInstitute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.ORCID 0000-0003-3558-0191

Funding

ANR RASTRANR REA1COMANR RIBOPRE60SAustrian Science FundCity of GrazERC ADG 885711Field of Excellence BioHealth-University of GrazFrench Ministry of Higher Education and ResearchLigue Nationale Contre le CancerProvince of StyriaSwiss National Science Foundation 310 030_204 801
6 · The paper itself

Abstract

Eukaryotic ribosome synthesis is a highly complex, multistep process that is best characterized in the yeast Saccharomyces cerevisiae. It is orchestrated by >200 ribosome assembly factors and 75 small nucleolar ribonucleoproteins (snoRNPs), which guide site-specific chemical modifications of precursor rRNA (pre-rRNA). While canonical box C/D snoRNPs guide 2'-O-methylation, the atypical box C/D snoRNPs snR4 and snR45 guide acetylation of 18S rRNA residues C1280 and C1773, respectively, catalyzed by the acetyltransferase Kre33. Here, we identify and characterize Ynl050c/Sni445 as a novel ribosome assembly factor and previously unrecognized auxiliary component of the snR4 and snR45 box C/D snoRNPs. Sni445 associates with snR4 and snR45 in their free form and is required for their stable incorporation into 90S pre-ribosomes. Genetic interactions link Sni445 and the snR4 and snR45 snoRNAs to ribosomal proteins Rps20 (uS10) and Rps14 (uS11), which are positioned near the respective acetylation sites in the 40S subunit. Moreover, Sni445 physically interacts with Kre33 within the 90S pre-ribosome, and its absence abolishes acetylation of C1280 and C1773. Our findings suggest that Sni445 facilitates the recruitment of snR4 and snR45 snoRNPs to 90S particles and might promote their interaction with Kre33, thereby enabling the site-specific acetylation of 18S rRNA by Kre33.

Indexed as

AcetyltransferasesRibonucleoproteins, Small NucleolarRNA, RibosomalSaccharomyces cerevisiae ProteinsAcetylationRibosomesRNA, Ribosomal, 18SSaccharomyces cerevisiaeAcetyltransferasesRibonucleoproteins, Small NucleolarRNA, RibosomalRNA, Ribosomal, 18SSaccharomyces cerevisiae Proteins

Identifiers

PMID41603732
PMCPMC12848939

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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.