Inhibition of Fe-S cluster biosynthesis decreases mitochondrial iron export: Evidence that Yfh1p affects Fe-S cluster synthesis

Chen, Opal S.; Hemenway, Shawn; Kaplan, Jerry

doi:10.1073/pnas.192449599

Cited by 152Metalloenzymes and iron-sulfur proteinsMitochondrial Function and PathologyNeurological diseases and metabolism

Inhibition of Fe-S cluster biosynthesis decreases mitochondrial iron export: Evidence that Yfh1p affects Fe-S cluster synthesis

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Chen, Opal S., Hemenway, Shawn, Kaplan, Jerry·2002·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.192449599PMC PMC129443

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Abstract

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 TIM-2 was identified as a ferritin H subunit receptor.
“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]
Ferritin L did not interact with TIM-2.
“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]
Ferritin H incorporation was not observed in the absence of TIM-2.
“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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Campuzano, V., Montermini, L., Moltò, M. D., Pianese, L., Cossée, M., Cavalcanti, F., Monros, E., Rodius, F., Duclos, F., Monticelli, A., et al. (1996) · Science · doi:10.1126/science.271.5254.1423 · Cited by 2,786 · see citing works
Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria.
Daum, G., Böhni, P. C., & Schatz, G. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33617-2 · Cited by 1,152 · see citing works
Aconitase and mitochondrial iron–sulphur protein deficiency in Friedreich ataxia
Rötig, A., de Lonlay, P., Chretien, D., Foury, F., Koenig, M., Sidi, D., Munnich, A., & Rustin, P. (1997) · Nature Genetics · doi:10.1038/ng1097-215 · Cited by 991 · see citing works
Regulation of Mitochondrial Iron Accumulation by Yfh1p, a Putative Homolog of Frataxin
Babcock, M., de Silva, D., Oaks, R., Davis-Kaplan, S., Jiralerspong, S., Montermini, L., Pandolfo, M., & Kaplan, J. (1997) · Science · doi:10.1126/science.276.5319.1709 · Cited by 921 · see citing works
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The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
Kispál, G., Csere, P., Prohl, C., & Lill, R. (1999) · The EMBO Journal · doi:10.1093/emboj/18.14.3981 · Cited by 699 · see citing works
Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae
Cabiscol, E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003140200 · Cited by 418 · see citing works
CCC1 Is a Transporter That Mediates Vacuolar Iron Storage in Yeast
Li, L., Chen, O. S., Ward, D. M., & Kaplan, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103944200 · Cited by 354 · see citing works
Self-citation
Respiratory deficiency due to loss of mitochondrial DNA in yeast lacking the frataxin homologue
Wilson, R. B., & Roof, D. M. (1997) · Nature Genetics · doi:10.1038/ng0897-352 · Cited by 345 · see citing works
Oxidative Stress Promotes Specific Protein Damage inSaccharomyces cerevisiae
Cabiscol, E., Piulats, E., Echave, P., Herrero, E., & Ros, J. (2000) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)61523-1 · Cited by 334 · see citing works
The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins
Mühlenhoff, U. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.17.2025 · Cited by 326 · see citing works
Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
Schilke, B. A., Voisine, C., Beinert, H., & Craig, E. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10206 · Cited by 284 · see citing works
The Yeast Frataxin Homologue Mediates Mitochondrial Iron Efflux
Radisky, D. C., Babcock, M. C., & Kaplan, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.8.4497 · Cited by 277 · see citing works
Self-citation
A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins
