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Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis.
Abstract
Iron is required to produce haem and iron-sulphur (Fe-S) clusters, processes thought to occur independently. Here we show that the hypochromic anaemia in shiraz (sir) zebrafish mutants is caused by deficiency of glutaredoxin 5 (grx5), a gene required in yeast for Fe-S cluster assembly. We found that grx5 was expressed in erythroid cells of zebrafish and mice. Zebrafish grx5 rescued the assembly of grx5 yeast Fe-S, showing that the biochemical function of grx5 is evolutionarily conserved. In contrast to yeast, vertebrates use iron regulatory protein 1 (IRP1) to sense intracellular iron and regulate mRNA stability or the translation of iron metabolism genes. We found that loss of Fe-S cluster assembly in sir animals activated IRP1 and blocked haem biosynthesis catalysed by aminolaevulinate synthase 2 (ALAS2). Overexpression of ALAS2 RNA without the 5' iron response element that binds IRP1 rescued sir embryos, whereas overexpression of ALAS2 including the iron response element did not. Further, antisense knockdown of IRP1 restored sir embryo haemoglobin synthesis. These findings uncover a connection between haem biosynthesis and Fe-S clusters, indicating that haemoglobin production in the differentiating red cell is regulated through Fe-S cluster assembly.
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“Perhaps less surprising, the clinical phenotype of a unique patient carrying a GLRX5 mutation also differs somewhat from an earlier animal model with a deletion of that gene, the shiraz zebrafish.177”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [177]
Citations
Cites
Iron-sulfur clusters: nature's modular, multipurpose structures
Beinert, H., Holm, R. H., & Münck, E. (1997) · Science · doi:10.1126/science.277.5326.653 · Cited by 1,944
Hentze, M. W., Muckenthaler, M. U., & Andrews, N. C. (2004) · Cell · doi:10.1016/s0092-8674(04)00343-5 · Cited by 1,736
Mootha, V. K., Bunkenborg, J., Olsen, J. V., Hjerrild, M., Wisniewski, J. R., Stahl, E., Bolouri, M. S., Ray, H. N., Sihag, S., Kamal, M., et al. (2003) · Cell · doi:10.1016/s0092-8674(03)00926-7 · Cited by 889
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
Fernandes, A. P., & Holmgren, A. (2004) · Antioxidants and Redox Signaling · doi:10.1089/152308604771978354 · Cited by 670
Grx5 Is a Mitochondrial Glutaredoxin Required for the Activity of Iron/Sulfur Enzymes
Rodrı́guez-Manzaneque, M. T., Tamarit, J., Bellı́, G., Ros, J., & Herrero, E. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-10-0517 · Cited by 464
Allikmets, R. L., Raskind, W. H., Hutchinson, A. A., Schueck, N. D., Dean, M. C., & Koeller, D. M. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.5.743 · Cited by 400
Mühlenhoff, U., Gerber, J., Richhardt, N., & Lill, R. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg446 · Cited by 383
Maturation of cellular Fe–S proteins: an essential function of mitochondria
Lill, R., & Kispal, G. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01589-9 · Cited by 358
Dernbach, E., Urbich, C., Brandes, R. P., Hofmann, W. K., Zeiher, A. M., & Dimmeler, S. (2004) · Blood · doi:10.1182/blood-2003-12-4103 · Cited by 331
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Long, S., Changmai, P., Tsaousis, A. D., Skalický, T., Verner, Z., Wen, Y., Roger, A. J., & Lukeš, J. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07769.x · Cited by 39
Seguin, A., Takahashi‐Makise, N., Yien, Y. Y., Huston, N. C., Whitman, J. C., Musso, G. A., Wallace, J. A., Bradley, T., Bergonia, H. A., Kafina, M. D., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.797415 · Cited by 39
