Iron–sulphur cluster biogenesis and mitochondrial iron homeostasis (original) (raw)

• Beinert, H., Holm, R. H. & Munck, E. Iron–sulfur clusters: nature's modular, multipurpose structures. Science 277, 653–659 (1997).
  Article CAS Google Scholar
• Rees, D. C. Great metalloclusters in enzymology. Annu. Rev. Biochem. 71, 221–246 (2002).
  Article CAS Google Scholar
• Beinert, H. Iron–sulfur proteins: ancient structures, still full of surprises. J. Biol. Inorg. Chem. 5, 2–15 (2000).
  Article CAS Google Scholar
• Schultz, B. E. & Chan, S. I. Structures and proton-pumping strategies of mitochondrial respiratory enzymes. Annu. Rev. Biophys. Biomol. Struct. 30, 23–65 (2001).
  Article CAS Google Scholar
• Wollman, F. A., Minai, L. & Nechushtai, R. The biogenesis and assembly of photosynthetic proteins in thylakoid membranes. Biochim. Biophys. Acta 1411, 21–85 (1999).
  Article CAS Google Scholar
• Frey, P. A. & Magnusson, O. T. _S_-adenosylmethionine: a wolf in sheep's clothing, or a rich man's adenosylcobalamin? Chem. Rev. 103, 2129–2148 (2003).
  Article CAS Google Scholar
• Aspinwall, R. et al. Cloning and characterization of a functional human homolog of Escherichia coli endonuclease III. Proc. Natl Acad. Sci. USA 94, 109–114 (1997).
  Article CAS Google Scholar
• McGoldrick, J. P. et al. Characterization of a mammalian homolog of the Escherichia coli MutY mismatch repair protein. Mol. Cell. Biol. 15, 989–996 (1995).
  Article CAS Google Scholar
• Kiley, P. J. & Beinert, H. The role of Fe–S proteins in sensing and regulation in bacteria. Curr. Opin. Microbiol. 6, 181–185 (2003).
  Article CAS Google Scholar
• Bouton, C. & Drapier, J. C. Iron regulatory proteins as NO signal transducers. Sci. STKE 182, pe17 (2003).
  Google Scholar
• Rouault, T. & Klausner, R. Regulation of iron metabolism in eukaryotes. Curr. Top. Cell Regul. 35, 1–19 (1997).
  Article CAS Google Scholar
• Meyron-Holtz, E. G., Ghosh, M. C. & Rouault, T. A. Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo. Science 306, 2087–2090 (2004).
  Article CAS Google Scholar
• Meyron-Holtz, E. G. et al. Genetic ablations of iron regulatory proteins 1 and 2 reveal why iron regulatory protein 2 dominates iron homeostasis. EMBO J. 23, 386–395 (2004).
  Article CAS Google Scholar
• Pantopoulos, K. Iron metabolism and the IRE/IRP regulatory system: an update. Ann. NY Acad. Sci. 1012, 1–13 (2004).
  Article CAS Google Scholar
• Frazzon, J. & Dean, D. R. Formation of iron–sulfur clusters in bacteria: an emerging field in bioinorganic chemistry. Curr. Opin. Chem. Biol. 7, 166–173 (2003).
  Article CAS Google Scholar
• Gerber, J. & Lill, R. Biogenesis of iron–sulfur proteins in eukaryotes: components, mechanism and pathology. Mitochondrion 2, 71–86 (2002).
  Article CAS Google Scholar
• Seidler, A., Jaschkowitz, K. & Wollenberg, M. Incorporation of iron–sulphur clusters in membrane-bound proteins. Biochem. Soc. Trans. 29, 418–421 (2001).
  Article CAS Google Scholar
• Leon, S. et al. The AtNFS2 gene from Arabidopsis thaliana encodes a NifS-like plastidial cysteine desulphurase. Biochem. J. 366, 557–564 (2002).
  Article CAS Google Scholar
• Agar, J. N. et al. IscU as a scaffold for iron–sulfur cluster biosynthesis: sequential assembly of [2Fe–2S] and [4Fe–4S] clusters in IscU. Biochemistry 39, 7856–7862 (2000).
  Article CAS Google Scholar
• Muhlenhoff, U. et al. Components involved in assembly and dislocation of iron–sulfur clusters on the scaffold protein Isu1p. EMBO J. 22, 4815–4825 (2003).
  Article Google Scholar
• Nishio, K. & Nakai, M. Transfer of iron–sulfur cluster from NifU to apoferredoxin. J. Biol. Chem. 275, 22615–22618 (2000).
  Article CAS Google Scholar
• Yabe, T. et al. The Arabidopsis chloroplastic NifU-like protein CnfU, which can act as an iron–sulfur cluster scaffold protein, is required for biogenesis of ferredoxin and photosystem I. Plant Cell 16, 993–1007 (2004).
