M. Aldea, T. Garrido, C. Hernández-chico, M. Vicente, and S. R. Kushner, Induction of a growth-phase-dependent promoter triggers transcription of bolA, an Escherichia coli morphogene, EMBO J, vol.8, pp.3923-3931, 1989.

R. Alves, E. Vilaprinyo, A. Sorribas, and E. Herrero, Evolution based on domain combinations: the case of glutaredoxins, BMC Evol. Biol, vol.9, p.66, 2009.

R. Attarian, G. Hu, E. Sánchez-león, M. Caza, D. Croll et al., The monothiol glutaredoxin grx4 regulates iron homeostasis and virulence in Cryptococcus neoformans, mBio, vol.9, pp.2377-2395, 2018.

L. Banci, F. Camponeschi, S. Ciofi-baffoni, and R. Muzzioli, Elucidating the molecular function of human BOLA2 in GRX3-dependent anamorsin maturation pathway, J. Am. Chem. Soc, vol.137, pp.16133-16143, 2015.

L. Banci, S. Ciofi-baffoni, K. Gajda, R. Muzzioli, R. Peruzzini et al., N-terminal domains mediate, Nat. Chem. Biol, vol.11, pp.772-778, 2015.

S. Bandyopadhyay, F. Gama, M. M. Molina-navarro, J. M. Gualberto, R. Claxton et al., Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe-2S] clusters, EMBO J, vol.27, pp.1122-1133, 2008.
URL : https://hal.archives-ouvertes.fr/hal-01332174

D. P. Barupala, S. P. Dzul, P. J. Riggs-gelasco, and T. L. Stemmler, Synthesis, delivery and regulation of eukaryotic heme and Fe-S cluster cofactors, Arch. Biochem. Biophys, vol.592, pp.60-75, 2016.

S. M. Benyamina, F. Baldacci-cresp, J. Couturier, K. Chibani, J. Hopkins et al., Two Sinorhizobium meliloti glutaredoxins regulate iron metabolism and symbiotic bacteroid differentiation, Environ. Microbiol, vol.15, pp.795-810, 2013.
URL : https://hal.archives-ouvertes.fr/hal-01577790

D. G. Bernard, D. J. Netz, T. J. Lagny, A. J. Pierik, and J. Balk, Requirements of the cytosolic iron-sulfur cluster assembly pathway in Arabidopsis, Philos. Trans. R. Soc. Lond. B. Biol. Sci, vol.368, p.20120259, 2013.

S. Boutigny, A. Saini, E. E. Baidoo, N. Yeung, J. D. Keasling et al., Physical and functional interactions of a monothiol glutaredoxin and an iron sulfur cluster carrier protein with the sulfur-donating radical S-adenosyl-L-methionine enzyme MiaB, J. Biol. Chem, vol.288, pp.14200-14211, 2013.

A. Brault, T. Mourer, and S. Labbé, Molecular basis of the regulation of iron homeostasis in fission and filamentous yeasts, IUBMB Life, vol.67, pp.801-815, 2015.

S. Burschel, D. Kreuzer-decovic, F. Nuber, M. Stiller, M. Hofmann et al., Iron-sulfur cluster carrier proteins involved in the assembly of Escherichia coli NADH:ubiquinone oxidoreductase (complex I), Mol. Microbiol, vol.111, pp.31-45, 2019.

G. Butland, M. Babu, J. J. Díaz-mejía, F. Bohdana, S. Phanse et al., eSGA: E. coli synthetic genetic array analysis, Nat. Methods, vol.5, pp.789-795, 2008.

C. Camaschella, A. Campanella, L. De-falco, L. Boschetto, R. Merlini et al., The human counterpart of zebrafish shiraz shows sideroblasticlike microcytic anemia and iron overload, Blood, vol.110, pp.1353-1358, 2007.

J. M. Cameron, A. Janer, V. Levandovskiy, N. Mackay, T. A. Rouault et al., Mutations in iron-sulfur cluster scaffold genes NFU1 and BOLA3 cause a fatal deficiency of multiple respiratory chain and 2-oxoacid dehydrogenase enzymes, Am. J. Hum. Genet, vol.89, pp.486-495, 2011.