Iron–Sulphur Clusters, Their Biosynthesis, and Biological Functions in Protozoan Parasites
Ali, V., & Nozaki, T. (2013) · Advances in Parasitology/Advances in parasitology · doi:10.1016/b978-0-12-407705-8.00001-x · Cited by 41
Proteomic analysis of Intercept-treated platelets
Prudent, M., Crettaz, D., Delobel, J., Tissot, J., & Lion, N. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.07.008 · Cited by 39
Mitochondrial Hspa9/Mortalin regulates erythroid differentiation via iron-sulfur cluster assembly
Shan, Y., & Cortopassi, G. A. (2015) · Mitochondrion · doi:10.1016/j.mito.2015.12.005 · Cited by 39
Johnson, N. B., Deck, K. M., Nizzi, C. P., & Eisenstein, R. S. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.785741 · Cited by 38
montalcino, A zebrafish model for variegate porphyria
Dooley, K. A., Fraenkel, P. G., Langer, N. B., Schmid, B., Davidson, A. J., Weber, G., Chiang, K., Foott, H., Dwyer, C. E., Wingert, R. A., et al. (2008) · Experimental Hematology · doi:10.1016/j.exphem.2008.04.008 · Cited by 38
The chemical form of mitochondrial iron in Friedreich’s ataxia
Popescu, B. F. G., Pickering, I. J., George, G. N., & Nichol, H. (2007) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2007.03.004 · Cited by 36
Valerio, L. G. (2007) · Toxicology Mechanisms and Methods · doi:10.1080/15376510701556690 · Cited by 38
Glutaredoxins with iron-sulphur clusters in eukaryotes - Structure, function and impact on disease
Berndt, C., Christ, L., Rouhier, N., & Mühlenhoff, U. (2020) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2020.148317 · Cited by 37
Herrero, E., Ros, J., Tamarit, J., & Bellı́, G. (2006) · Photosynthesis Research · doi:10.1007/s11120-006-9079-3 · Cited by 37
Nordin, A., Larsson, E., & Holmberg, M. (2011) · Human Mutation · doi:10.1002/humu.22002 · Cited by 36
Yadav, S., Kushwaha, H. R., Kumar, K., & Verma, P. K. (2012) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2012.05.014 · Cited by 35
Mammalian Fe–S proteins: definition of a consensus motif recognized by the co-chaperone HSC20
Maio, N., & Rouault, T. A. (2016) · Metallomics · doi:10.1039/c6mt00167j · Cited by 36
Zanello, P. (2014) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2014.08.003 · Cited by 35
Metabolic regulation of erythrocyte development and disorders
Lyu, J., Ni, M., Weiss, M. J., & Xu, J. (2024) · Experimental Hematology · doi:10.1016/j.exphem.2024.104153 · Cited by 36
Mutations in the iron-sulfur cluster biogenesis protein HSCB cause congenital sideroblastic anemia
Crispin, A., Guo, C., Chen, C., Campagna, D. R., Schmidt, P. J., Lichtenstein, D. A., Cao, C. Q., Sendamarai, A. K., Hildick-Smith, G. J., Huston, N. C., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci135479 · Cited by 32
González‐Cabo, P., Bolinches-Amorós, A., Cabello, J., Ros, S., Moreno, S., Baylis, H. A., Palau, F., & Vázquez‐Manrique, R. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.211201 · Cited by 31
Daher, R., Mansouri, A., Martelli, A., Bayart, S., Manceau, H., Callebaut, I., Moulouel, B., Gouya, L., Puy, H., Kannengiesser, C., et al. (2019) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2018.12.012 · Cited by 31
IRP1-independent alterations of cardiac iron metabolism in doxorubicin-treated mice
Corna, G., Galy, B., Hentze, M. W., & Cairo, G. (2006) · Journal of Molecular Medicine · doi:10.1007/s00109-006-0068-y · Cited by 32
Pharmacological Silencing of MicroRNA-152 Prevents Pressure Overload–Induced Heart Failure
LaRocca, T. J., Seeger, T., Prado, M., Perea‐Gil, I., Neofytou, E. A., Mecham, B. H., Ameen, M., Chang, A. C. Y., Pandey, G. S., Wu, J. C., et al. (2020) · Circulation Heart Failure · doi:10.1161/circheartfailure.119.006298 · Cited by 31