  Article CAS Google Scholar
• Land, T. & Rouault, T. A. Targeting of a human iron–sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization. Mol. Cell 2, 807–815 (1998).
  Article CAS Google Scholar
• Tong, W. H. & Rouault, T. Distinct iron–sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells. EMBO J. 19, 5692–5700 (2000).
  Article CAS Google Scholar
• Tong, W. H. et al. Subcellular compartmentalization of human Nfu, an iron–sulfur cluster scaffold protein, and its ability to assemble a [4Fe–4S] cluster. Proc. Natl Acad. Sci. USA 100, 9762–9767 (2003).
  Article CAS Google Scholar
• Kispal, G. et al. The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins. EMBO J. 18, 3981–3989 (1999).
  Article CAS Google Scholar
• Li, J. et al. Yeast mitochondrial protein, Nfs1p, coordinately regulates iron–sulfur cluster proteins, cellular iron uptake, and iron distribution. J. Biol. Chem. 274, 33025–33034 (1999).
  Article CAS Google Scholar
• Strain, J. et al. Suppressors of superoxide dismutase (SOD1) deficiency in S. cerevisiae. J. Biol. Chem. 273, 31138–31144 (1998).
  Article CAS Google Scholar
• Knight, S. A. et al. Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis. J. Biol. Chem. 273, 18389–18393 (1998).
  Article CAS Google Scholar
• Garland, S. A. et al. Saccharomyces cerevisiae ISU1 and ISU2: members of a well-conserved gene family for iron–sulfur cluster assembly. J. Mol. Biol. 294, 897–907 (1999).
  Article CAS Google Scholar
• Schilke, B. et al. Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 96, 10206–10211 (1999).
  Article CAS Google Scholar
• Chen, O. S. et al. Transcription of the yeast iron regulon responds not directly to iron but rather to iron–sulfur cluster biosynthesis. J. Biol. Chem. 279, 29513–29518 (2004).
  Article CAS Google Scholar
• Rutherford, J. C. et al. Activation of the iron regulon by the yeast Aft1/Aft2 transcription factors depends on mitochondrial, but not cytosolic iron–sulfur protein biogenesis. J. Biol. Chem. 13 Jan 2005 (doi:10.1074/jbc.M413731200).
• Puccio, H. & Koenig, M. Recent advances in the molecular pathogenesis of Friedreich ataxia. Hum. Mol. Genet. 9, 887–892 (2000).
  Article CAS Google Scholar
• Pandolfo, M. Friedreich ataxia. Semin. Pediatr. Neurol. 10, 163–172 (2003).
  Article Google Scholar
• Campuzano, V. et al. Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion. Science 271, 1423–1427 (1996).
  Article CAS Google Scholar
• Rotig, A. et al. Aconitase and mitochondrial iron–sulphur protein deficiency in Friedreich ataxia. Nature Genet. 17, 215–217 (1997).
  Article CAS Google Scholar
• Babcock, M. et al. Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog of frataxin. Science 276, 1709–1712 (1997).
  Article CAS Google Scholar
• Gerber, J., Muhlenhoff, U. & Lill, R. An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1. EMBO Rep. 4, 906–911 (2003).
  Article CAS Google Scholar
• Ramazzotti, A., Vanmansart, V. & Foury, F. Mitochondrial functional interactions between frataxin and Isu1p, the iron–sulfur cluster scaffold protein, in Saccharomyces cerevisiae. FEBS Lett. 557, 215–220 (2004).
  Article CAS Google Scholar
• Bulteau, A. L. et al. Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science 305, 242–245 (2004).
  Article CAS Google Scholar
• Seznec, H. et al. Idebenone delays the onset of cardiac functional alteration without correction of Fe–S enzymes deficit in a mouse model for Friedreich ataxia. Hum. Mol. Genet. 13, 1017–1024 (2004).
  Article CAS Google Scholar
• Puccio, H. et al. Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe–S enzyme deficiency followed by intramitochondrial iron deposits. Nature Genet. 27, 181–186 (2001).
  Article CAS Google Scholar
• Cavadini, P. et al. Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia. Hum. Mol. Genet. 11, 217–227 (2002).
  Article CAS Google Scholar
• Gakh, O. et al. Physical evidence that yeast frataxin is an iron storage protein. Biochemistry 41, 6798–6804 (2002).
  Article CAS Google Scholar
• Radisky, D. C., Babcock, M. C. & Kaplan, J. The yeast frataxin homologue mediates mitochondrial iron efflux. Evidence for a mitochondrial iron cycle. J. Biol. Chem. 274, 4497–4499 (1999).
  Article CAS Google Scholar
• Aloria, K. et al. Iron-induced oligomerization of yeast frataxin homologue Yfh1 is dispensable in vivo. EMBO Rep. 5, 1096–1101 (2004).
