Evidence map›Paper›PMID 23615440›Full record

ArticleMolecular biology of the cell2013

The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation.

Marta A Uzarska, Rafal Dutkiewicz, Sven-Andreas Freibert, Roland Lill, Ulrich Mühlenhoff

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing 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

64 citing papers in PubMed.

  1. Article
  2. Article
  3. Mitochondria function in cytoplasmic FeS protein biogenesis.Biochimica et biophysica acta. Molecular cell research · 2024
    Review
  4. 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
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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. [4Fe-4S] cluster trafficking mediated byThe Journal of biological chemistry · 2020
    Article
  19. Article
  20. Article

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

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

5 authors.

Marta A UzarskaInstitut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, 35032 Marburg, Germany.
Rafal Dutkiewicz
Sven-Andreas Freibert
Roland Lill
Ulrich Mühlenhoff

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mitochondrial Hsp70 chaperone Ssq1 plays a dedicated role in the maturation of iron-sulfur (Fe/S) proteins, an essential process of mitochondria. Similar to its bacterial orthologue HscA, Ssq1 binds to the scaffold protein Isu1, thereby facilitating dissociation of the newly synthesized Fe/S cluster on Isu1 and its transfer to target apoproteins. Here we use in vivo and in vitro approaches to show that Ssq1 also interacts with the monothiol glutaredoxin 5 (Grx5) at a binding site different from that of Isu1. Grx5 binding does not stimulate the ATPase activity of Ssq1 and is most pronounced for the ADP-bound form of Ssq1, which interacts with Isu1 most tightly. The vicinity of Isu1 and Grx5 on the Hsp70 chaperone facilitates rapid Fe/S cluster transfer from Isu1 to Grx5. Grx5 and its bound Fe/S cluster are required for maturation of all cellular Fe/S proteins, regardless of the type of bound Fe/S cofactor and subcellular localization. Hence Grx5 functions as a late-acting component of the core Fe/S cluster (ISC) assembly machinery linking the Fe/S cluster synthesis reaction on Isu1 with late assembly steps involving Fe/S cluster targeting to dedicated apoproteins.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateBinding SitesCytosolElectrophoresis, Polyacrylamide GelGlutaredoxinsHSP70 Heat-Shock ProteinsImmunoprecipitationIron-Sulfur ProteinsMitochondriaMitochondrial ProteinsMolecular ChaperonesMutationProtein BindingSaccharomyces cerevisiae ProteinsAdenosine DiphosphateAdenosine TriphosphateGlutaredoxinsGrx5 protein, S cerevisiaeHSP70 Heat-Shock ProteinsIron-Sulfur ProteinsISU1 protein, S cerevisiaeJAC1 protein, S cerevisiaeMitochondrial ProteinsMolecular ChaperonesSaccharomyces cerevisiae ProteinsSSQ1 protein, S cerevisiae

Identifiers

PMID23615440
PMCPMC3681689

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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.