Evidence map›Paper›PMID 39747487›Full record

ArticleNature structural & molecular biology2025

Molecular basis of human nuclear and mitochondrial tRNA 3' processing.

Arjun Bhatta, Bernhard Kuhle, Ryan D Yu, Lucas Spanaus, Katja Ditter, Katherine E Bohnsack, Hauke S Hillen

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Review
  5. The regulation, function and disease relevance of cytoplasmic tRNAs.Nature reviews. Molecular cell biology · 2026
    Review
  6. Article
  7. Review
  8. Review
  9. Ribonuclease RNase Z is an evolutionarily conserved deAMPylase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

7 authors.

Arjun Bhatta *Department of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.
Bernhard Kuhle *Department of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.
Ryan D Yu *Department of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.
Lucas SpanausDepartment of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.
Katja DitterDepartment of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.
Katherine E BohnsackDepartment of Molecular Biology, University Medical Center Göttingen, Göttingen, Germany.ORCID http://orcid.org/0000-0001-6035-4255
Hauke S HillenDepartment of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany. hauke.hillen@med.uni-goettingen.de.ORCID http://orcid.org/0000-0002-1206-0129

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic transfer RNA (tRNA) precursors undergo sequential processing steps to become mature tRNAs. In humans, ELAC2 carries out 3' end processing of both nucleus-encoded (nu-tRNAs) and mitochondria-encoded (mt-tRNAs) tRNAs. ELAC2 is self-sufficient for processing of nu-tRNAs but requires TRMT10C and SDR5C1 to process most mt-tRNAs. Here we show that TRMT10C and SDR5C1 specifically facilitate processing of structurally degenerate mt-tRNAs lacking the canonical elbow. Structures of ELAC2 in complex with TRMT10C, SDR5C1 and two divergent mt-tRNA substrates reveal two distinct mechanisms of pre-tRNA recognition. While canonical nu-tRNAs and mt-tRNAs are recognized by direct ELAC2-RNA interactions, processing of noncanonical mt-tRNAs depends on protein-protein interactions between ELAC2 and TRMT10C. These results provide the molecular basis for tRNA 3' processing in both the nucleus and the mitochondria and explain the organelle-specific requirement for additional factors. Moreover, they suggest that TRMT10C-SDR5C1 evolved as a mitochondrial tRNA maturation platform to compensate for the structural erosion of mt-tRNAs in bilaterian animals.

Indexed as

Cell NucleusMitochondriaRNA Processing, Post-TranscriptionalRNA, TransferHumansMethyltransferasesModels, MolecularNeoplasm ProteinsNucleic Acid ConformationRNA, MitochondrialtRNA MethyltransferasesELAC2 protein, humanMethyltransferasesNeoplasm ProteinsRNA, MitochondrialRNA, TransferTRMT10c protein, humantRNA Methyltransferases

Identifiers

PMID39747487
PMCPMC11996679

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.