  Article CAS Google Scholar
• Hentze, M. W., Muckenthaler, M. U. & Andrews, N. C. Balancing acts: molecular control of mammalian iron metabolism. Cell 117, 285–297 (2004).
  Article CAS Google Scholar
• Foury, F. & Talibi, D. Mitochondrial control of iron homeostasis. A genome wide analysis of gene expression in a yeast frataxin-deficient strain. J. Biol. Chem. 276, 7762–7768 (2001).
  Article CAS Google Scholar
• Lill, R. & Kispal, G. Maturation of cellular Fe–S proteins: an essential function of mitochondria. Trends Biochem. Sci. 25, 352–356 (2000).
  Article CAS Google Scholar
• Gerber, J. et al. The yeast scaffold proteins Isu1p and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteins. Mol. Cell. Biol. 24, 4848–4857 (2004).
  Article CAS Google Scholar
• Alcindor, T. & Bridges, K. R. Sideroblastic anaemias. Br. J. Haematol. 116, 733–743 (2002).
  Article Google Scholar
• Djaldetti, M. et al. Ultrastructural features of bone marrow cells from patients with acquired sideroblastic anemia. Microsc. Res. Tech. 63, 155–158 (2004).
  Article Google Scholar
• Balk, J. et al. The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron–sulphur proteins. EMBO J. 23, 2105–2115 (2004).
  Article CAS Google Scholar
• Chloupkova, M., LeBard, L. S. & Koeller, D. M. MDL1 is a high copy suppressor of ATM1: evidence for a role in resistance to oxidative stress. J. Mol. Biol. 331, 155–165 (2003).
  Article CAS Google Scholar
• Li, L. & Kaplan, J. A mitochondrial–vacuolar signaling pathway in yeast that affects iron and copper metabolism. J. Biol. Chem. 279, 33653–33661 (2004).
  Article CAS Google Scholar
• Butow, R. A. & Avadhani, N. G. Mitochondrial signaling: the retrograde response. Mol. Cell 14, 1–15 (2004).
  Article CAS Google Scholar
• Zhao, Q. et al. A mitochondrial specific stress response in mammalian cells. EMBO J. 21, 4411–4419 (2002).
  Article CAS Google Scholar
• Lesuisse, E. et al. Role of YHM1, encoding a mitochondrial carrier protein, in iron distribution of yeast. Biochem. J. 378, 599–607 (2004).
  Article CAS Google Scholar
• Van Ho, A., Ward, D. M. & Kaplan, J. Transition metal transport in yeast. Annu. Rev. Microbiol. 56, 237–261 (2002).
  Article CAS Google Scholar
• Tovar, J. et al. Mitochondrial remnant organelles of Giardia function in iron–sulphur protein maturation. Nature 426, 172–176 (2003).
  Article CAS Google Scholar
• Roy, A. et al. A novel eukaryotic factor for cytosolic Fe–S cluster assembly. EMBO J. 22, 4826–4835 (2003).
  Article CAS Google Scholar
• Nakai, Y., Nakai, M., Hayashi, H. & Kagamiyama, H. Nuclear localization of yeast Nfs1p is required for cell survival. J. Biol. Chem. 276, 8314–8320 (2001).
  Article CAS Google Scholar
• Nakai, Y. et al. Yeast Nfs1p is involved in thio-modification of both mitochondrial and cytoplasmic tRNAs. J. Biol. Chem. 279, 12363–12368 (2004).
  Article CAS Google Scholar
• Sutak, R. et al. Mitochondrial-type assembly of FeS centers in the hydrogenosomes of the amitochondriate eukaryote Trichomonas vaginalis. Proc. Natl Acad. Sci. USA 101, 10368–10373 (2004).
  Article CAS Google Scholar
• Huynen, M. A. et al. The phylogenetic distribution of frataxin indicates a role in iron–sulfur cluster protein assembly. Hum. Mol. Genet. 10, 2463–2468 (2001).
  Article CAS Google Scholar
• Lareau, L. F. et al. The evolving roles of alternative splicing. Curr. Opin. Struct. Biol. 14, 273–282 (2004).
  Article CAS Google Scholar
• Morris, D. R. & Geballe, A. P. Upstream open reading frames as regulators of mRNA translation. Mol. Cell. Biol. 20, 8635–8642 (2000).
  Article CAS Google Scholar
• Rees, D. C. & Howard, J. B. The interface between the biological and inorganic worlds: iron–sulfur metalloclusters. Science 300, 929–931 (2003).
  Article CAS Google Scholar
• Foury, F. & Roganti, T. Deletion of the mitochondrial carrier genes MRS3 and MRS4 suppresses mitochondrial iron accumulation in a yeast frataxin-deficient strain. J. Biol. Chem. 277, 24475–24483 (2002).
  Article CAS Google Scholar