N. Cheng, J. Liu, X. Liu, Q. Wu, S. M. Thompson et al., Arabidopsis monothiol glutaredoxin, AtGRXS17, is critical for temperature-dependent postembryonic growth and development via modulating auxin response, J. Biol. Chem, vol.286, pp.20398-20406, 2011.

W. Chung, K. Kim, and J. Roe, Localization and function of three monothiol glutaredoxins in Schizosaccharomyces pombe, Biochem. Biophys. Res. Commun, vol.330, pp.604-610, 2005.

M. A. Comini, J. Rettig, N. Dirdjaja, E. Hanschmann, C. Berndt et al., Monothiol glutaredoxin-1 is an essential iron-sulfur protein in the mitochondrion of African trypanosomes, J. Biol. Chem, vol.283, pp.27785-27798, 2008.

J. Couturier, J. Jacquot, and N. Rouhier, Evolution and diversity of glutaredoxins in photosynthetic organisms, Cell. Mol. Life Sci, vol.66, pp.2539-2557, 2009.

J. Couturier, J. Przybyla-toscano, T. Roret, C. Didierjean, and N. Rouhier, The roles of glutaredoxins ligating Fe-S clusters: sensing, transfer or repair functions?, Biochim. Biophys. Acta, vol.1853, pp.1513-1527, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01521788

J. Couturier, B. Touraine, J. Briat, F. Gaymard, and N. Rouhier, The iron-sulfur cluster assembly machineries in plants: current knowledge and open questions, Front. Plant Sci, vol.4, p.259, 2013.
URL : https://hal.archives-ouvertes.fr/hal-00920681

J. Couturier, H. Wu, T. Dhalleine, H. Pégeot, D. Sudre et al., Monothiol glutaredoxin-BolA interactions: redox control of Arabidopsis thaliana BolA2 and SufE1, Mol. Plant, vol.7, pp.187-205, 2014.
URL : https://hal.archives-ouvertes.fr/hal-00936792

T. Dhalleine, N. Rouhier, and J. Couturier, Putative roles of glutaredoxinBolA holo-heterodimers in plants, Plant Signal. Behav, vol.9, p.28564, 2014.
URL : https://hal.archives-ouvertes.fr/hal-01579702

A. C. Dlouhy, J. Beaudoin, S. Labbé, and C. E. Outten, , 2017.

, Schizosaccharomyces pombe Grx4 regulates the transcriptional repressor Php4 via, vol.9, pp.1096-1105

A. C. Dlouhy, H. Li, A. Albetel, B. Zhang, D. T. Mapolelo et al., The Escherichia coli BolA protein IbaG forms a histidine-Ligated [2Fe-2S]-bridged complex with Grx4, Biochemistry, vol.55, pp.6869-6879, 2016.

E. Del-dedo, J. Gabrielli, N. Carmona, M. Ayté, J. Hidalgo et al., A cascade of iron-containing proteins governs the genetic iron starvation response to promote iron uptake and inhibit iron storage in fission yeast, PLoS Genet, vol.11, 2015.

A. G. Frey, D. J. Palenchar, J. D. Wildemann, and C. C. Philpott, A glutaredoxin · bola complex serves as an iron-sulfur cluster chaperone for the cytosolic cluster assembly machinery, J. Biol. Chem, vol.291, pp.22344-22356, 2016.

B. Guo, J. D. Phillips, Y. Yu, and E. A. Leibold, Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome, J. Biol. Chem, vol.270, pp.21645-21651, 1995.

P. Haunhorst, E. Hanschmann, L. Bräutigam, O. Stehling, B. Hoffmann et al., Crucial function of vertebrate glutaredoxin 3 (PICOT) in iron homeostasis and hemoglobin maturation, Mol. Biol. Cell, vol.24, pp.1895-1903, 2013.

S. Iñigo, A. N. Durand, A. Ritter, S. Le-gall, M. Termathe et al., Glutaredoxin GRXS17 associates with the cytosolic iron-sulfur cluster assembly pathway, Plant Physiol, vol.172, pp.858-873, 2016.

