Evidence map›Paper›PMID 10468587›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae.

B Schilke, C Voisine, H Beinert, E Craig

Abstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers.

0numbers the graph read from it
0cells of the map it votes in
125citing papers in PubMed
30.0field-weighted citation impact, top 1% 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

125 citing papers in PubMed, 283 citations in OpenAlex.

  1. A kinetic mathematical model of comprehensive iron metabolism in a respiring yeast cell: a basic-pathways approach to solving a large system dynamically.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
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  5. Characteristics of the Isu1 C-terminus in relation to [2Fe-2S] cluster assembly and ISCU Myopathy.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
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  15. Fe-S Protein Synthesis in Green Algae Mitochondria.Plants (Basel, Switzerland) · 2021
    Review
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65 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

4 authors at 1 institution in 1 country.

B SchilkeDepartment of Biomolecular Chemistry, University of Wisconsin, 1300 University Avenue, Madison, WI 53706, USA.
C Voisine
H Beinert
E Craig
University of Wisconsin–Madison · US

Funding

TRANSCRIPTIONALLY REGULATED GENESR01GM027870 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CRAIG, ELIZABETH A · 1985 to 2017
$5.8M
NIGMS NIH HHS GM27870NIGMS NIH HHS R01 GM027870
6 · The paper itself

Abstract

nifU of nitrogen-fixing bacteria is involved in the synthesis of the Fe-S cluster of nitrogenase. In a synthetic lethal screen with the mitochondrial heat shock protein (HSP)70, SSQ1, we identified a gene of Saccharomyces cerevisiae, NFU1, which encodes a protein with sequence identity to the C-terminal domain of NifU. Two other yeast genes were found to encode proteins related to the N-terminal domain of bacterial NifU. They have been designated ISU1 and ISU2. Isu1, Isu2, and Nfu1 are located in the mitochondrial matrix. ISU genes of yeast carry out an essential function, because a Deltaisu1Deltaisu2 strain is inviable. Growth of Deltanfu1Delta isu1 cells is significantly compromised, allowing assessment of the physiological roles of Nfu and Isu proteins. Mitochondria from Deltanfu1Deltaisu1 cells have decreased activity of several respiratory enzymes that contain Fe-S clusters. As a result, Deltanfu1Deltaisu1 cells grow poorly on carbon sources requiring respiration. Deltanfu1Deltaisu1 cells also accumulate abnormally high levels of iron in their mitochondria, similar to Deltassq1 cells, indicating a role for these proteins in iron metabolism. We suggest that NFU1 and ISU1 gene products play a role in iron homeostasis, perhaps in assembly, insertion, and/or repair of mitochondrial Fe-S clusters. The conservation of these protein domains in many organisms suggests that this role has been conserved throughout evolution.

Indexed as

Genes, FungalSaccharomyces cerevisiae ProteinsAmino Acid SequenceBacterial ProteinsCell FractionationFungal ProteinsGenes, LethalHSP70 Heat-Shock ProteinsIronMitochondriaMitochondrial ProteinsMolecular ChaperonesMolecular Sequence DataSaccharomyces cerevisiaeSequence AlignmentSequence Homology, Amino AcidBacterial ProteinsFungal ProteinsHSP70 Heat-Shock ProteinsIronISU1 protein, S cerevisiaeISU2 protein, S cerevisiaeMitochondrial ProteinsMolecular ChaperonesNFU1 protein, S cerevisiaeNifU protein, BacteriaSaccharomyces cerevisiae ProteinsSSQ1 protein, S cerevisiae

Identifiers

PMID10468587
PMCPMC17867
OpenAlexW2153371171

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.