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Inhibition of Fe-S cluster biosynthesis decreases mitochondrial iron export: Evidence that Yfh1p affects Fe-S cluster synthesis
Open accessAbstract
Decreased expression of Yfh1p in the budding yeast, Saccharomyces cerevisiae , and the orthologous human gene frataxin results in respiratory deficiency and mitochondrial iron accumulation. The absence of Yfh1p decreases mitochondrial iron export. We demonstrate that decreased expression of Nfs1p, the yeast cysteine desulfurase that plays a central role in Fe-S cluster synthesis, also results in mitochondrial iron accumulation due to decreased export of mitochondrial iron. In the absence of Yfh1p, activity of Fe-S-containing enzymes (aconitase, succinate dehydrogenase) is decreased, whereas the activity of a non-Fe-S-containing enzyme (malate dehydrogenase) is unaffected. Aconitase protein was abundant even though the activity of aconitase was decreased in both aerobic and anaerobic conditions. These results demonstrate a direct role of Yfh1p in the formation of Fe-S clusters and indicate that mitochondrial iron export requires Fe-S cluster biosynthesis.
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“Mouse T-cell immunoglobulin-domain and mucin-domain (TIM)-2 was identified as a ferritin H subunit receptor (48)”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [48]
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“Additional experiments also showed that ferritin L did not interact with TIM-2 (48).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [48]
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“Ferritin H incorporation was not observed in the absence of TIM-2 (48).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [48]
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Metadata
- Authors
- Chen, O. S., Hemenway, S., & Kaplan, J.
- Affiliations
- University of Utah (US)
- ORCID
- Chen, Opal S.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2002-09-09
- Volume
- 99
- Issue
- 19
- Pages
- 12321-12326
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC129443
- OpenAlex
- W2039280518
- Cited by
- 152
- References
- 31
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 3 · 2023: 3 · 2022: 1 · 2021: 8 · 2020: 5 · 2019: 4 · 2018: 2 · 2017: 5 · 2015: 2 · 2014: 5 · 2013: 8 · 2012: 7
- FWCI
- 16.64
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases (DK 52380, R01DK052380)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Keywords
- frataxin, iron-sulfur cluster assembly, mitochondrial iron accumulation, Saccharomyces cerevisiae, aconitase, succinate dehydrogenase, malate dehydrogenase, respiratory deficiency, cysteine desulfurase
- MeSH terms
- Frataxin, Aconitate Hydratase, Biological Transport, Active, Carrier Proteins, Fungal Proteins, Humans, Iron, Iron-Sulfur Proteins, Mitochondria, Oxidation-Reduction, RNA, Fungal, RNA, Messenger, Saccharomyces cerevisiae, Sulfurtransferases, Mitochondrial Proteins, Saccharomyces cerevisiae Proteins, Iron-Binding Proteins
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