Evidence map›Paper›PMID 25653167›Full record

ArticleNucleic acids research2015

Yeast Kre33 and human NAT10 are conserved 18S rRNA cytosine acetyltransferases that modify tRNAs assisted by the adaptor Tan1/THUMPD1.

Sunny Sharma, Jean-Louis Langhendries, Peter Watzinger, Peter Kötter, Karl-Dieter Entian, Denis L J Lafontaine

Abstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 255 papers.

0numbers the graph read from it
0cells of the map it votes in
255citing 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

255 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Beyond mBiomedicines · 2026
    Review
  7. Review
  8. Article
  9. Review
  10. Review
  11. RNA regulation in plants.Science China. Life sciences · 2026
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. NAT10-mediated acCellular & molecular biology letters · 2026
    Article
  17. Article
  18. Article
  19. Article
  20. Review

195 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

6 authors.

Sunny SharmaInstitute of Molecular Biosciences, Goethe University, 60438 Frankfurt am Main, Germany RNA Molecular Biology, F.R.S./FNRS, Université Libre de Bruxelles, B-6041 Charleroi-Gosselies, Belgium.
Jean-Louis LanghendriesRNA Molecular Biology, F.R.S./FNRS, Université Libre de Bruxelles, B-6041 Charleroi-Gosselies, Belgium.
Peter WatzingerInstitute of Molecular Biosciences, Goethe University, 60438 Frankfurt am Main, Germany.
Peter KötterInstitute of Molecular Biosciences, Goethe University, 60438 Frankfurt am Main, Germany.
Karl-Dieter EntianInstitute of Molecular Biosciences, Goethe University, 60438 Frankfurt am Main, Germany.
Denis L J LafontaineRNA Molecular Biology, F.R.S./FNRS, Université Libre de Bruxelles, B-6041 Charleroi-Gosselies, Belgium Center for Microscopy and Molecular Imaging, B-6041 Charleroi-Gosselies, Belgium denis.lafontaine@ulb.ac.be.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The function of RNA is subtly modulated by post-transcriptional modifications. Here, we report an important crosstalk in the covalent modification of two classes of RNAs. We demonstrate that yeast Kre33 and human NAT10 are RNA cytosine acetyltransferases with, surprisingly, specificity toward both 18S rRNA and tRNAs. tRNA acetylation requires the intervention of a specific and conserved adaptor: yeast Tan1/human THUMPD1. In budding and fission yeasts, and in human cells, we found two acetylated cytosines on 18S rRNA, one in helix 34 important for translation accuracy and another in helix 45 near the decoding site. Efficient 18S rRNA acetylation in helix 45 involves, in human cells, the vertebrate-specific box C/D snoRNA U13, which, we suggest, exposes the substrate cytosine to modification through Watson-Crick base pairing with 18S rRNA precursors during small subunit biogenesis. Finally, while Kre33 and NAT10 are essential for pre-rRNA processing reactions leading to 18S rRNA synthesis, we demonstrate that rRNA acetylation is dispensable to yeast cells growth. The inactivation of NAT10 was suggested to suppress nuclear morphological defects observed in laminopathic patient cells through loss of microtubules modification and cytoskeleton reorganization. We rather propose the effects of NAT10 on laminopathic cells are due to reduced ribosome biogenesis or function.

Indexed as

AcetylationAcetyltransferasesAmino Acid SequenceCell LineConserved SequenceCytosineHumansN-Terminal Acetyltransferase EN-Terminal AcetyltransferasesRibosome Subunits, Small, EukaryoticRNA-Binding ProteinsRNA, FungalRNA, PlantRNA, Ribosomal, 18SRNA, Small NucleolarRNA, TransferAcetyltransferasesCytosineNAT10 protein, humanN-Terminal Acetyltransferase EN-Terminal AcetyltransferasesRNA-Binding ProteinsRNA, FungalRNA, PlantRNA, Ribosomal, 18SRNA, Small NucleolarRNA, TransferRRA1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTHUMPD1 protein, human

Identifiers

PMID25653167
PMCPMC4344512

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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.