Zhang, F., Shen, G., Liu, X., Wang, F., Zhao, H.-L., Yu, J., & Zhang, J. (2011) · Biochemistry · doi:10.1021/bi101585c · Cited by 28
Fidai, I., Wachnowsky, C., & Cowan, J. A. (2016) · Metallomics · doi:10.1039/c6mt00193a · Cited by 29
Marra, A. N., Cheng, C. N., Adeeb, B., Addiego, A., Wesselman, H. M., Chambers, B. E., Chambers, J. M., & Wingert, R. A. (2019) · Scientific Reports · doi:10.1038/s41598-019-42943-y · Cited by 30
The zebrafish as a tool in leukemia research
Teittinen, K. J., Grönroos, T., Parikka, M., Rämet, M., & Lohi, O. (2012) · Leukemia Research · doi:10.1016/j.leukres.2012.06.001 · Cited by 30
Hematopoietic stem cells, hematopoiesis and disease: lessons from the zebrafish model
Martin, C. S., Moriyama, A., & Zon, L. I. (2011) · Genome Medicine · doi:10.1186/gm299 · Cited by 29
Self-citationMammalian iron sulfur cluster biogenesis and human diseases
Maio, N., & Rouault, T. A. (2022) · IUBMB Life · doi:10.1002/iub.2597 · Cited by 28
Bolstad, H. M., Botelho, D., & Wood, M. J. A. (2010) · Journal of Proteome Research · doi:10.1021/pr1006087 · Cited by 28
Conservation in the Iron Responsive Element Family
Volz, K. W. (2021) · Genes · doi:10.3390/genes12091365 · Cited by 26
Iron Metabolism in the Disorders of Heme Biosynthesis
Ricci, A., Betto, G. D., Bergamini, E., Buzzetti, E., Corradini, E., & Ventura, P. (2022) · Metabolites · doi:10.3390/metabo12090819 · Cited by 30
Iron and erythropoiesis: a dual relationship
Camaschella, C., & Pagani, A. (2010) · International Journal of Hematology · doi:10.1007/s12185-010-0743-1 · Cited by 27
Sood, R. B., & Liu, P. (2012) · Advances in Hematology · doi:10.1155/2012/830703 · Cited by 26
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Rey, P., Taupin-Broggini, M., Couturier, J., Vignols, F., & Rouhier, N. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2019.00712 · Cited by 26
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Gibert, Y., Lattanzi, V. J., Zhen, A. W., Vedder, L. M., Brunet, F., Faasse, S. A., Babitt, J. L., Lin, H. Y.-F., Hammerschmidt, M., & Fraenkel, P. G. (2011) · PLoS ONE · doi:10.1371/journal.pone.0014553 · Cited by 29
Biani, F. F. D., & Zanello, P. (2016) · Inorganica Chimica Acta · doi:10.1016/j.ica.2016.09.028 · Cited by 27
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Mallikarjun, V., Sriram, A., Scialò, F., & Sanz, A. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2013.12.015 · Cited by 25
Zhang, Z., Jia, H., Zhang, Q., Wan, Y., Zhou, Y., Jia, Q., Zhang, W., Yuan, W., Cheng, T., Zhu, X., et al. (2013) · BMC Genomics · doi:10.1186/1471-2164-14-896 · Cited by 25
Zebrafish as a model system to delineate the role of heme and iron metabolism during erythropoiesis
Zhang, J., & Hamza, I. (2018) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2018.12.007 · Cited by 25
Methionine sulphoxide reductases protect iron–sulphur clusters from oxidative inactivation in yeast
Sideri, T. C., Willetts, S. A., & Avery, S. V. (2009) · Microbiology · doi:10.1099/mic.0.022665-0 · Cited by 24
Dycke, C., Bougault, C., Gaillard, J., Andrieu, J., Pantopoulos, K., & Moulis, J. (2007) · Biochemical Journal · doi:10.1042/bj20070983 · Cited by 25
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Chiabrando, D., Bertino, F., & Tolosano, E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113760 · Cited by 23
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Azam, T., Przybyla‐Toscano, J., Vignols, F., Couturier, J., Rouhier, N., & Johnson, M. K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239237 · Cited by 23
Kim, S., Jung, H., & Lim, C. (2013) · Biochemical Genetics · doi:10.1007/s10528-013-9616-7 · Cited by 24
Does any drug to treat cancer target mTOR and iron hemostasis in neurodegenerative disorders?