Lange, H., Kaut, A., Kispál, G., & Lill, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.3.1050 · Cited by 272 · see citing works
Iron-Dependent Self-Assembly of Recombinant Yeast Frataxin: Implications for Friedreich Ataxia
Adamec, J., Rusnak, F., Owen, W. G., Naylor, S., Benson, L. M., Gacy, A. M., & Isaya, G. (2000) · The American Journal of Human Genetics · doi:10.1086/303056 · Cited by 255 · see citing works
Mutations in PMR1 suppress oxidative damage in yeast cells lacking superoxide dismutase
Lapinskas, P. J., Cunningham, K. W., Liu, X. F., Fink, G. R., & Culotta, V. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.3.1382 · Cited by 240 · see citing works
Parallel pathways of gene regulation: homologous regulators SWI5 and ACE2 differentially control transcription of HO and chitinase.Preprint
Dohrmann, P. R., Butler, G., Tamai, T. K., Dorland, S., Greene, J. R., Thiele, D. J., & Stillman, D. J. (1992) · Genes & Development · doi:10.1101/gad.6.1.93 · Cited by 220 · see citing works
Yeast Mitochondrial Protein, Nfs1p, Coordinately Regulates Iron-Sulfur Cluster Proteins, Cellular Iron Uptake, and Iron Distribution
Li, J., Kogan, M., Knight, S. A. B., Pain, D., & Dancis, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.46.33025 · Cited by 201 · see citing works
Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells
Tong, W., & Rouault, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5692 · Cited by 194 · see citing works
Subcellular Localization of Aft1 Transcription Factor Responds to Iron Status in Saccharomyces cerevisiae
Yamaguchi‐Iwai, Y., Ueta, R., Fukunaka, A., & Sasaki, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200949200 · Cited by 174 · see citing works
The Essential Role of Mitochondria in the Biogenesis of Cellular Iron-Sulfur Proteins
Lill, R., Diekert, K., Kaut, A., Lange, H., Pelzer, W., Prohl, C., & Kispál, G. (1999) · Biological Chemistry · doi:10.1515/bc.1999.147 · Cited by 156 · see citing works
Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain
Foury, F. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00961-8 · Cited by 145 · see citing works
Assay of Succinate Dehydrogenase Activity by a Colorimetric-Continuous Method Using Iodonitrotetrazolium Chloride as Electron Acceptor
Munujos, P., Collcanti, J., González‐Sastre, F., & Gella, F.-J. (1993) · Analytical Biochemistry · doi:10.1006/abio.1993.1360 · Cited by 126 · see citing works
The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria
Lutz, T., Westermann, B., Neupert, W., & Herrmann, J. M. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4527 · Cited by 125 · see citing works
Functional analysis reports. Precise gene disruption in Saccharomyces cerevisiae by double fusion polymerase chain reaction
Amberg, D. C., Botstein, D., & Beasley, E. M. (1995) · Yeast · doi:10.1002/yea.320111307 · Cited by 124 · see citing works
Adrenodoxin Reductase Homolog (Arh1p) of Yeast Mitochondria Required for Iron Homeostasis
Li, J., Saxena, S., Pain, D., & Dancis, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007198200 · Cited by 119 · see citing works
Dietary Iron Intake Modulates the Activity of Iron Regulatory Proteins and the Abundance of Ferritin and Mitochondrial Aconitase in Rat Liver , ,
Chen, O. S., Schalinske, K. L., & Eisenstein Richard, S. (1997) · Journal of Nutrition · doi:10.1093/jn/127.2.238 · Cited by 110 · see citing works
Self-citation
[18] Mitochondrial l-malate dehydrogenase of beef heart
Englard, S., & Siegel, L. (1969) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(69)13022-0 · Cited by 95 · see citing works
Novel role of phosphorylation in Fe–S cluster stability revealed by phosphomimetic mutations at Ser-138 of iron regulatory protein 1
