Evidence map›Paper›PMID 24914049›Full record

ArticleNucleic acids research2014

TtcA a new tRNA-thioltransferase with an Fe-S cluster.

Denis Bouvier, Natty Labessan, Martin Clémancey, Jean-Marc Latour, Jean-Luc Ravanat, Marc Fontecave, Mohamed Atta

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 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. 2-Thiouridine formation inJournal of bacteriology · 2025
    Review
  8. Article
  9. Structure-based insights into the mechanism of [4Fe-4S]-dependent sulfur insertase LarE.Protein science : a publication of the Protein Society · 2024
    Article
  10. Article
  11. At the Crossroad of Nucleotide Dynamics and Protein Synthesis in Bacteria.Microbiology and molecular biology reviews : MMBR · 2023
    Review
  12. Article
  13. Article
  14. Article
  15. Biosynthesis and Degradation of Sulfur Modifications in tRNAs.International journal of molecular sciences · 2021
    Review
  16. Review
  17. Article
  18. tRNA Modifications as a Readout of S and Fe-S Metabolism.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  19. Article
  20. Metal utilization in genome-reduced bacteria: Do human mycoplasmas rely on iron?Computational and structural biotechnology journal · 2021
    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

7 authors.

Denis BouvierUniversity of Grenoble Alpes, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CNRS, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CEA, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France.
Natty LabessanUniversity of Grenoble Alpes, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CNRS, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CEA, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France.
Martin ClémanceyUniversity of Grenoble Alpes, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CNRS, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CEA, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France.
Jean-Marc LatourUniversity of Grenoble Alpes, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CNRS, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CEA, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France.
Jean-Luc RavanatUniversity of Grenoble Alpes, INAC, SCIB, F-38000 Grenoble, France CEA, iNAC, SCIB, F-38054 Grenoble, France.
Marc FontecaveUniversity of Grenoble Alpes, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CNRS, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CEA, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France Laboratoire de Chimie des Processus Biologiques, UMR 8229 Collège de France/CNRS/UPMC, 11 place Marcellin-Berthelot, Paris, France.
Mohamed AttaUniversity of Grenoble Alpes, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CNRS, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CEA, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France mohamed.atta@cea.fr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TtcA catalyzes the post-transcriptional thiolation of cytosine 32 in some tRNAs. The enzyme from Escherichia coli was homologously overexpressed in E. coli. The purified enzyme is a dimer containing an iron-sulfur cluster and displays activity in in vitro assays. The type and properties of the cluster were investigated using a combination of UV-visible absorption, EPR and Mössbauer spectroscopy, as well as by site-directed mutagenesis. These studies demonstrated that the TtcA enzyme contains a redox-active and oxygen-sensitive [4Fe-4S] cluster, chelated by only three cysteine residues and absolutely essential for activity. TtcA is unique tRNA-thiolating enzyme using an iron-sulfur cluster for catalyzing a non-redox reaction.

Indexed as

Cloning, MolecularCysteineEscherichia coliEscherichia coli ProteinsGene ExpressionGlutaredoxinsIron-Sulfur ProteinsSulfurtransferasesCysteineEscherichia coli ProteinsGlutaredoxinsIron-Sulfur ProteinsSulfurtransferasesTtcA protein, E coli

Identifiers

PMID24914049
PMCPMC4081106

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.