Evidence map›Paper›PMID 24939895›Full record

ArticleNucleic acids research2014

The flavoprotein Mcap0476 (RlmFO) catalyzes m5U1939 modification in Mycoplasma capricolum 23S rRNA.

Carole Lartigue, Anne Lebaudy, Alain Blanchard, Basma El Yacoubi, Simon Rose, Henri Grosjean, Stephen Douthwaite

Open access · goldAbstract 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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

21 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Temperature-Dependent tRNA Modifications in Bacillales.International journal of molecular sciences · 2024
    Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Naturally occurring modified ribonucleosides.Wiley interdisciplinary reviews. RNA · 2020
    Review
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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

7 authors at 5 institutions in 3 countries.

Carole LartigueINRA, UMR 1332 de Biologie du Fruit et Pathologie, F-33140 Villenave d'Ornon, France Université de Bordeaux, UMR 1332 de Biologie du Fruit et Pathologie, F-33140 Villenave d'Ornon, France.
Anne LebaudyINRA, UMR 1332 de Biologie du Fruit et Pathologie, F-33140 Villenave d'Ornon, France Université de Bordeaux, UMR 1332 de Biologie du Fruit et Pathologie, F-33140 Villenave d'Ornon, France.
Alain BlanchardINRA, UMR 1332 de Biologie du Fruit et Pathologie, F-33140 Villenave d'Ornon, France Université de Bordeaux, UMR 1332 de Biologie du Fruit et Pathologie, F-33140 Villenave d'Ornon, France.
Basma El YacoubiDepartment of Microbiology and Cell Science, University of Florida, FL 32611, USA.
Simon RoseDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense M, Denmark.
Henri GrosjeanCentre de Génétique Moléculaire, UPR3404, CNRS, Associée à l'Université Paris Sud 11, FRC 3115, F-91190 Gif-sur-Yvette, France henri.grosjean@cgm.cnrs-gif.fr.
Stephen DouthwaiteDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense M, Denmark srd@bmb.sdu.dk.
Université de Bordeaux · FRUniversity of Southern Denmark · DKBiologie du Fruit et Pathologie · FRCentre de Génétique Moléculaire · FRUniversity of Florida · US

Funding

Synthesis and function of Queuosine in BacteriaR01GM070641 · NIGMS · UNIVERSITY OF FLORIDA · PI DE CRECY-LAGARD, VALERIE A · 2006 to 2023
$5.3M
NIGMS NIH HHS R01 GM70641
6 · The paper itself

Abstract

Efficient protein synthesis in all organisms requires the post-transcriptional methylation of specific ribosomal ribonucleic acid (rRNA) and transfer RNA (tRNA) nucleotides. The methylation reactions are almost invariably catalyzed by enzymes that use S-adenosylmethionine (AdoMet) as the methyl group donor. One noteworthy exception is seen in some bacteria, where the conserved tRNA methylation at m5U54 is added by the enzyme TrmFO using flavin adenine dinucleotide together with N5,N10-methylenetetrahydrofolate as the one-carbon donor. The minimalist bacterium Mycoplasma capricolum possesses two homologs of trmFO, but surprisingly lacks the m5U54 tRNA modification. We created single and dual deletions of the trmFO homologs using a novel synthetic biology approach. Subsequent analysis of the M. capricolum RNAs by mass spectrometry shows that the TrmFO homolog encoded by Mcap0476 specifically modifies m5U1939 in 23S rRNA, a conserved methylation catalyzed by AdoMet-dependent enzymes in all other characterized bacteria. The Mcap0476 methyltransferase (renamed RlmFO) represents the first folate-dependent flavoprotein seen to modify ribosomal RNA.

Indexed as

Bacterial ProteinsBiocatalysisFlavoproteinsMethylationMethyltransferasesMycoplasma capricolumRNA, Ribosomal, 23SRNA, TransferUridineBacterial ProteinsFlavoproteinsMethyltransferasesRNA, Ribosomal, 23SRNA, TransferUridine

Identifiers

PMID24939895
PMCPMC4081110
OpenAlexW2171488057

What OpenQuestion holds

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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.