Brown, N. M., Anderson, S. A., Steffen, D. W., Carpenter, T. B., Kennedy, M. C., Walden, W. E., & Eisenstein, R. S. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.26.15235 · Cited by 83 · see citing works
CCC1 Suppresses Mitochondrial Damage in the Yeast Model of Friedreich's Ataxia by Limiting Mitochondrial Iron Accumulation
Chen, O. S., & Kaplan, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.7626 · Cited by 77 · see citing works
Self-citation
The Aconitase Function of Iron Regulatory Protein 1
Narahari, J., Ma, R., Wang, M., & Walden, W. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910450199 · Cited by 66 · see citing works
YFH1‐mediated iron homeostasis is independent of mitochondrial respiration
Chen, O. S., & Kaplan, J. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)03137-4 · Cited by 11 · see citing works
Self-citation

Flagged first, then by citations

Research works printed but not linked: 30

[1]Campuzano V., Montermini, L., Molto, M. D., Pianese, L., Cossee, M., Cavalcanti, F., Monros, E., Rodius, F., Duclos, F., Monticelli, A., et al. (1996) Science 271, 1423-1427. [DOI] [PubMed] [Google Scholar]
[2]Babcock M., de Silva, D., Oaks, R., Davis-Kaplan, S., Jiralerspong, S., Montermini, L., Pandolfo, M. & Kaplan, J. (1997) Science 276, 1709-1172. [DOI] [PubMed] [Google Scholar]
[3]Radisky D. C., Babcock, M. C. & Kaplan, J. (1999) J. Biol. Chem. 274, 4497-4499. [DOI] [PubMed] [Google Scholar]
[4]Foury F. (1999) FEBS Lett. 456, 281-284. [DOI] [PubMed] [Google Scholar]
[5]Chen O. S. & Kaplan, J. (2000) J. Biol. Chem. 275, 7626-7632. [DOI] [PubMed] [Google Scholar]
[6]Lill R., Diekert, K., Kaut, A., Lange, H., Pelzer, W., Prohl, C. & Kispal, G. (1999) Biol Chem 380, 1157-1166. [DOI] [PubMed] [Google Scholar]
[7]Kispal G., Csere, P., Prohl, C. & Lill, R. (1999) EMBO J. 18, 3981-3989. [DOI] [PMC free article] [PubMed] [Google Scholar]
[8]Li J., Kogan, M., Knight, S. A., Pain, D. & Dancis, A. (1999) J. Biol. Chem. 274, 33025-33034. [DOI] [PubMed] [Google Scholar]
[9]Schilke B., Voisine, C., Beinert, H. & Craig, E. (1999) Proc. Natl. Acad. Sci. USA 96, 10206-10211. [DOI] [PMC free article] [PubMed] [Google Scholar]
[10]Lange H., Kaut, A., Kispal, G. & Lill, R. (2000) Proc. Natl. Acad. Sci. USA 97, 1050-1055. [DOI] [PMC free article] [PubMed] [Google Scholar]
[11]Li J., Saxena, S., Pain, D. & Dancis, A. (2001) J. Biol. Chem. 276, 1503-1509. [DOI] [PubMed] [Google Scholar]
[12]Amberg D. C., Botstein, D. & Beasley, E. M. (1995) Yeast 11, 1275-1280. [DOI] [PubMed] [Google Scholar]
[13]Narahari J., Ma, R., Wang, M. & Walden, W. E. (2000) J. Biol. Chem. 275, 16227-16234. [DOI] [PubMed] [Google Scholar]
[14]Dohrmann P. R., Butler, G., Tamai, K., Dorland, S., Greene, J. R., Thiele, D. J. & Stillman, D. J. (1992) Genes Dev. 6, 93-104. [DOI] [PubMed] [Google Scholar]
[15]Brown N. M., Anderson, S. A., Steffen, D. W., Carpenter, T. B., Kennedy, M. C., Walden, W. E. & Eisenstein, R. S. (1998) Proc. Natl. Acad. Sci. USA 95, 15235-15240. [DOI] [PMC free article] [PubMed] [Google Scholar]
[16]Daum G., Bohni, P. C. & Schatz, G. (1982) J. Biol. Chem. 257, 13028-13033. [PubMed] [Google Scholar]
[17]Chen O. S., Schalinske, K. L. & Eisenstein, R. S. (1997) J. Nutr. 127, 238-248. [DOI] [PubMed] [Google Scholar]
[18]Englard S. & Siegel, L. (1969) Methods Enzymol. 13, 99-106. [Google Scholar]
[19]Munujos P., Coll-Canti, J., Gonzalez-Sastre, F. & Gella, F. J. (1993) Anal. Biochem. 212, 506-509. [DOI] [PubMed] [Google Scholar]
[20]Yamaguchi-Iwai Y., Ueta, R., Fukunaka, A. & Sasaki, R. (2002) J. Biol. Chem. 277, 18914-18918. [DOI] [PubMed] [Google Scholar]
[21]Chen O. S. & Kaplan, J. (2001) FEBS Lett. 509, 131-134. [DOI] [PubMed] [Google Scholar]
[22]Rotig A., de Lonlay, P., Chretien, D., Foury, F., Koenig, M., Sidi, D., Munnich, A. & Rustin, P. (1997) Nat. Genet. 17, 215-217. [DOI] [PubMed] [Google Scholar]