J. Jacques, A. Mercier, A. Brault, T. Mourer, and S. Labbé, Fra2 is a coregulator of Fep1 inhibition in response to iron starvation, PLoS One, vol.9, p.98959, 2014.

K. Kim, W. Chung, H. Kim, K. Lee, and J. Roe, Monothiol glutaredoxin Grx5 interacts with Fe-S scaffold proteins Isa1 and Isa2 and supports Fe-S assembly and DNA integrity in mitochondria of fission yeast, Biochem. Biophys. Res. Commun, vol.392, pp.467-472, 2010.

J. Knuesting, C. Riondet, C. Maria, I. Kruse, N. Bécuwe et al., Arabidopsis glutaredoxin S17 and its partner, the nuclear factor Y subunit C11/negative cofactor 2?, contribute to maintenance of the shoot apical meristem under long-day photoperiod, Plant Physiol, vol.167, pp.1643-1658, 2015.

A. Kumánovics, O. S. Chen, L. Li, D. Bagley, E. M. Adkins et al., Identification of FRA1 and FRA2 as genes involved in regulating the yeast iron regulon in response to decreased mitochondrial iron-sulfur cluster synthesis, J. Biol. Chem, vol.283, pp.10276-10286, 2008.

E. Lesuisse, S. A. Knight, M. Courel, R. Santos, J. Camadro et al., Genome-wide screen for genes with effects on distinct iron uptake activities in Saccharomyces cerevisiae, Genetics, vol.169, pp.107-122, 2005.
URL : https://hal.archives-ouvertes.fr/hal-00007533

H. Li, D. T. Mapolelo, N. N. Dingra, G. Keller, P. J. Riggs-gelasco et al., Histidine 103 in Fra2 is an iron-sulfur cluster ligand in the [2Fe-2S] Fra2-Grx3 complex and is required for in vivo iron signaling in yeast, J. Biol. Chem, vol.286, pp.867-876, 2011.

H. Li, D. T. Mapolelo, S. Randeniya, M. K. Johnson, and C. E. Outten, Human glutaredoxin 3 forms [2Fe-2S]-bridged complexes with human BolA2, Biochemistry, vol.51, pp.1687-1696, 2012.

H. Li and C. E. Outten, Monothiol CGFS glutaredoxins and BolAlike proteins: [2Fe-2S] binding partners in iron homeostasis, Biochemistry, vol.51, pp.4377-4389, 2012.

H. Li, M. Stümpfig, C. Zhang, X. An, J. Stubbe et al., The diferric-tyrosyl radical cluster of ribonucleotide reductase and cytosolic ironsulfur clusters have distinct and similar biogenesis requirements, J. Biol. Chem, vol.292, pp.11445-11451, 2017.

R. Lill, Function and biogenesis of iron-sulphur proteins, Nature, vol.460, pp.831-838, 2009.

D. T. Mapolelo, B. Zhang, S. Randeniya, A. Albetel, H. Li et al., Monothiol glutaredoxins and A-type proteins: partners in Fe-S cluster trafficking, Dalton Trans. Camb. Engl, pp.3107-3115, 2003.
URL : https://hal.archives-ouvertes.fr/hal-01268219

A. Melber, U. Na, A. Vashisht, B. D. Weiler, R. Lill et al., Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial clients, vol.5, p.15991, 2016.

D. Mil-homens, S. Barahona, R. N. Moreira, I. J. Silva, S. N. Pinto et al., Stress response protein bola influences fitness and promotes Salmonella enterica Serovar Typhimurium virulence, Appl. Environ. Microbiol, vol.84, pp.2850-2867, 2018.

M. M. Molina, G. Bellí, M. A. De-la-torre, M. T. Rodríguez-manzaneque, and E. Herrero, Nuclear monothiol glutaredoxins of Saccharomyces cerevisiae can function as mitochondrial glutaredoxins, J. Biol. Chem, vol.279, pp.51923-51930, 2004.

