Evidence map›Paper›PMID 41136621›Full record

ArticleNature cell biology2025

A comprehensive tRNA pseudouridine map uncovers targets dependent on human stand-alone pseudouridine synthases.

Haiqi Xu, Linzhen Kong, Mengjie Li, Giuseppina Pisignano, Jingfei Cheng, Feng Feng, Parinaz Mehdipour, Chun-Xiao Song

Abstract read
In one paragraph

Article in Nature cell biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. The impact of psuedouridine modification on human tRNA.Biochemical Society transactions · 2026
    Review
  3. Article
  4. Article
  5. Pseudouridylation landscape across 42bioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Article
  8. Review
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

8 authors.

Haiqi Xu *Ludwig Institute for Cancer Research, Nuffield Department of Medicine, University of Oxford, Oxford, UK.ORCID http://orcid.org/0009-0006-4486-5075
Linzhen Kong *Ludwig Institute for Cancer Research, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Mengjie Li *Ludwig Institute for Cancer Research, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Giuseppina Pisignano *Ludwig Institute for Cancer Research, Nuffield Department of Medicine, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-7476-3447
Jingfei ChengLudwig Institute for Cancer Research, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Feng FengLudwig Institute for Cancer Research, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Parinaz MehdipourLudwig Institute for Cancer Research, Nuffield Department of Medicine, University of Oxford, Oxford, UK. parinaz.mehdipour@ludwig.ox.ac.uk.ORCID http://orcid.org/0000-0002-4476-9925
Chun-Xiao SongLudwig Institute for Cancer Research, Nuffield Department of Medicine, University of Oxford, Oxford, UK. chunxiao.song@ludwig.ox.ac.uk.ORCID http://orcid.org/0000-0002-7781-6521

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pseudouridine (Ψ) is one of the most abundant RNA modifications in human cells, introduced post-transcriptionally by pseudouridine synthases (PUS). Despite its prevalence, the biological functions of Ψ remain poorly understood, largely due to the limited knowledge linking specific PUS enzymes to their targets. Here, to address this gap, we systematically knocked out or knocked down nine stand-alone PUS in HCT116 cells and mapped their Ψ profiles using 2-bromoacrylamide-assisted cyclization sequencing. Through this approach, we uncovered previously unknown targets of several PUS enzymes, including RPUSD1, RPUSD2, PUS3, PUSL1 and PUS7L. In addition, we revealed that TRUB1 and PUS10 function redundantly to catalyse the highly conserved Ψ55 modification in cytosolic tRNAs. Intriguingly, we found that RPUSD3 and TRUB2 do not exhibit noticeable enzymatic activities in human cells. By integrating these findings with earlier results for TRUB1, PUS7 and PUS1, we constructed a comprehensive map of stand-alone PUS-dependent Ψ modifications across human tRNAs. Using this map, we further demonstrated that different PUS enzymes introduce Ψ modifications at distinct stages of pre-tRNA processing.

Indexed as

Hydro-LyasesIntramolecular TransferasesPseudouridineRNA Processing, Post-TranscriptionalRNA, TransferHCT116 CellsHumansHydro-LyasesIntramolecular TransferasesPseudouridinepseudouridine synthasespseudouridylate synthetaseRNA, Transfer

Identifiers

PMID41136621
PMCPMC12716993

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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.