[23]Cabiscol E., Piulats, E., Echave, P., Herrero, E. & Ros, J. (2000) J. Biol. Chem. 275, 27393-27398. [DOI] [PubMed] [Google Scholar]
[24]Wilson R. B. & Roof, D. M. (1997) Nat. Genet. 16, 352-357. [DOI] [PubMed] [Google Scholar]
[25]Li L., Chen, O. S., Ward, D. M. & Kaplan, J. (2001) J. Biol. Chem. 276, 29515-29519. [DOI] [PubMed] [Google Scholar]
[26]Lapinskas P. J., Cunningham, K. W., Liu, X. F., Fink, G. R. & Culotta, V. C. (1995) Mol. Cell. Biol. 15, 1382-1388. [DOI] [PMC free article] [PubMed] [Google Scholar]
[27]Tong W. H. & Rouault, T. (2000) EMBO J. 19, 5692-5700. [DOI] [PMC free article] [PubMed] [Google Scholar]
[28]Lutz T., Westermann, B., Neupert, W. & Herrmann, J. M. (2001) J. Mol. Biol. 307, 815-825. [DOI] [PubMed] [Google Scholar]
[29]Adamec J., Rusnak, F., Owen, W. G., Naylor, S., Benson, L. M., Gacy, A. M. & Isaya, G. (2000) Am. J. Hum. Genet. 67, 549-562. [DOI] [PMC free article] [PubMed] [Google Scholar]
[30]Muhlenhoff U., Richhardt, N., Ristow, M., Kispal, G. & Lill, R. (2002) Hum. Mol. Genet. 11, 2025-2036. [DOI] [PubMed] [Google Scholar]

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Frataxin interacts functionally with mitochondrial electron transport chain proteins
González-Cabo, P., Vázquez-Manrique, R. P., García-Gimeno, M. A., Sanz, P., & Palau, F. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi214 · Cited by 140 · see citing works
Idebenone delays the onset of cardiac functional alteration without correction of Fe-S enzymes deficit in a mouse model for Friedreich ataxia
Seznec, H. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh114 · Cited by 138 · see citing works
Biochemical Characterization of Yeast Mitochondrial Grx5 Monothiol Glutaredoxin
Tamarit, J., Bellı́, G., Cabiscol, E., Herrero, E., & Ros, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303477200 · Cited by 129 · see citing works
The roles of glutaredoxins ligating Fe–S clusters: Sensing, transfer or repair functions?
Couturier, J., Przybyla‐Toscano, J., Roret, T., Claude Didierjean, B., & Rouhier, N. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.09.018 · Cited by 122 · see citing works
The MCK mouse heart model of Friedreich's ataxia: Alterations in iron-regulated proteins and cardiac hypertrophy are limited by iron chelation
Whitnall, M., Rahmanto, Y. S., Šuťák, R., Xu, X., Becker, E., Mikhael, M., Ponka, P., & Richardson, D. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804261105 · Cited by 122 · see citing works
In vivo maturation of human frataxin
Condò, I., Ventura, N., Malisan, F., Rufini, A., Tomassini, B., & Testi, R. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm102 · Cited by 118 · see citing works
The Yeast Scaffold Proteins Isu1p and Isu2p Are Required inside Mitochondria for Maturation of Cytosolic Fe/S Proteins
Gerber, J., Neumann, K., Prohl, C., Mühlenhoff, U., & Lill, R. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.11.4848-4857.2004 · Cited by 115 · see citing works
Deficiency of Arabidopsis thaliana frataxin alters activity of mitochondrial Fe–S proteins and induces oxidative stress
Busi, M. V., Maliandi, M. V., Valdez, H., Clemente, M., Zabaleta, E. J., Araya, A., & Gomez‐Casati, D. F. (2006) · The Plant Journal · doi:10.1111/j.1365-313x.2006.02923.x · Cited by 115 · see citing works
Cellular and mitochondrial remodeling upon defects in iron-sulfur protein biogenesis
Hausmann, A., Samans, B., Lill, R., & Mühlenhoff, U. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m705570200 · Cited by 111 · see citing works
How Escherichia coli and Saccharomyces cerevisiae Build Fe/S Proteins
Barras, F., Loiseau, L., & Py, B. (2005) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/s0065-2911(05)50002-x · Cited by 111 · see citing works
Frataxin and Mitochondrial Carrier Proteins, Mrs3p and Mrs4p, Cooperate in Providing Iron for Heme Synthesis
