Cited by 391Metalloenzymes and iron-sulfur proteinsMitochondrial Function and PathologyEnzyme Structure and Function

Iron–sulfur cluster biogenesis and trafficking in mitochondria

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Braymer, Joseph J., Lill, Roland·2017·Journal of Biological Chemistry

Abstract

The biogenesis of iron-sulfur (Fe/S) proteins in eukaryotes is a multistage, multicompartment process that is essential for a broad range of cellular functions, including genome maintenance, protein translation, energy conversion, and the antiviral response. Genetic and cell biological studies over almost 2 decades have revealed some 30 proteins involved in the synthesis of cellular [2Fe-2S] and [4Fe-4S] clusters and their incorporation into numerous apoproteins. Mechanistic aspects of Fe/S protein biogenesis continue to be elucidated by biochemical and ultrastructural investigations. Here, we review recent developments in the pursuit of constructing a comprehensive model of Fe/S protein assembly in the mitochondrion.

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  • Once inside mitochondria, iron is incorporated into heme and iron-sulfur clusters by frataxin and GLRX5.

    “Once inside the organelle the iron is incorporated into heme and iron-sulfur (Fe-S) clusters by frataxin and GLRX5 (Glutaredoxin-related protein 5) (Lill, 2009; Braymer and Lill, 2017).”

    From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Braymer and Lill, 2017

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  1. [42]42. Angerer, H., Radermacher, M., Man ´kowska, M., Steger, M., Zwicker, K., Heide, H., Wittig, I., Brandt, U., and Zickermann, V. (2014) The LYR protein subunit NB4M/NDUFA6ofmitochondrialcomplexIanchorsan acyl carrier protein and is essential for catalytic activity. Proc. Natl. Acad. Sci. U.S.A. 111, 5207-5212

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Authors
Braymer, J. J., & Lill, R.
Affiliations
Philipps University of Marburg (DE)
Corresponding author
Lill, Roland
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2017-08
Volume
292
Issue
31
Pages
12754-12763
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2625087901
Cited by
389
References
100
Citations by year
2026: 29 · 2025: 29 · 2024: 32 · 2023: 39 · 2022: 45 · 2021: 40 · 2020: 56 · 2019: 44 · 2018: 57 · 2017: 16
FWCI
1.91
Type
journal article
Language
en
Open access
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Deutsche Forschungsgemeinschaft (Koselleck grant, LI 415/5, SFB 987, SPP 1710, and SPP 1927)
  • German-Israeli Foundation for Scientific Research and Development (I-1302-412.13/2015)
  • H2020 Marie Skłodowska-Curie Actions (659325)
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, mitochondrial iron-sulfur proteins, [2Fe-2S] cluster, [4Fe-4S] cluster, cluster assembly, iron-sulfur proteins, genome maintenance, mRNA translation, energy conversion, antiviral response
MeSH terms
Frataxin, Acyl Carrier Protein, Adrenodoxin, Animals, Apoenzymes, Humans, Iron-Sulfur Proteins, Mitochondria, Models, Biological, Models, Molecular, Protein Conformation, Species Specificity, Sulfurtransferases, Gene Expression Regulation, Enzymologic, Protein Folding, Protein Transport, Mitochondrial Proteins, Saccharomyces cerevisiae Proteins, Iron-Binding Proteins, Protein Multimerization

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