Evidence map›Paper›PMID 24066190›Full record

ArticleOxidative medicine and cellular longevity2013

Mitochondrial DNA instability in cells lacking aconitase correlates with iron citrate toxicity.

Muhammad A Farooq, Tammy M Pracheil, Zhejun Dong, Fei Xiao, Zhengchang Liu

Open access · hybridAbstract read
In one paragraph

Article in Oxidative medicine and cellular longevity, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Kinetic and Regulatory Properties ofInternational journal of molecular sciences · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Organization and dynamics of yeast mitochondrial nucleoids.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2017
    Review
  10. Article
  11. Article
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  13. Review
  14. Article
  15. Review
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 at 2 institutions in 2 countries.

Muhammad A FarooqDepartment of Biological Sciences, University of New Orleans, New Orleans, LA 70148, USA.
Tammy M Pracheil
Zhejun Dong
Fei Xiao
Zhengchang Liu
University of New Orleans · USBeijing Hospital · CN

Funding

Amino Acid Sensing and Signaling in YeastR15GM094772 · NIGMS · UNIVERSITY OF NEW ORLEANS · PI LIU, ZHENGCHANG · 2011 to 2011
$284k
NIGMS NIH HHS 1R15GM094772-01A1NIGMS NIH HHS R15 GM094772
6 · The paper itself

Abstract

Aconitase, the second enzyme of the tricarboxylic acid cycle encoded by ACO1 in the budding yeast Saccharomyces cerevisiae, catalyzes the conversion of citrate to isocitrate. aco1Δ results in mitochondrial DNA (mtDNA) instability. It has been proposed that Aco1 binds to mtDNA and mediates its maintenance. Here we propose an alternative mechanism to account for mtDNA loss in aco1Δ mutant cells. We found that aco1Δ activated the RTG pathway, resulting in increased expression of genes encoding citrate synthase. By deleting RTG1, RTG3, or genes encoding citrate synthase, mtDNA instability was prevented in aco1Δ mutant cells. Increased activity of citrate synthase leads to iron accumulation in the mitochondria. Mutations in MRS3 and MRS4, encoding two mitochondrial iron transporters, also prevented mtDNA loss due to aco1Δ. Mitochondria are the main source of superoxide radicals, which are converted to H2O2 through two superoxide dismutases, Sod1 and Sod2. H2O2 in turn reacts with Fe(2+) to generate very active hydroxyl radicals. We found that loss of Sod1, but not Sod2, prevents mtDNA loss in aco1Δ mutant cells. We propose that mtDNA loss in aco1Δ mutant cells is caused by the activation of the RTG pathway and subsequent iron citrate accumulation and toxicity.

Indexed as

Aconitate HydrataseBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsCation Transport ProteinsDNA, MitochondrialIron Regulatory Protein 1Microscopy, FluorescenceMitochondrial ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSuperoxide DismutaseSuperoxide Dismutase-1Superoxide Dismutase 2Aconitate HydrataseBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsCation Transport ProteinsDNA, MitochondrialIron Regulatory Protein 1Mitochondrial ProteinsMRS3 protein, S cerevisiaeMRS4 protein, S cerevisiaeRTG1 protein, S cerevisiaeRTG3 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSuperoxide DismutaseSuperoxide Dismutase-1Superoxide Dismutase 2

Identifiers

PMID24066190
PMCPMC3770056
OpenAlexW1999476577

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.