Evidence map›Paper›PMID 41997936›Full record

ArticleNature communications2026

Cytoplasmic localization of pseudouridine synthase 7 facilitates a pseudouridine-dependent enhancement of cellular stress tolerance.

Minli Ruan, Sean M Engels, Matthew R Burroughs, Xiaoyan Li, Rosella Stower, Talia Tzadikario, Connor Powell, Dylan Bloch, Oleksandra Fanari, Stuart Akeson and 6 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. The impact of psuedouridine modification on human tRNA.Biochemical Society transactions · 2026
    Review
  3. Integrating mass spectrometry with Nanopore direct RNA sequencing forbioRxiv : the preprint server for biology · 2026
    Article
  4. Pseudouridylation landscape across 42bioRxiv : the preprint server for biology · 2026
    Article
  5. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

16 authors.

Minli RuanDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI, USA.
Sean M EngelsMcKetta Department of Chemical Engineering, University of Texas, Austin, TX, USA.ORCID http://orcid.org/0000-0002-4866-6050
Matthew R BurroughsMcKetta Department of Chemical Engineering, University of Texas, Austin, TX, USA.ORCID http://orcid.org/0009-0007-1611-647X
Xiaoyan LiDepartment of Chemistry, University of Michigan, Ann Arbor, MI, USA.
Rosella StowerDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI, USA.
Talia TzadikarioDepartment of Bioengineering, Northeastern University, Boston, MA, USA.
Connor PowellDepartment of Bioengineering, Northeastern University, Boston, MA, USA.ORCID http://orcid.org/0009-0006-6889-0099
Dylan BlochDepartment of Bioengineering, Northeastern University, Boston, MA, USA.ORCID http://orcid.org/0000-0002-5382-5765
Oleksandra FanariDepartment of Bioengineering, Northeastern University, Boston, MA, USA.ORCID http://orcid.org/0009-0003-2915-859X
Stuart AkesonDepartment of Bioengineering, Northeastern University, Boston, MA, USA.ORCID http://orcid.org/0009-0008-8008-2486
Daniel E EylerDepartment of Chemistry, University of Michigan, Ann Arbor, MI, USA.ORCID http://orcid.org/0000-0002-6425-9770
Chase A WeidmannDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI, USA.ORCID http://orcid.org/0000-0002-2941-0500
Sara RouhanifardDepartment of Bioengineering, Northeastern University, Boston, MA, USA.ORCID http://orcid.org/0000-0002-6991-4877
Miten JainDepartment of Bioengineering, Northeastern University, Boston, MA, USA.ORCID http://orcid.org/0000-0002-4571-3982
Lydia M ContrerasMcKetta Department of Chemical Engineering, University of Texas, Austin, TX, USA.
Kristin S KoutmouDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI, USA. kkoutmou@umich.edu.ORCID http://orcid.org/0000-0002-7763-9262

Funding

Mechanisms of translational controlR35GM128836 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Kristin S Koutmou · 2018 to 2026
$3.2M
MFB: Integrating LC-MS/MS and Nanopore Sequencing Platforms to Enable the Direct and Quantatative Detection of RNA ModificationsR01HG013876 · NHGRI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Kristin S Koutmou · 2024 to 2026
$1.2M
American Heart Association (American Heart Association, Inc.) 24PRE1194152Foundation for the National Institutes of Health (Foundation for the National Institutes of Health, Inc.) K22CA26234Foundation for the National Institutes of Health (Foundation for the National Institutes of Health, Inc.) R01HG012856Foundation for the National Institutes of Health (Foundation for the National Institutes of Health, Inc.) R21ES032124National Science Foundation (NSF) DGE 2137420National Science Foundation (NSF) NSF CAREER 2045562NHGRI NIH HHS R01 HG013876NIGMS NIH HHS R35 GM128836U.S. Department of Health & Human Services | National Institutes of Health (NIH) 2R35 GM128836
6 · The paper itself

Abstract

Pseudouridine (Ψ) is an abundant post-transcriptional modification found across all classes of RNA. It is widely speculated that Ψ inclusion in messenger RNAs (mRNAs) might provide an avenue for cells to control gene expression post-transcriptionally. Here we demonstrate that one of the principal mRNA pseudouridylating enzymes, pseudouridine synthase 7 (PUS7), exhibits a stress-induced accumulation in the cytoplasm of yeast and human epithelial lung cells. Stress-induced and cytoplasmic localization of PUS7 promotes Ψ-incorporation into hundreds of mRNA targets. In contrast, the modification status of tRNA sites targeted by PUS7 (Ψ13 and Ψ35) is unperturbed. Furthermore, engineered PUS7 cytoplasmic localization increases cellular fitness under reactive oxygen species (ROS) and divalent metal ion stress. Quantitative proteomics reveal a reshaping of the proteome upon PUS7 relocalization under stress. Collectively, our data demonstrate that PUS7 localization alters mRNA pseudouridylation patterns, reshapes the proteome, and influences cellular fitness.

Indexed as

CytoplasmHydro-LyasesIntramolecular TransferasesPseudouridineSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStress, PhysiologicalHumansReactive Oxygen SpeciesRNA, MessengerRNA, TransferHydro-LyasesIntramolecular TransferasesPseudouridinepseudouridine synthasesPUS7 protein, humanPus7 protein, S cerevisiaeReactive Oxygen SpeciesRNA, MessengerRNA, TransferSaccharomyces cerevisiae Proteins

Identifiers

PMID41997936
PMCPMC13276364

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.