Farshbaf, M. J., & Ghaedi, K. (2016) · BioMetals · doi:10.1007/s10534-016-9981-x · Cited by 22
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Phillips, J. D., & Kushner, J. P. (2005) · Nature Medicine · doi:10.1038/nm1005-1049 · Cited by 22
Maio, N., & Rouault, T. A. (2022) · IUBMB Life · doi:10.1002/iub.2593 · Cited by 21
Sen, S., & Cowan, J. A. (2017) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-017-1485-9 · Cited by 21
Miyahara, S., Ohuchi, M., Nomura, M., Hashimoto, E., Soga, T., Saito, R., Hayashi, K., Sato, T., Saito, M., Yamashita, Y., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107678 · Cited by 19
Bilan, D. S., Shokhina, A. G., Lukyanov, S., & Belousov, V. V. (2015) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162015040044 · Cited by 32
Congenital sideroblastic anemia: Advances in gene mutations and pathophysiology
Long, Z., Li, H., Du, Y., & Han, B. (2018) · Gene · doi:10.1016/j.gene.2018.05.074 · Cited by 19
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Duarte, T. L., Viveiros, N., Godinho, C., & Duarte, D. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2024.1436897 · Cited by 18
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Bury, N. R., Boyle, D., & Cooper, C. A. (2011) · Fish physiology · doi:10.1016/s1546-5098(11)31004-7 · Cited by 19
Zhang, S., Shen, Z., Liu, X., Li, Z., Zhang, Q.-W., & Liu, X. (2016) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2016.06.007 · Cited by 17
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Herrero, E. (2005) · Revista Iberoamericana de Micología · doi:10.1016/s1130-1406(05)70046-2 · Cited by 16
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Deponte, M. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-90219-9.00017-0 · Cited by 17
Zhao, T., & Zhang-Akiyama, Q.-M. (2020) · Free Radical Research · doi:10.1080/10715762.2020.1819994 · Cited by 16
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Cairo, G., Recalcati, S., & Gammella, E. (2015) · Hypoxia · doi:10.2147/hp.s83537 · Cited by 17
Mutation analysis of Chinese sporadic congenital sideroblastic anemia by targeted capture sequencing
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Petry, S. F., Sun, L. M., Knapp, A., Reinl, S., & Linn, T. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00084 · Cited by 13
Muckenthaler, M. U., & Lill, R. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_2 · Cited by 13
Roux, S. L., Devys, A., Girard, C., Harb, J., & Hourmant, M. (2010) · Transplantation Proceedings · doi:10.1016/j.transproceed.2010.09.006 · Cited by 13
Cai, K., & Markley, J. L. (2018) · Molecules · doi:10.3390/molecules23092213 · Cited by 15
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Song, X., Xu, Y., Ying, Z., Wu, K., Liu, J., & Liu, Q. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.03091-22 · Cited by 10
Mardini, L., Gasiorek, J. J., Derjuga, A., Carrière, L., Schranzhofer, M., Paw, B. H., Ponka, P., & Blank, V. (2010) · Biochemical Journal · doi:10.1042/bj20100541 · Cited by 10
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Kim, S.-J., Jung, H.-J., Choi, H., & Lim, C. (2011) · Molecular Biology Reports · doi:10.1007/s11033-011-1152-0 · Cited by 9
