Evidence map›Paper›PMID 24214967›Full record

ArticleNucleic acids research2014

The mechanism of pseudouridine synthases from a covalent complex with RNA, and alternate specificity for U2605 versus U2604 between close homologs.

Nadine Czudnochowski, Gary W Ashley, Daniel V Santi, Akram Alian, Janet Finer-Moore, Robert M Stroud

Abstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Compendium of RNA modifications for bacterial stress adaptation.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  2. Major bioactive metabolites derived fromFrontiers in pharmacology · 2026
    Review
  3. Review
  4. Article
  5. tRNA pseudouridine synthase D (TruD) fromRNA (New York, N.Y.) · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. The Pseudouridine Synthases Proceed through a Glycal Intermediate.Journal of the American Chemical Society · 2016
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. 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.

Nadine CzudnochowskiDepartment of Biochemistry and Biophysics, University of California, San Francisco, 600 16th Street, San Francisco, CA 94158, USA, ProLynx, 455 Mission Bay Blvd., Suite 145, San Francisco, CA 94158, USA and Faculty of Biology, Technion-Israel Institute of Technology, Technion City, Haifa 320003, Israel.
Gary W Ashley
Daniel V Santi
Akram Alian
Janet Finer-Moore
Robert M Stroud

Funding

TRNA METHYLASE AND TRNA PSEUDOURIDINE SYNTHASER01GM051232 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 1996 to 2012
$3.4M
NIGMS NIH HHS GM51232
6 · The paper itself

Abstract

RluB catalyses the modification of U2605 to pseudouridine (Ψ) in a stem-loop at the peptidyl transferase center of Escherichia coli 23S rRNA. The homolog RluF is specific to the adjacent nucleotide in the stem, U2604. The 1.3 Å resolution crystal structure of the complex between the catalytic domain of RluB and the isolated substrate stem-loop, in which the target uridine is substituted by 5-fluorouridine (5-FU), reveals a covalent bond between the isomerized target base and tyrosine 140. The structure is compared with the catalytic domain alone determined at 2.5 Å resolution. The RluB-bound stem-loop has essentially the same secondary structure as in the ribosome, with a bulge at A2602, but with 5-FU2605 flipped into the active site. We showed earlier that RluF induced a frame-shift of the RNA, moving A2602 into the stem and translating its target, U2604, into the active site. A hydrogen-bonding network stabilizes the bulge in the RluB-RNA but is not conserved in RluF and so RluF cannot stabilize the bulge. On the basis of the covalent bond between enzyme and isomerized 5-FU we propose a Michael addition mechanism for pseudouridine formation that is consistent with all experimental data.

Indexed as

ApoenzymesArginineCatalytic DomainEscherichia coli ProteinsIntramolecular TransferasesModels, MolecularNucleic Acid ConformationProtein ConformationRNA, Ribosomal, 23SSubstrate SpecificityTyrosineUridineWater5-fluorouridineApoenzymesArginineEscherichia coli ProteinsIntramolecular Transferasespseudouridine synthasesRNA, Ribosomal, 23STyrosineUridineWater

Identifiers

PMID24214967
PMCPMC3919597

What OpenQuestion holds

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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.