Components involved in assembly and dislocation of iron–sulfur clusters on the scaffold protein Isu1p
Open accessAbstract
The mitochondrial proteins Isu1p and Isu2p play an essential role in the maturation of cellular iron-sulfur (Fe/S) proteins in eukaryotes. By radiolabelling of yeast cells with 55Fe we demonstrate that Isu1p binds an oxygen-resistant non-chelatable Fe/S cluster providing in vivo evidence for a scaffolding function of Isu1p during Fe/S cluster assembly. Depletion of the cysteine desulfurase Nfs1p, the ferredoxin Yah1p or the yeast frataxin homologue Yfh1p by regulated gene expression causes a strong decrease in the de novo synthesis of Fe/S clusters on Isu1p. In contrast, depletion of the Hsp70 chaperone Ssq1p, its co-chaperone Jac1p or the glutaredoxin Grx5p markedly increased the amount of Fe/S clusters bound to Isu1p, even though these mitochondrial proteins are crucial for maturation of Fe/S proteins. Hence Ssq1p/Jac1p and Grx5p are required in a step after Fe/S cluster synthesis on Isu1p, for instance in dissociation of preassembled Fe/S clusters from Isu1p and/or their insertion into apoproteins. We propose a model that dissects Fe/S cluster biogenesis into two major steps and assigns its central components to one of these two steps.
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Ssq1 transfers the assembled Fe-S cluster from the Isu1 scaffold to the target protein by destabilizing the connection between the cluster and this scaffold.
“Ssq1 is responsible for transferring the assembled Fe-S cluster from the Isu1 scaffold to the target protein by destabilizing the connection between the cluster and this scaffold (25).”
From Mitochondrial Cochaperone Mge1 Is Involved in Regulating Susceptibility to Fluconazole in <i>Saccharomyces cerevisiae</i> and <i>Candida</i> Species (2017) · cites this paper as [25]
The Discussion (page unavailable) proposes that the Ssq1p/Jac1p chaperone system is most likely required to dislodge a preassembled Fe/S cluster from Isu1p, consistent with a role in transfer to target proteins. It presents this as a proposed role, not an established responsibility, and explicitly says how the chaperones facilitate dislocation remains unknown; it does not establish the claimed destabilization mechanism. (LLM, conf=0.88)
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“Ssq1 is responsible for transferring the assembled Fe-S cluster from the Isu1 scaffold to the target protein by destabilizing the connection between the cluster and this scaffold (25).”
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- Authors
- Mühlenhoff, U., Gerber, J., Richhardt, N., & Lill, R.
- Affiliations
- Philipps University of Marburg (DE)
- Corresponding author
- Lill, Roland
- Venue
- The EMBO Journal
- Published
- 2003-09-15
- Volume
- 22
- Issue
- 18
- Pages
- 4815-4825
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC212715
- OpenAlex
- W1770775467
- Cited by
- 383
- References
- 54
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 3 · 2023: 6 · 2022: 14 · 2021: 10 · 2020: 17 · 2019: 5 · 2018: 12 · 2017: 21 · 2016: 6 · 2015: 14 · 2014: 17 · 2013: 19 · 2012: 26
- FWCI
- 23.94
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- iron-sulfur clusters, iron-sulfur cluster assembly, Hsp70 chaperones, glutaredoxin, yeast, mitochondrial iron-sulfur proteins
- MeSH terms
- Frataxin, Adrenodoxin, Cytosol, Iron-Sulfur Proteins, Mitochondria, Models, Biological, Saccharomyces cerevisiae, Molecular Chaperones, Mitochondrial Proteins, Saccharomyces cerevisiae Proteins, Iron-Binding Proteins
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