Zhang, Y., Lyver, E. R., Knight, S. A. B., Lesuisse, E., & Dancis, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500397200 · Cited by 111 · see citing works
The expression of human mitochondrial ferritin rescues respiratory function infrataxin-deficient yeast
Campanella, A. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh232 · Cited by 109 · see citing works
Prediction of protein function and pathways in the genome era
Gabald�n, T., & Huynen, M. A. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-3387-y · Cited by 108 · see citing works
Hydrogen peroxide scavenging rescues frataxin deficiency in a <i>Drosophila</i> model of Friedreich's ataxia
Anderson, P. R., Kirby, K., Orr, W. C., Hilliker, A. J., & Phillips, J. P. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709691105 · Cited by 105 · see citing works
Mitochondrial iron metabolism and its role in diseases
Gao, J., Zhou, Q., Wu, D., & Chen, L. (2020) · Clinica Chimica Acta · doi:10.1016/j.cca.2020.12.005 · Cited by 103 · see citing works
Metal Ion availability in mitochondria
Pierrel, F., Cobine, P. A., & Winge, D. R. (2007) · BioMetals · doi:10.1007/s10534-006-9052-9 · Cited by 105 · see citing works
Reduction in frataxin causes progressive accumulation of mitochondrial damage
Karthikeyan, G. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg349 · Cited by 102 · see citing works
The role of oxidative stress in Friedreich's ataxia
Lupoli, F., Vannocci, T., Longo, G., Niccolai, N., & Pastore, A. (2017) · FEBS Letters · doi:10.1002/1873-3468.12928 · Cited by 102 · see citing works
Mrs3p, Mrs4p, and Frataxin Provide Iron for Fe-S Cluster Synthesis in Mitochondria
Zhang, Y., Lyver, E. R., Knight, S. A. B., Pain, D., Lesuisse, E., & Dancis, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604246200 · Cited by 98 · see citing works
Regulation of Sulphur Assimilation Is Essential for Virulence and Affects Iron Homeostasis of the Human-Pathogenic Mould Aspergillus fumigatus
Amich, J., Schafferer, L., Haas, H., & Krappmann, S. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003573 · Cited by 91 · see citing works
Deferiprone for the treatment of Friedreich's ataxia
Pandolfo, M., & Hausmann, L. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12300 · Cited by 88 · see citing works
Molecular Mechanisms and Regulation of Iron Transport
Chung, J., & Wessling‐Resnick, M. (2003) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/713609332 · Cited by 85 · see citing works
Inhibition of Heme Biosynthesis Prevents Transcription of Iron Uptake Genes in Yeast
Crisp, R., Pollington, A. M., Galea, C. A., Jaron, S., Yamaguchi‐Iwai, Y., & Kaplan, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307229200 · Cited by 83 · see citing works
Self-citation
Mechanisms of iron sensing and regulation in the yeast Saccharomyces cerevisiae
Martínez‐Pastor, M. T., Perea‐García, A., & Puig, S. (2017) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-017-2215-8 · Cited by 81 · see citing works
Frataxin deficiency causes upregulation of mitochondrial Lon and ClpP proteases and severe loss of mitochondrial Fe–S proteins
Guillon, B., Bulteau, A., Wattenhofer‐Donzé, M., Schmucker, S., Friguet, B., Puccio, H. M., Drapier, J., & Bouton, C. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06847.x · Cited by 76 · see citing works
Drosophila Frataxin: An Iron Chaperone during Cellular Fe−S Cluster Bioassembly
Kondapalli, K. C., Kok, N. M., Dancis, A., & Stemmler, T. L. (2008) · Biochemistry · doi:10.1021/bi800366d · Cited by 70 · see citing works
CoA‐dependent activation of mitochondrial acyl carrier protein links four neurodegenerative diseases
Lambrechts, R. A., Schepers, H., Yu, Y., van der Zwaag, M., Autio, K. J., Vieira‐Lara, M. A., Bakker, B. M., Tijssen, M. A. J., Hayflick, S. J., Grzeschik, N. A., et al. (2019) · EMBO Molecular Medicine · doi:10.15252/emmm.201910488 · Cited by 67 · see citing works
