Evidence map›Paper›PMID 20802492›Full record

ArticleNature chemical biology2010

Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein biogenesis.

Daili J A Netz, Martin Stümpfig, Carole Doré, Ulrich Mühlenhoff, Antonio J Pierik, Roland Lill

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Article in Nature chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

93 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Mitochondria function in cytoplasmic FeS protein biogenesis.Biochimica et biophysica acta. Molecular cell research · 2024
    Review
  8. Requirements for the biogenesis of [2Fe-2S] proteins in the human and yeast cytosol.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. CysB Is a Key Regulator of the Antifungal Activity ofInternational journal of molecular sciences · 2023
    Article
  11. Article
  12. Review
  13. Iron-Sulfur Clusters: A Key Factor of Regulated Cell Death in Cancer.Oxidative medicine and cellular longevity · 2022
    Review
  14. Review
  15. Article
  16. Biogenesis of Iron-Sulfur Clusters and Their Role in DNA Metabolism.Frontiers in cell and developmental biology · 2021
    Review
  17. Review
  18. Article
  19. CIAO3 protein forms a stable ternary complex with two key players of the human cytosolic iron-sulfur cluster assembly machinery.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Article
  20. Article

33 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Daili J A NetzInstitut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Marburg, Germany.
Martin Stümpfig
Carole Doré
Ulrich Mühlenhoff
Antonio J Pierik
Roland Lill

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytosolic and nuclear iron-sulfur (Fe-S) proteins play key roles in processes such as ribosome maturation, transcription and DNA repair-replication. For biosynthesis of their Fe-S clusters, a dedicated cytosolic Fe-S protein assembly (CIA) machinery is required. Here, we identify the essential flavoprotein Tah18 as a previously unrecognized CIA component and show by cell biological, biochemical and spectroscopic approaches that the complex of Tah18 and the CIA protein Dre2 is part of an electron transfer chain functioning in an early step of cytosolic Fe-S protein biogenesis. Electrons are transferred from NADPH via the FAD- and FMN-containing Tah18 to the Fe-S clusters of Dre2. This electron transfer chain is required for assembly of target but not scaffold Fe-S proteins, suggesting a need for reduction in the generation of stably inserted Fe-S clusters. The pathway is conserved in eukaryotes, as human Ndor1-Ciapin1 proteins can functionally replace yeast Tah18-Dre2.

Indexed as

ElectronsCytosolElectron TransportFlavoproteinsHumansIntracellular Signaling Peptides and ProteinsIron-Sulfur ProteinsMitochondrial ProteinsNADPNuclear ProteinsOxidoreductasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSulfurtransferasesTime FactorsCIAPIN1 protein, humanDre2 protein, S cerevisiaeFlavoproteinsIntracellular Signaling Peptides and ProteinsIron-Sulfur ProteinsMitochondrial ProteinsNADPNDOR1 protein, humanNFS1 protein, S cerevisiaeNuclear ProteinsOxidoreductasesSaccharomyces cerevisiae ProteinsSulfurtransferasesTah18 protein, S cerevisiae

Identifiers

PMID20802492

What OpenQuestion holds

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Registered trials

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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.