Evidence map›Paper›PMID 26160102›Full record

ArticleRNA (New York, N.Y.)2015

NSUN6 is a human RNA methyltransferase that catalyzes formation of m5C72 in specific tRNAs.

Sara Haag, Ahmed S Warda, Jens Kretschmer, Manuel A Günnigmann, Claudia Höbartner, Markus T Bohnsack

Abstract read
In one paragraph

Article in RNA (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 129 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
129citing papers in PubMed, 1 pooled it
–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

129 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Interplay of RNA mFASEB bioAdvances · 2026
    Article
  8. mAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  9. Review
  10. mBiology direct · 2026
    Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. NSUN7 is a catalytically inactive RNA mNature communications · 2025
    Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Review

69 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.

Sara HaagCentre for Biochemistry and Molecular Cell Biology, Georg-August-University, 37073 Göttingen, Germany.
Ahmed S WardaCentre for Biochemistry and Molecular Cell Biology, Georg-August-University, 37073 Göttingen, Germany.
Jens KretschmerCentre for Biochemistry and Molecular Cell Biology, Georg-August-University, 37073 Göttingen, Germany.
Manuel A GünnigmannCentre for Biochemistry and Molecular Cell Biology, Georg-August-University, 37073 Göttingen, Germany.
Claudia HöbartnerInstitute for Organic and Biomolecular Chemistry, Georg-August-University, 37077 Göttingen, Germany.
Markus T BohnsackCentre for Biochemistry and Molecular Cell Biology, Georg-August-University, 37073 Göttingen, Germany Göttingen Centre for Molecular Biosciences, Georg-August-University, 37073 Göttingen, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many cellular RNAs require modification of specific residues for their biogenesis, structure, and function. 5-methylcytosine (m(5)C) is a common chemical modification in DNA and RNA but in contrast to the DNA modifying enzymes, only little is known about the methyltransferases that establish m(5)C modifications in RNA. The putative RNA methyltransferase NSUN6 belongs to the family of Nol1/Nop2/SUN domain (NSUN) proteins, but so far its cellular function has remained unknown. To reveal the target spectrum of human NSUN6, we applied UV crosslinking and analysis of cDNA (CRAC) as well as chemical crosslinking with 5-azacytidine. We found that human NSUN6 is associated with tRNAs and acts as a tRNA methyltransferase. Furthermore, we uncovered tRNA(Cys) and tRNA(Thr) as RNA substrates of NSUN6 and identified the cytosine C72 at the 3' end of the tRNA acceptor stem as the target nucleoside. Interestingly, target recognition in vitro depends on the presence of the 3'-CCA tail. Together with the finding that NSUN6 localizes to the cytoplasm and largely colocalizes with marker proteins for the Golgi apparatus and pericentriolar matrix, our data suggest that NSUN6 modifies tRNAs in a late step in their biogenesis.

Indexed as

5-MethylcytosineAzacitidineCross-Linking ReagentsCytoplasmEnzyme InhibitorsGolgi ApparatusHEK293 CellsHeLa CellsHumansIn Vitro TechniquesMethylationRNA, TransfertRNA Methyltransferases5-MethylcytosineAzacitidineCross-Linking ReagentsEnzyme InhibitorsNSUN6 protein, humanRNA, TransfertRNA Methyltransferases5-methylcytosinemethyltransferaseNSUN proteinRNA modificationtRNA

Identifiers

PMID26160102
PMCPMC4536315

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.