Iron homeostasis: new players, newer insights
Edison, E. S., Bajel, A. R., & Chandy, M. (2008) · European Journal Of Haematology · doi:10.1111/j.1600-0609.2008.01143.x · Cited by 67 · see citing works
Iron Metabolism and Mitochondrial Abnormalities in Friedreich Ataxia
Pandolfo, M. (2002) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2002.0591 · Cited by 65 · see citing works
Functional and molecular characterization of the frataxin homolog from Arabidopsis thaliana,
Busi, M. V., Zabaleta, E. J., Araya, A., & Gomez‐Casati, D. F. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.09.003 · Cited by 64 · see citing works
EPR and Mössbauer Spectroscopy of Intact Mitochondria Isolated from Yah1p-DepletedSaccharomyces cerevisiae
Miao, R., Martinho, M., Morales, J. G., Kim, H., Ellis, E. A., Lill, R., Hendrich, M. P., Münck, E., & Lindahl, P. A. (2008) · Biochemistry · doi:10.1021/bi801047q · Cited by 61 · see citing works
Saccharomyces cerevisiae Glutaredoxin 5-deficient Cells Subjected to Continuous Oxidizing Conditions Are Affected in the Expression of Specific Sets of Genes
Bellı́, G., Molina‐Navarro, M. M., García‐Martínez, J., Pérez-Ortín, J. E., & Herrero, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311879200 · Cited by 61 · see citing works
A Role for Iron-Sulfur Clusters in the Regulation of Transcription Factor Yap5-dependent High Iron Transcriptional Responses in Yeast
Li, L., Miao, R., Bertram, S., Jia, X., Ward, D. M., & Kaplan, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.395533 · Cited by 60 · see citing works
Self-citation
Knockout of frataxin gene causes embryo lethality in Arabidopsis
Vazzola, V., Losa, A., Soave, C., & Murgia, I. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.01.030 · Cited by 60 · see citing works
Iron Dysregulation in Friedreich Ataxia
Wilson, R. B. (2006) · Seminars in Pediatric Neurology · doi:10.1016/j.spen.2006.08.005 · Cited by 59 · see citing works
The Cell's Cookbook For Iron–Sulfur Clusters: Recipes For Fool's Gold?
Balk, J., & Lill, R. (2004) · ChemBioChem · doi:10.1002/cbic.200400061 · Cited by 57 · see citing works
Iron Dynamics in Plants
Briat, J. (2007) · Advances in botanical research · doi:10.1016/s0065-2296(07)46004-9 · Cited by 56 · see citing works
Therapeutic Effects of Coenzyme Q10 in Neurodegenerative Diseases
Beal, M. F. (2004) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(04)82026-3 · Cited by 54 · see citing works
<i>Candida albicans</i> lacking the frataxin homologue: a relevant yeast model for studying the role of frataxin
Santos, R., Buisson, N., Knight, S. A. B., Dancis, A., Camadro, J., & Lesuisse, E. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04281.x · Cited by 55 · see citing works
Fixing frataxin: ‘ironing out’ the metabolic defect in Friedreich's ataxia
Anzovino, A., Lane, D., Huang, L.-H. M., & Richardson, D. R. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12470 · Cited by 54 · see citing works
Evolution and cellular function of monothiol glutaredoxins: involvement in iron–sulphur cluster assembly
Vilella, F., Alves, R., Rodríguez‐Manzaneque, M. T., Bellí, G., Swaminathan, S., Sunnerhagen, P., & Herrero, E. (2004) · Comparative and Functional Genomics · doi:10.1002/cfg.406 · Cited by 54 · see citing works
Deconstructing the genetic architecture of iron deficiency chlorosis in soybean using genome-wide approaches
Assefa, T., Zhang, J., Chowda-Reddy, R. V., Lauter, A. N. M., Singh, A., O’Rourke, J. A., Graham, M. A., & Singh, A. K. (2020) · BMC Plant Biology · doi:10.1186/s12870-020-2237-5 · Cited by 55 · see citing works
Genetic analysis of iron citrate toxicity in yeast: Implications for mammalian iron homeostasis
Chen, O. S., Hemenway, S., & Kaplan, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.232392299 · Cited by 49 · see citing works