A. Moseler, I. Aller, S. Wagner, T. Nietzel, J. Przybyla-toscano et al., The mitochondrial monothiol glutaredoxin S15 is essential for iron-sulfur protein maturation in Arabidopsis thaliana, Proc. Natl. Acad. Sci. U.S.A, vol.112, pp.13735-13740, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01269453

U. Mühlenhoff, J. Gerber, N. Richhardt, and R. Lill, Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p, EMBO J, vol.22, pp.4815-4825, 2003.

U. Mühlenhoff, S. Molik, J. R. Godoy, M. A. Uzarska, N. Richter et al., Cytosolic monothiol glutaredoxins function in intracellular iron sensing and trafficking via their bound iron-sulfur cluster, Cell Metab, vol.12, pp.373-385, 2010.

V. Nasta, A. Giachetti, S. Ciofi-baffoni, and L. Banci, Structural insights into the molecular function of human, 2017.

. Bola3-grx5-complexes, Biochim. Biophys. Acta, vol.1861, pp.2119-2131

L. Ojeda, G. Keller, U. Muhlenhoff, J. C. Rutherford, R. Lill et al., Role of glutaredoxin-3 and glutaredoxin-4 in the iron regulation of the Aft1 transcriptional activator in Saccharomyces cerevisiae, J. Biol. Chem, vol.281, pp.17661-17669, 2006.

C. E. Outten, A. , and A. , Iron sensing and regulation in Saccharomyces cerevisiae: ironing out the mechanistic details, Curr. Opin. Microbiol, vol.16, pp.662-668, 2013.

C. C. Philpott, M. Ryu, A. Frey, P. , and S. , Cytosolic iron chaperones: proteins delivering iron cofactors in the cytosol of mammalian cells, J. Biol. Chem, vol.292, pp.12764-12771, 2017.

C. B. Poor, S. V. Wegner, H. Li, A. C. Dlouhy, J. P. Schuermann et al., Molecular mechanism and structure of the Saccharomyces cerevisiae iron regulator Aft2, Proc. Natl. Acad. Sci. U.S.A, vol.111, pp.4043-4048, 2014.

J. Przybyla-toscano, T. Roret, J. Couturier, and N. Rouhier, FeS Cluster Assembly: Role of Monothiol Grxs and Nfu Proteins, Encyclopedia of Inorganic and Bioinorganic Chemistry, pp.1-19, 2017.

N. Pujol-carrion, G. Belli, E. Herrero, A. Nogues, and M. A. Torre-ruiz, Glutaredoxins Grx3 and Grx4 regulate nuclear localisation of Aft1 and the oxidative stress response in Saccharomyces cerevisiae, J. Cell Sci, vol.119, pp.4554-4564, 2006.

L. Qin, M. Wang, J. Zuo, X. Feng, X. Liang et al., Cytosolic bolA plays a repressive role in the tolerance against excess iron and mv-induced oxidative stress in plants, PLoS One, vol.10, 2015.

P. Rey, N. Becuwe, S. Tourrette, and N. Rouhier, Involvement of Arabidopsis glutaredoxin S14 in the maintenance of chlorophyll content, Plant Cell Environ, vol.40, pp.2319-2332, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01686869

N. Rietzschel, A. J. Pierik, E. Bill, R. Lill, and U. Mühlenhoff, The basic leucine zipper stress response regulator Yap5 senses high-iron conditions by coordination of, Mol. Cell. Biol, vol.35, pp.370-378, 2015.

M. T. Rodríguez-manzaneque, J. Tamarit, G. Bellí, J. Ros, and E. Herrero, Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes, Mol. Biol. Cell, vol.13, pp.1109-1121, 2002.

T. Roret, P. Tsan, J. Couturier, B. Zhang, M. K. Johnson et al., Structural and spectroscopic insights into BolA-glutaredoxin complexes, J. Biol. Chem, vol.289, pp.24588-24598, 2014.
URL : https://hal.archives-ouvertes.fr/hal-01521194

T. A. Rouault and N. Maio, Biogenesis and functions of mammalian ironsulfur proteins in the regulation of iron homeostasis and pivotal metabolic pathways, J. Biol. Chem, vol.292, pp.12744-12753, 2017.

