Evidence map›Paper›PMID 27551044›Full record

ArticleThe Journal of biological chemistry2016

Pseudouridine in the Anticodon of Escherichia coli tRNATyr(QΨA) Is Catalyzed by the Dual Specificity Enzyme RluF.

Balasubrahmanyam Addepalli, Patrick A Limbach

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.6field-weighted citation impact, top 16% of its field
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

39 citing papers in PubMed, 51 citations in OpenAlex.

  1. Compendium of RNA modifications for bacterial stress adaptation.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  2. Article
  3. Ψ-Atlas: An Integrated Atlas for Pseudouridine Epitranscriptome.Genomics, proteomics & bioinformatics · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Functions and therapeutic applications of pseudouridylation.Nature reviews. Molecular cell biology · 2025
    Review
  11. Article
  12. tRNA pseudouridine synthase D (TruD) fromRNA (New York, N.Y.) · 2025
    Article
  13. Stress-induced modification ofProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Article
  15. Review
  16. RNA modifying enzymes shape tRNA biogenesis and function.The Journal of biological chemistry · 2024
    Review
  17. Article
  18. Complete list of canonical post-transcriptional modifications in thebioRxiv : the preprint server for biology · 2024
    Article
  19. Review
  20. TheRNA (New York, N.Y.) · 2024
    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

2 authors at 1 institution in 1 country.

Balasubrahmanyam AddepalliFrom the Department of Chemistry, Rieveschl Laboratories for Mass Spectrometry, University of Cincinnati, Cincinnati, Ohio 45221 balasual@ucmail.uc.edu.ORCID http://orcid.org/0000-0001-6257-7700
Patrick A LimbachFrom the Department of Chemistry, Rieveschl Laboratories for Mass Spectrometry, University of Cincinnati, Cincinnati, Ohio 45221 Pat.Limbach@uc.edu.ORCID http://orcid.org/0000-0003-1526-4546
University of Cincinnati · US

Funding

LCenter for Clinical and Translational Science and TrainingUL1TR001425 · NCATS · UNIVERSITY OF CINCINNATI · PI HEUBI, JAMES E., KISSELA, BRETT M · 2015 to 2024
$37.5M
UPLC for Enhanced Mass Spectrometry of Modified RNAsR01GM058843 · NIGMS · UNIVERSITY OF CINCINNATI · PI LIMBACH, PATRICK A · 1999 to 2025
$5.1M
NCATS NIH HHS UL1 TR001425NIGMS NIH HHS R01 GM058843
6 · The paper itself

Abstract

Pseudouridine is found in almost all cellular ribonucleic acids (RNAs). Of the multiple characteristics attributed to pseudouridine, making messenger RNAs (mRNAs) highly translatable and non-immunogenic is one such feature that directly implicates this modification in protein synthesis. We report the existence of pseudouridine in the anticodon of Escherichia coli tyrosine transfer RNAs (tRNAs) at position 35. Pseudouridine was verified by multiple detection methods, which include pseudouridine-specific chemical derivatization and gas phase dissociation of RNA during liquid chromatography tandem mass spectrometry (LC-MS/MS). Analysis of total tRNA isolated from E. coli pseudouridine synthase knock-out mutants identified RluF as the enzyme responsible for this modification. Furthermore, the absence of this modification compromises the translational ability of a luciferase reporter gene coding sequence when it is preceded by multiple tyrosine codons. This effect has implications for the translation of mRNAs that are rich in tyrosine codons in bacterial expression systems.

Indexed as

CatalysisEscherichia coliEscherichia coli ProteinsGene Knockdown TechniquesHydro-LyasesPseudouridineRNA, BacterialRNA, Transfer, TyrEscherichia coli ProteinsHydro-LyasesPseudouridinepseudouridylate synthetaseRNA, BacterialRNA, Transfer, Tyracrylonitrilechemical modificationCMCTderivatizationmass spectrometry (MS)pseudouridineRluFRNA modificationtransfer RNA (tRNA)translation

Identifiers

PMID27551044
PMCPMC5064010
OpenAlexW2509921900

What OpenQuestion holds

Textmetadata
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.