Evidence map›Paper›PMID 36220828›Full record

ArticleNature communications2022

Sequential action of a tRNA base editor in conversion of cytidine to pseudouridine.

Satoshi Kimura, Veerasak Srisuknimit, Kacie L McCarty, Peter C Dedon, Philip J Kranzusch, Matthew K Waldor

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

11 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. ADATs: roles in tRNA editing and relevance to disease.Acta biochimica et biophysica Sinica · 2024
    Review
  7. Article
  8. Article
  9. Article
  10. A tRNA modification inbioRxiv : the preprint server for biology · 2023
    Article
  11. AlphaFold2 and its applications in the fields of biology and medicine.Signal transduction and targeted therapy · 2023
    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

6 authors at 3 institutions in 2 countries.

Satoshi KimuraDivision of Infectious Diseases, Brigham and Women's Hospital, Boston, MA, USA. s.kimura.res@gmail.com.ORCID 0000-0003-3555-5877
Veerasak SrisuknimitDivision of Infectious Diseases, Brigham and Women's Hospital, Boston, MA, USA.
Kacie L McCartyDepartment of Microbiology, Harvard Medical School, Boston, MA, USA.
Peter C DedonDepartment of Biological Engineering, Massachusetts Institution of Technology, Cambridge, MA, USA.ORCID 0000-0003-0011-3067
Philip J KranzuschDepartment of Microbiology, Harvard Medical School, Boston, MA, USA.ORCID 0000-0002-4943-733X
Matthew K WaldorDivision of Infectious Diseases, Brigham and Women's Hospital, Boston, MA, USA. mwaldor@research.bwh.harvard.edu.ORCID 0000-0003-1843-7000
Brigham and Women's Hospital · USHarvard University · USSingapore-MIT Alliance for Research and Technology · SG

Funding

Vibrio cholerae intestinal colonization and vaccine developmentR01AI042347 · NIAID · TUFTS UNIVERSITY BOSTON · PI WALDOR, MATTHEW K · 1998 to 2025
$7.3M
Molecular Biology and Virulence of CTX PhageR37AI042347 · NIAID · BRIGHAM AND WOMEN'S HOSPITAL · PI WALDOR, MATTHEW K · 2008 to 2017
$3.8M
Howard Hughes Medical InstituteNIAID NIH HHS R01 AI042347NIAID NIH HHS R37 AI042347
6 · The paper itself

Abstract

Post-transcriptional RNA editing modulates gene expression in a condition-dependent fashion. We recently discovered C-to-Ψ editing in Vibrio cholerae tRNA. Here, we characterize the biogenesis, regulation, and functions of this previously undescribed RNA editing process. We show that an enzyme, TrcP, mediates the editing of C-to-U followed by the conversion of U to Ψ, consecutively. AlphaFold-2 predicts that TrcP consists of two globular domains (cytidine deaminase and pseudouridylase) and a long helical domain. The latter domain tethers tRNA substrates during both the C-to-U editing and pseudouridylation, likely enabling a substrate channeling mechanism for efficient catalysis all the way to the terminal product. C-to-Ψ editing both requires and suppresses other modifications, creating an interdependent network of modifications in the tRNA anticodon loop that facilitates coupling of tRNA modification states to iron availability. Our findings provide mechanistic insights into an RNA editing process that likely promotes environmental adaptation.

Indexed as

AnticodonPseudouridineCytidineCytidine DeaminaseIronRNA, TransferAnticodonCytidineCytidine DeaminaseIronPseudouridineRNA, Transfer

Identifiers

PMID36220828
PMCPMC9553926
OpenAlexW4304191875

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.