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Erber, L. N., Liu, S. X., Gong, Y., Tran, P., & Chen, Y. (2022) · Molecules · doi:10.3390/molecules27020484 · Cited by 8
Dufay, J. N., Fernández-Murray, J. P., & McMaster, C. R. (2017) · G3 Genes Genomes Genetics · doi:10.1534/g3.117.041194 · Cited by 8
Messens, J., Rouhier, N., & Collet, J. (2013) · Springer eBooks · doi:10.1007/978-94-007-5787-5_3 · Cited by 7
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Joshi, A., Farber, K., & Scheiber, I. F. (2021) · Advances in neurotoxicology · doi:10.1016/bs.ant.2020.11.001 · Cited by 6
Fan, R., Jiang, S., Li, Y., Yang, Q., Jiang, S., Huang, J., Yang, L., Chen, X., & Zhou, F. (2022) · Frontiers in Marine Science · doi:10.3389/fmars.2022.909827 · Cited by 7
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Joshi, R. S., Moran, E. L., & Sánchez, M. (2012) · BiblioBoard Library Catalog (Open Research Library) · doi:10.5772/34987 · Cited by 6
Thioredoxins and Related Proteins
Michelet, L., Zaffagnini, M., & Lemaire, D. (2009) · Elsevier eBooks · doi:10.1016/b978-0-12-370873-1.00019-8 · Cited by 7
Heme Biosynthesis and Its Disorders
Fuller, S. J., & Wiley, J. S. (2017) · Elsevier eBooks · doi:10.1016/b978-0-323-35762-3.00038-x · Cited by 6
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Metadata
- Authors
- The Tübingen 2000 Screen Consortium, Wingert, R. A., Galloway, J. L., Barut, B., Foott, H., Fraenkel, P., Axe, J. L., Weber, G. J., Dooley, K., Davidson, A. J., Schmidt, B., Paw, B. H., Shaw, G. C., Kingsley, P., Palis, J., Schubert, H., Chen, O., Kaplan, J., & Zon, L. I.
- Affiliations
- Howard Hughes Medical Institute (US)
- Brigham and Women's Hospital (US)
- University of Rochester Medicine (US)
- University of Utah (US)
- Corresponding author
- Zon, Leonard I.
- ORCID
- Venue
- Nature
- Published
- 2005-08-18
- Volume
- 436
- Issue
- 7053
- Pages
- 1035-1039
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1992193197
- Cited by
- 370
- References
- 33
- Citations by year
- 2026: 6 · 2025: 1 · 2024: 8 · 2023: 6 · 2022: 11 · 2021: 15 · 2020: 17 · 2019: 11 · 2018: 14 · 2017: 17 · 2016: 15 · 2015: 13 · 2014: 18 · 2013: 17 · 2012: 21
- FWCI
- 16.29
- Type
- journal article
- Language
- en
- Update notices
- erratum (2005-10-06)
- Open access
- closed
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- Albert J. Ryan Foundation
- Harvard University
- National Institutes of Health
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Keywords
- heme biosynthesis, iron regulatory protein 1, erythroid cells, hypochromic anemia, iron-responsive element, hemoglobin synthesis, iron metabolism regulation
- MeSH terms
- Amino Acid Sequence, 5-Aminolevulinate Synthetase, Animals, Cloning, Molecular, Erythrocytes, Gene Expression Regulation, Heme, Homeostasis, Iron, Iron-Sulfur Proteins, Molecular Sequence Data, Oxidoreductases, Saccharomyces cerevisiae, Zebrafish, Response Elements, Iron Regulatory Protein 1, Mice, Glutaredoxins
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