Self-citation
The metabolic growth limitations of petite cells lacking the mitochondrial genome
Vowinckel, J., Hartl, J., Marx, H., Kerick, M., Runggatscher, K., Keller, M. A., Mülleder, M., Day, J., Weber, M., Rinnerthaler, M., et al. (2021) · Nature Metabolism · doi:10.1038/s42255-021-00477-6 · Cited by 48 · see citing works
Human BAC-mediated rescue of the Friedreich ataxia knockout mutation in transgenic mice
Sarsero, J. P., Li, L., Holloway, T. P., Voullaire, L. E., Gazeas, S., Fowler, K. J., Kirby, D. M., Thorburn, D. R., Galle, A., Cheema, S. S., et al. (2004) · Mammalian Genome · doi:10.1007/s00335-004-3019-3 · Cited by 48 · see citing works
The mitochondrial protein frataxin is essential for heme biosynthesis in plants
Maliandi, M. V., Busi, M. V., Turowski, V. R., Leaden, L., Araya, A., & Gomez‐Casati, D. F. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07968.x · Cited by 47 · see citing works
Autosomal recessive cerebellar ataxias: the current state of affairs
Vermeer, S., van de Warrenburg, B. P. C., Willemsen, M. A. A. P., Cluitmans, M., Scheffer, H., Kremer, B. P. H., & Knoers, N. V. A. M. (2011) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2011-100210 · Cited by 46 · see citing works
Exploring frataxin function
Busi, M. V., & Gomez‐Casati, D. F. (2011) · IUBMB Life · doi:10.1002/iub.577 · Cited by 46 · see citing works
Conserved electron donor complex Dre2–Tah18 is required for ribonucleotide reductase metallocofactor assembly and DNA synthesis
Zhang, Y., Li, H., Zhang, C., An, X., Liu, L., Stubbe, J., & Huang, M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405204111 · Cited by 44 · see citing works
Frataxin interacts with Isu1 through a conserved tryptophan in its β-sheet
Leidgens, S., Smet, S. D., & Foury, F. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp495 · Cited by 44 · see citing works
The power of yeast to model diseases of the powerhouse of the cell
Claypool, S. M. (2012) · Frontiers in bioscience · doi:10.2741/4098 · Cited by 42 · see citing works
Frataxin Depletion in Yeast Triggers Up-regulation of Iron Transport Systems before Affecting Iron-Sulfur Enzyme Activities
Moreno-Cermeño, A., Òbis, È., Bellı́, G., Cabiscol, E., Ros, J., & Tamarit, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.149443 · Cited by 43 · see citing works
Assembly of the Iron-binding Protein Frataxin in Saccharomyces cerevisiae Responds to Dynamic Changes in Mitochondrial Iron Influx and Stress Level
Gakh, O., Smith, D. Y., & Isaya, G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805415200 · Cited by 38 · see citing works
Functional studies of frataxin
Isaya, G., O'Neill, H., Gakh, O., Park, S., Mantcheva, R., & Mooney, S. (2004) · Acta Paediatrica · doi:10.1111/j.1651-2227.2004.tb03061.x · Cited by 37 · see citing works
Genomic characterization of POS5, the Saccharomyces cerevisiae mitochondrial NADH kinase
Shianna, K. V., Marchuk, D. A., & Strand, M. K. (2006) · Mitochondrion · doi:10.1016/j.mito.2006.02.003 · Cited by 35 · see citing works
Frataxin Is Localized to Both the Chloroplast and Mitochondrion and Is Involved in Chloroplast Fe-S Protein Function in Arabidopsis
Turowski, V. R., Aknin, C., Maliandi, M. V., Buchensky, C., Leaden, L., Peralta, D. A., Busi, M. V., Araya, A., & Gomez‐Casati, D. F. (2015) · PLoS ONE · doi:10.1371/journal.pone.0141443 · Cited by 33 · see citing works
Frataxin Structure and Function
Castro, I. H., Pignataro, M. F., Sewell, K. E., Espeche, L. D., Herrera, M. G., Noguera, M. E., Daín, L., Nadra, A. D., Arán, M., Smal, C., et al. (2019) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-28151-9_13 · Cited by 33 · see citing works
Altered sterol metabolism in budding yeast affects mitochondrial iron-sulfur (Fe-S) cluster synthesis
