Evidence map›Paper›PMID 26396185›Full record

ArticleThe Journal of biological chemistry2015

Cytosolic Fe-S Cluster Protein Maturation and Iron Regulation Are Independent of the Mitochondrial Erv1/Mia40 Import System.

Hatice K Ozer, Adrienne C Dlouhy, Jeremy D Thornton, Jingjing Hu, Yilin Liu, Joseph J Barycki, Janneke Balk, Caryn E Outten

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

10 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. A copper(II)-binding triazole derivative with ionophore properties is active against Candida spp.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Article
  5. Article
  6. Review
  7. Article
  8. Clinical and genetic aspects of defects in the mitochondrial iron-sulfur cluster synthesis pathway.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Review
  9. Iron-sulfur clusters: from metals through mitochondria biogenesis to disease.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Review
  10. Article
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

8 authors at 3 institutions in 2 countries.

Hatice K OzerFrom the Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208.
Adrienne C DlouhyFrom the Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208.
Jeremy D Thorntonthe John Innes Centre and University of East Anglia, Norwich Research Park, Norwich NR4 7UH, United Kingdom, and.
Jingjing HuFrom the Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208.
Yilin Liuthe Department of Biochemistry and the Redox Biology Center, University of Nebraska, Lincoln, Nebraska 68588.
Joseph J Baryckithe Department of Biochemistry and the Redox Biology Center, University of Nebraska, Lincoln, Nebraska 68588.
Janneke Balkthe John Innes Centre and University of East Anglia, Norwich Research Park, Norwich NR4 7UH, United Kingdom, and.
Caryn E OuttenFrom the Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208, outten@mailbox.sc.edu.
University of South Carolina · USJohn Innes Centre · GBUniversity of Nebraska–Lincoln · US

Funding

Glutathione and Redox Control in the Mitochondrial Intermembrane SpaceR01GM086619 · NIGMS · UNIVERSITY OF SOUTH CAROLINA AT COLUMBIA · PI OUTTEN, CARYN E · 2010 to 2015
$1.5M
Structural insights into redox homeostasisR01GM077289 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI BARYCKI, JOSEPH J · 2006 to 2010
$1.4M
Biotechnology and Biological Sciences Research CouncilNIGMS NIH HHS GM077289NIGMS NIH HHS GM086619NIGMS NIH HHS R01 GM077289NIGMS NIH HHS R01 GM086619
6 · The paper itself

Abstract

The sulfhydryl oxidase Erv1 partners with the oxidoreductase Mia40 to import cysteine-rich proteins in the mitochondrial intermembrane space. In Saccharomyces cerevisiae, Erv1 has also been implicated in cytosolic Fe-S protein maturation and iron regulation. To investigate the connection between Erv1/Mia40-dependent mitochondrial protein import and cytosolic Fe-S cluster assembly, we measured Mia40 oxidation and Fe-S enzyme activities in several erv1 and mia40 mutants. Although all the erv1 and mia40 mutants exhibited defects in Mia40 oxidation, only one erv1 mutant strain (erv1-1) had significantly decreased activities of cytosolic Fe-S enzymes. Further analysis of erv1-1 revealed that it had strongly decreased glutathione (GSH) levels, caused by an additional mutation in the gene encoding the glutathione biosynthesis enzyme glutamate cysteine ligase (GSH1). To address whether Erv1 or Mia40 plays a role in iron regulation, we measured iron-dependent expression of Aft1/2-regulated genes and mitochondrial iron accumulation in erv1 and mia40 strains. The only strain to exhibit iron misregulation is the GSH-deficient erv1-1 strain, which is rescued with addition of GSH. Together, these results confirm that GSH is critical for cytosolic Fe-S protein biogenesis and iron regulation, whereas ruling out significant roles for Erv1 or Mia40 in these pathways.

Indexed as

Amino Acid SequenceCytosolGlutamate-Cysteine LigaseGlutathioneIronIron-Sulfur ProteinsMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsMolecular Sequence DataMutationOxidation-ReductionOxidoreductasesOxidoreductases Acting on Sulfur Group DonorsProtein TransportERV1 protein, S cerevisiaeGlutamate-Cysteine LigaseGlutathioneGSH1 protein, S cerevisiaeIronIron-Sulfur ProteinsMIA40 protein, S cerevisiaeMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsOxidoreductasesOxidoreductases Acting on Sulfur Group DonorsSaccharomyces cerevisiae Proteinsglutathioneiron metabolismiron-sulfur proteinmitochondrial metabolismmitochondrial transportsulfhydryl

Identifiers

PMID26396185
PMCPMC4646028
OpenAlexW2282554994

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.