N. Rouhier, H. Unno, S. Bandyopadhyay, L. Masip, S. Kim et al., Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe-2S] cluster in poplar glutaredoxin C1, Proc. Natl. Acad. Sci. U.S.A, vol.104, pp.7379-7384, 2007.

K. Sipos, H. Lange, Z. Fekete, P. Ullmann, R. Lill et al., Maturation of cytosolic iron-sulfur proteins requires glutathione, J. Biol. Chem, vol.277, pp.26944-26949, 2002.

E. Ströher, J. Grassl, C. Carrie, R. Fenske, J. Whelan et al., Glutaredoxin S15 is involved in Fe-S cluster transfer in mitochondria influencing lipoic acid-dependent enzymes, plant growth, and arsenic tolerance in Arabidopsis, Plant Physiol, vol.170, pp.1284-1299, 2016.

B. Touraine, F. Vignols, J. Przybyla-toscano, T. Ischebeck, T. Dhalleine et al., Iron-sulfur protein NFU2 is required for branched-chain amino acid synthesis in Arabidopsis roots, J. Exp. Bot, vol.70, pp.1875-1889, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02095655

R. Ueta, N. Fujiwara, K. Iwai, and Y. Yamaguchi-iwai, Iron-induced dissociation of the Aft1p transcriptional regulator from target gene promoters is an initial event in iron-dependent gene suppression, Mol. Cell. Biol, vol.32, pp.4998-5008, 2012.

M. A. Uzarska, R. Dutkiewicz, S. Freibert, R. Lill, and U. Mühlenhoff, The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation, Mol. Biol. Cell, vol.24, pp.1830-1841, 2013.

M. A. Uzarska, V. Nasta, B. D. Weiler, F. Spantgar, S. Ciofi-baffoni et al., Mitochondrial Bol1 and Bol3 function as assembly factors for specific iron-sulfur proteins, vol.5, p.16673, 2016.

M. A. Uzarska, J. Przybyla-toscano, F. Spantgar, F. Zannini, R. Lill et al., Conserved functions of Arabidopsis mitochondrial late-acting maturation factors in the trafficking of iron-sulfur clusters, Biochim. Biophys. Acta Mol. Cell Res, vol.1865, pp.1250-1259, 2018.
URL : https://hal.archives-ouvertes.fr/hal-01893946

P. Willems, B. F. Wanschers, J. Esseling, R. Szklarczyk, U. Kudla et al., BOLA1 is an aerobic protein that prevents mitochondrial morphology changes induced by glutathione depletion, Antioxid. Redox Signal, vol.18, pp.129-138, 2013.

R. A. Wingert, J. L. Galloway, B. Barut, H. Foott, P. Fraenkel et al., Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis, Nature, vol.436, pp.1035-1039, 2005.

H. Xia, B. Li, Z. Zhang, Q. Wang, T. Qiao et al., Human glutaredoxin 3 can bind and effectively transfer, Biochem. Biophys. Res. Commun, vol.465, pp.620-624, 2015.

H. Ye, S. Y. Jeong, M. C. Ghosh, G. Kovtunovych, L. Silvestri et al., Glutaredoxin 5 deficiency causes sideroblastic anemia by specifically impairing heme biosynthesis and depleting cytosolic iron in human erythroblasts, J. Clin. Invest, vol.120, pp.1749-1761, 2010.

N. Yeung, B. Gold, N. L. Liu, R. Prathapam, H. J. Sterling et al., The E. coli monothiol glutaredoxin GrxD forms homodimeric and heterodimeric FeS cluster containing complexes, Biochemistry, vol.50, pp.8957-8969, 2011.

H. Yu, J. Yang, Y. Shi, J. Donelson, S. M. Thompson et al., Arabidopsis glutaredoxin S17 contributes to vegetative growth, mineral accumulation, and redox balance during iron deficiency, Front. Plant Sci, vol.8, p.1045, 2017.

Y. Zhang, L. Liu, X. Wu, X. An, J. Stubbe et al., Investigation of in vivo diferric tyrosyl radical formation in Saccharomyces cerevisiae Rnr2 protein: requirement of Rnr4 and contribution of Grx3/4 AND Dre2 proteins, J. Biol. Chem, vol.286, pp.41499-41509, 2011.