Evidence map›Paper›PMID 20972225›Full record

ArticleNucleic acids research2011

The Bowen-Conradi syndrome protein Nep1 (Emg1) has a dual role in eukaryotic ribosome biogenesis, as an essential assembly factor and in the methylation of Ψ1191 in yeast 18S rRNA.

Britta Meyer, Jan Philip Wurm, Peter Kötter, Matthias S Leisegang, Valeska Schilling, Markus Buchhaupt, Martin Held, Ute Bahr, Michael Karas, Alexander Heckel and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
2.7field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

92 citing papers in PubMed, 124 citations in OpenAlex.

  1. Review
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  7. Review
  8. Mechanisms of ribosomopathy and phase separation-related ribosomopathy.Journal of Zhejiang University. Science. B · 2025
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  9. Specialized ribosomes: integrating new insights and current challenges.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
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  13. Pseudouridine andRSC chemical biology · 2024
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  19. Natural product reports · 2023
    Review
  20. Article

32 more citing papers are in PubMed but not listed here.

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

13 authors at 3 institutions in 3 countries.

Britta MeyerCluster of Excellence Frankfurt: Macromolecular Complexes, Max-von-Laue Str. 9, D-60438 Frankfurt/M., Germany.
Jan Philip Wurm
Peter Kötter
Matthias S Leisegang
Valeska Schilling
Markus Buchhaupt
Martin Held
Ute Bahr
Michael Karas
Alexander Heckel
Markus T Bohnsack
Jens Wöhnert
Karl-Dieter Entian
Goethe University Frankfurt · DEInstitute of Macromolecular Chemistry · UAMRB Research Center for Magnetic Resonance Bavaria · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Nep1 (Emg1) SPOUT-class methyltransferase is an essential ribosome assembly factor and the human Bowen-Conradi syndrome (BCS) is caused by a specific Nep1(D86G) mutation. We recently showed in vitro that Methanocaldococcus jannaschii Nep1 is a sequence-specific pseudouridine-N1-methyltransferase. Here, we show that in yeast the in vivo target site for Nep1-catalyzed methylation is located within loop 35 of the 18S rRNA that contains the unique hypermodification of U1191 to 1-methyl-3-(3-amino-3-carboxypropyl)-pseudouri-dine (m1acp3Ψ). Specific (14)C-methionine labelling of 18S rRNA in yeast mutants showed that Nep1 is not required for acp-modification but suggested a function in Ψ1191 methylation. ESI MS analysis of acp-modified Ψ-nucleosides in a Δnep1-mutant showed that Nep1 catalyzes the Ψ1191 methylation in vivo. Remarkably, the restored growth of a nep1-1(ts) mutant upon addition of S-adenosylmethionine was even observed after preventing U1191 methylation in a Δsnr35 mutant. This strongly suggests a dual Nep1 function, as Ψ1191-methyltransferase and ribosome assembly factor. Interestingly, the Nep1 methyltransferase activity is not affected upon introduction of the BCS mutation. Instead, the mutated protein shows enhanced dimerization propensity and increased affinity for its RNA-target in vitro. Furthermore, the BCS mutation prevents nucleolar accumulation of Nep1, which could be the reason for reduced growth in yeast and the Bowen-Conradi syndrome.

Indexed as

Base SequenceCell NucleolusDimerizationFetal Growth RetardationHumansMethanococcalesMethylationMethyltransferasesMolecular Sequence DataNuclear ProteinsPoint MutationPseudouridinePsychomotor DisordersRibosomal ProteinsRibosomesRNA, Ribosomal, 18SEMG1 protein, humanEMG1 protein, S cerevisiaeMethyltransferasesNuclear ProteinsPseudouridineRibosomal ProteinsRNA, Ribosomal, 18SSaccharomyces cerevisiae ProteinsS-Adenosylmethionine

Identifiers

PMID20972225
PMCPMC3045603
OpenAlexW2125047925

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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.