Cited by 255Mitochondrial Function and PathologyGenetic Neurodegenerative DiseasesNeurological diseases and metabolism

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Iron-Dependent Self-Assembly of Recombinant Yeast Frataxin: Implications for Friedreich Ataxia

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Adamec, Jiri, Rusnak, Frank, Owen, Whyte G., Naylor, Stephen, Benson, Linda M., Gacy, A. Marquis, Isaya, Grazia·2000·The American Journal of Human Genetics

DOI 10.1086/303056PMC PMC1287515

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Abstract

Frataxin deficiency is the primary cause of Friedreich ataxia (FRDA), an autosomal recessive cardiodegenerative and neurodegenerative disease. Frataxin is a nuclear-encoded mitochondrial protein that is widely conserved among eukaryotes. Genetic inactivation of the yeast frataxin homologue (Yfh1p) results in mitochondrial iron accumulation and hypersensitivity to oxidative stress. Increased iron deposition and evidence of oxidative damage have also been observed in cardiac tissue and cultured fibroblasts from patients with FRDA. These findings indicate that frataxin is essential for mitochondrial iron homeostasis and protection from iron-induced formation of free radicals. The functional mechanism of frataxin, however, is still unknown. We have expressed the mature form of Yfh1p (mYfh1p) in Escherichia coli and have analyzed its function in vitro. Isolated mYfh1p is a soluble monomer (13,783 Da) that contains no iron and shows no significant tendency to self-associate. Aerobic addition of ferrous iron to mYfh1p results in assembly of regular spherical multimers with a molecular mass of approximately 1. 1 MDa (megadaltons) and a diameter of 13+/-2 nm. Each multimer consists of approximately 60 subunits and can sequester >3,000 atoms of iron. Titration of mYfh1p with increasing iron concentrations supports a stepwise mechanism of multimer assembly. Sequential addition of an iron chelator and a reducing agent results in quantitative iron release with concomitant disassembly of the multimer, indicating that mYfh1p sequesters iron in an available form. In yeast mitochondria, native mYfh1p exists as monomer and a higher-order species with a molecular weight >600,000. After addition of (55)Fe to the medium, immunoprecipitates of this species contain >16 atoms of (55)Fe per molecule of mYfh1p. We propose that iron-dependent self-assembly of recombinant mYfh1p reflects a physiological role for frataxin in mitochondrial iron sequestration and bioavailability.

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Authors: Adamec, J., Rusnak, F., Owen, W. G., Naylor, S., Benson, L. M., Gacy, A. M., & Isaya, G.
Affiliations: University of Minnesota Rochester (US)
Mayo Clinic (US)
Corresponding author: Isaya, Grazia
ORCID: Naylor, Stephen
Isaya, Grazia
Venue: The American Journal of Human Genetics
Publisher: Elsevier BV
Published: 2000-09
Volume: 67
Issue: 3
Pages: 549-562
ISSN: 0002-9297 (ISSN-L)
DOI: 10.1086/303056
PMC: PMC1287515
OpenAlex: W2080731376
Cited by: 255
References: 34
Citations by year: 2026: 3 · 2025: 4 · 2024: 2 · 2023: 1 · 2022: 3 · 2021: 5 · 2020: 5 · 2019: 10 · 2018: 6 · 2017: 9 · 2016: 8 · 2015: 7 · 2014: 9 · 2013: 10 · 2012: 6
FWCI: 8.08
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 4704 d)
Locations: The American Journal of Human Genetics (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute on Aging (AG-15709, R01AG015709)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
Keywords: frataxin, Friedreich's ataxia, mitochondrial iron homeostasis, iron sequestration, iron chelation, oxidative stress, iron bioavailability, recombinant protein expression
MeSH terms: Frataxin, Chromatography, Gel, Escherichia coli, Friedreich Ataxia, Homeostasis, Humans, Iron, Iron Chelating Agents, Microscopy, Electron, Mitochondria, Models, Biological, Molecular Sequence Data, Molecular Weight, Protein Binding, Recombinant Proteins, Saccharomyces cerevisiae, Solubility, Phosphotransferases (Alcohol Group Acceptor), Oxidative Stress, Microscopy, Atomic Force, Reducing Agents, Protein Structure, Quaternary, Iron-Binding Proteins

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Iron-Dependent Self-Assembly of Recombinant Yeast Frataxin: Implications for Friedreich Ataxia

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