Ward, D. M., Chen, O. S., Li, L., Kaplan, J., Bhuiyan, S. A., Natarajan, S. K., Bard, M., & Cox, J. E. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.001781 · Cited by 32 · see citing works
Self-citation
Expression of the human ferritin light chain in a frataxin mutant yeast affects ageing and cell death
Desmyter, L., Dewaele, S., Reekmans, R., Nystrom, T., Contreras, R., & Chen, C. (2004) · Experimental Gerontology · doi:10.1016/j.exger.2004.01.008 · Cited by 31 · see citing works
Hypoxia rescues early mortality conferred by superoxide dismutase deficiency
Wicks, S. E., Bain, N. T., Duttaroy, A., Hilliker, A. J., & Phillips, J. P. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.09.036 · Cited by 31 · see citing works
Zinc suppresses the iron-accumulation phenotype of Saccharomyces cerevisiae lacking the yeast frataxin homologue (Yfh1)
Santos, R., Dancis, A., Eide, D. J., Camadro, J., & Lesuisse, E. (2003) · Biochemical Journal · doi:10.1042/bj20030835 · Cited by 30 · see citing works
A copper-doped mesoporous nanoplatform with dual enzyme-mimic activities for amplified cuproptosis and immune response
Xu, Q., Feng, S., Cao, Y., Yang, L., Liu, Z., Deng, Q., Lan, J., Di, D., Mao, Y., Wang, S., et al. (2025) · Chemical Engineering Journal · doi:10.1016/j.cej.2025.164753 · Cited by 29 · see citing works
Mitochondrial Iron-Sulfur Cluster Activity and Cytosolic Iron Regulate Iron Traffic in Saccharomyces cerevisiae
Wofford, J. D., & Lindahl, P. A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.676668 · Cited by 27 · see citing works
Friedreich ataxia
Pandolfo, M. (2011) · Handbook of clinical neurology · doi:10.1016/b978-0-444-51892-7.00017-6 · Cited by 26 · see citing works
Role of sulfate in detoxification of arsenate-induced toxicity inZea maysL. (SRHM 445): nutrient status and antioxidants
Mallick, S., Kumar, N., Singh, A. P., Sinam, G., Yadav, R. N., & Sinha, S. (2012) · Journal of Plant Interactions · doi:10.1080/17429145.2012.734863 · Cited by 26 · see citing works
Friedreich Ataxia
Pandolfo, M. (2012) · Journal of Child Neurology · doi:10.1177/0883073812448534 · Cited by 26 · see citing works

Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain
Foury, F. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00961-8 · Cited by 145 · see citing works
A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins
Lange, H., Kaut, A., Kispál, G., & Lill, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.3.1050 · Cited by 272 · see citing works
Cloning and characterization of Saccharomyces cerevisiae Nfs1p: An essential mitochondrial protein required for iron-sulfur cluster assembly and for cellular and mitochondrial iron homeostasis
Li, J. (2000) · Scholarly Commons (University of Pennsylvania)
During FeS cluster biogenesis, ferredoxin and frataxin use overlapping binding sites on yeast cysteine desulfurase Nfs1
Uzarska, M. A., Grochowina, I., Soldek, J., Jelen, M., Schilke, B. A., Marszałek, J., Craig, E. A., & Dutkiewicz, R. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101570 · Cited by 18 · see citing works
Salutary Effects of Overexpression of Rsm22, an Assembly Factor for the Mitochondrial Ribosome, on Frataxin/Yfh1 Depletion Phenotypes in Saccharomyces cerevisiae
Pandey, A. K., Singh, P., Pain, J., Dancis, A., & Pain, D. (2025) · Biomolecules · doi:10.3390/biom15060785 · Cited by 2 · see citing works

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
DOI: 10.1073/pnas.192449599
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: 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
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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Inhibition of Fe-S cluster biosynthesis decreases mitochondrial iron export: Evidence that Yfh1p affects Fe-S cluster synthesis

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