Evidence map›Paper›PMID 21987576›Full record

ArticleThe Journal of biological chemistry2011

Specialized function of yeast Isa1 and Isa2 proteins in the maturation of mitochondrial [4Fe-4S] proteins.

Ulrich Mühlenhoff, Nadine Richter, Ophry Pines, Antonio J Pierik, Roland Lill

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

82 citing papers in PubMed, 171 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Isa2p is essential inJournal of biosciences · 2025
    Article
  6. Article
  7. Review
  8. Article
  9. Recent progress of methods for cuproptosis detection.Frontiers in molecular biosciences · 2024
    Review
  10. Essentiality of theInternational journal of molecular sciences · 2023
    Article
  11. Article
  12. Article
  13. Assembly of the Multi-Subunit CytochromeInternational journal of molecular sciences · 2022
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Biogenesis of Iron-Sulfur Clusters and Their Role in DNA Metabolism.Frontiers in cell and developmental biology · 2021
    Review
  19. [4Fe-4S] cluster trafficking mediated byThe Journal of biological chemistry · 2020
    Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Ulrich MühlenhoffInstitut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch Strasse 6, 35032 Marburg, Germany.
Nadine RichterInstitut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch Strasse 6, 35032 Marburg, Germany.
Ophry PinesDepartment of Microbiology and Molecular Genetics, IMRIC, Faculty of Medicine, Hebrew University, Jerusalem 91120, Israel.
Antonio J PierikInstitut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch Strasse 6, 35032 Marburg, Germany.
Roland LillInstitut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch Strasse 6, 35032 Marburg, Germany. Electronic address: Lill@staff.uni-marburg.de.
Philipps University of Marburg · DEHebrew University of Jerusalem · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Most eukaryotes contain iron-sulfur cluster (ISC) assembly proteins related to Saccharomyces cerevisiae Isa1 and Isa2. We show here that Isa1 but not Isa2 can be functionally replaced by the bacterial relatives IscA, SufA, and ErpA. The specific function of these "A-type" ISC proteins within the framework of mitochondrial and bacterial Fe/S protein biogenesis is still unresolved. In a comprehensive in vivo analysis, we show that S. cerevisiae Isa1 and Isa2 form a complex that is required for maturation of mitochondrial [4Fe-4S] proteins, including aconitase and homoaconitase. In contrast, Isa1-Isa2 were dispensable for the generation of mitochondrial [2Fe-2S] proteins and cytosolic [4Fe-4S] proteins. Targeting of bacterial [2Fe-2S] and [4Fe-4S] ferredoxins to yeast mitochondria further supported this specificity. Isa1 and Isa2 proteins are shown to bind iron in vivo, yet the Isa1-Isa2-bound iron was not needed as a donor for de novo assembly of the [2Fe-2S] cluster on the general Fe/S scaffold proteins Isu1-Isu2. Upon depletion of the ISC assembly factor Iba57, which specifically interacts with Isa1 and Isa2, or in the absence of the major mitochondrial [4Fe-4S] protein aconitase, iron accumulated on the Isa proteins. These results suggest that the iron bound to the Isa proteins is required for the de novo synthesis of [4Fe-4S] clusters in mitochondria and for their insertion into apoproteins in a reaction mediated by Iba57. Taken together, these findings define Isa1, Isa2, and Iba57 as a specialized, late-acting ISC assembly subsystem that is specifically dedicated to the maturation of mitochondrial [4Fe-4S] proteins.

Indexed as

DNA-Binding ProteinsIronIron-Sulfur ProteinsMitochondrial ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSulfurTranscription FactorsDNA-Binding ProteinsIba57 protein, S cerevisiaeIronIron-Sulfur ProteinsISA1 protein, S cerevisiaeISA2 protein, S cerevisiaeMitochondrial ProteinsSaccharomyces cerevisiae ProteinsSulfurTranscription Factors

Identifiers

PMID21987576
PMCPMC3308834
OpenAlexW2148522029

What OpenQuestion holds

Textmetadata
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.