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Volumn 580, Issue 9, 2006, Pages 2273-2280

Prokaryotic and eukaryotic monothiol glutaredoxins are able to perform the functions of Grx5 in the biogenesis of Fe/S clusters in yeast mitochondria

Author keywords

Glutaredoxin; Glutathione; Iron sulfur cluster; Mitochondria; Redox regulation

Indexed keywords

GLUTAREDOXIN; IRON; SULFUR;

EID: 33645990964     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.03.037     Document Type: Article
Times cited : (72)

References (32)
  • 1
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: nature's modular, multipurpose structures
    • Beinert H., Holm R.H., and Münck E. Iron-sulfur clusters: nature's modular, multipurpose structures. Science 277 (1997) 653-659
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Münck, E.3
  • 2
    • 0034003112 scopus 로고    scopus 로고
    • Iron-sulfur clusters: ancient structures, still full of surprises
    • Beinert H. Iron-sulfur clusters: ancient structures, still full of surprises. J. Biol. Inorg. Chem. 5 (2000) 2-15
    • (2000) J. Biol. Inorg. Chem. , vol.5 , pp. 2-15
    • Beinert, H.1
  • 3
    • 4544321137 scopus 로고    scopus 로고
    • The cells's cookbook for iron-sulfur clusters: recipes for fool's gold
    • Balk J., and Lill R. The cells's cookbook for iron-sulfur clusters: recipes for fool's gold. ChemBioChem 5 (2004) 1044-1049
    • (2004) ChemBioChem , vol.5 , pp. 1044-1049
    • Balk, J.1    Lill, R.2
  • 4
    • 17144378216 scopus 로고    scopus 로고
    • Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis
    • Rouault T.A., and Tong W.H. Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis. Nat. Rev. Mol. Cell Biol. 6 (2005) 345-351
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 345-351
    • Rouault, T.A.1    Tong, W.H.2
  • 5
    • 14744294785 scopus 로고    scopus 로고
    • Iron-sulfur-protein biogenesis in eukaryotes
    • Lill R., and Mühlenhoff U. Iron-sulfur-protein biogenesis in eukaryotes. Trends Biochem. Sci. 30 (2005) 133-141
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 133-141
    • Lill, R.1    Mühlenhoff, U.2
  • 6
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function and formation of biological iron-sulfur clusters
    • Johnson D.C., Dean D.R., Smith A.D., and Johnson M.K. Structure, function and formation of biological iron-sulfur clusters. Annu. Rev. Biochem. 74 (2005) 247-281
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 7
    • 0141737067 scopus 로고    scopus 로고
    • Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p
    • Mühlenhoff U., Gerber J., Richhardt N., and Lill R. Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. EMBO J. 22 (2003) 4815-4825
    • (2003) EMBO J. , vol.22 , pp. 4815-4825
    • Mühlenhoff, U.1    Gerber, J.2    Richhardt, N.3    Lill, R.4
  • 8
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur clusters
    • Rodríguez-Manzaneque M.T., Tamarit J., Bellí G., Ros J., and Herrero E. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur clusters. Mol. Biol. Cell 13 (2002) 1109-1121
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1109-1121
    • Rodríguez-Manzaneque, M.T.1    Tamarit, J.2    Bellí, G.3    Ros, J.4    Herrero, E.5
  • 9
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren A. Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264 (1989) 13963-13966
    • (1989) J. Biol. Chem. , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 10
    • 0348230942 scopus 로고    scopus 로고
    • Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system
    • Fernandes A.P., and Holmgren A. Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Antiox. Red. Sign. 6 (2004) 63-74
    • (2004) Antiox. Red. Sign. , vol.6 , pp. 63-74
    • Fernandes, A.P.1    Holmgren, A.2
  • 11
    • 0036130729 scopus 로고    scopus 로고
    • Thioredoxin and glutaredoxin isoforms
    • Vlamis-Gardikas A., and Holmgren A. Thioredoxin and glutaredoxin isoforms. Methods Enzymol. 347 (2002) 286-296
    • (2002) Methods Enzymol. , vol.347 , pp. 286-296
    • Vlamis-Gardikas, A.1    Holmgren, A.2
  • 12
    • 0026799490 scopus 로고
    • Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14-S) and its mixed disulfide with glutathione
    • Bushweller J.H., Aslund F., Wüthrich K., and Holmgren A. Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14-S) and its mixed disulfide with glutathione. Biochemistry 31 (1992) 9288-9293
    • (1992) Biochemistry , vol.31 , pp. 9288-9293
    • Bushweller, J.H.1    Aslund, F.2    Wüthrich, K.3    Holmgren, A.4
  • 13
    • 0040932016 scopus 로고    scopus 로고
    • Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae
    • Rodríguez-Manzaneque M.T., Ros J., Cabiscol E., Sorribas A., and Herrero E. Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae. Mol. Cell. Biol. 19 (1999) 8180-8190
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8180-8190
    • Rodríguez-Manzaneque, M.T.1    Ros, J.2    Cabiscol, E.3    Sorribas, A.4    Herrero, E.5
  • 14
    • 1642547105 scopus 로고    scopus 로고
    • Regulation of redox homeostasis in the yeast Saccharomyces cerevisiae
    • Wheeler G.L., and Grant C.M. Regulation of redox homeostasis in the yeast Saccharomyces cerevisiae. Physiol. Plant. 120 (2004) 12-20
    • (2004) Physiol. Plant. , vol.120 , pp. 12-20
    • Wheeler, G.L.1    Grant, C.M.2
  • 15
    • 0942268722 scopus 로고    scopus 로고
    • Analysis of the interaction between piD261/Bud32, an evolutionarily conserved protein kinase of Saccharomyces cerevisiae, and the Grx4 glutaredoxin
    • Lopreiato R., Facchin S., Sartori G., Arrigoni G., Casonato S., Ruzzene M., Pinna L.A., and Carignani G. Analysis of the interaction between piD261/Bud32, an evolutionarily conserved protein kinase of Saccharomyces cerevisiae, and the Grx4 glutaredoxin. Biochem. J. 377 (2004) 395-405
    • (2004) Biochem. J. , vol.377 , pp. 395-405
    • Lopreiato, R.1    Facchin, S.2    Sartori, G.3    Arrigoni, G.4    Casonato, S.5    Ruzzene, M.6    Pinna, L.A.7    Carignani, G.8
  • 16
    • 10644242480 scopus 로고    scopus 로고
    • Nuclear monothiol glutaredoxins of Saccharomyces cerevisiae can function as mitochondrial glutaredoxins
    • Molina M.M., Bellí G., de la Torre M.A., Rodríguez-Manzaneque M.T., and Herrero E. Nuclear monothiol glutaredoxins of Saccharomyces cerevisiae can function as mitochondrial glutaredoxins. J. Biol. Chem. 279 (2004) 51923-51930
    • (2004) J. Biol. Chem. , vol.279 , pp. 51923-51930
    • Molina, M.M.1    Bellí, G.2    de la Torre, M.A.3    Rodríguez-Manzaneque, M.T.4    Herrero, E.5
  • 17
    • 0034326925 scopus 로고    scopus 로고
    • PICOT-HD: a highly conserved oritein domain that is often associated with thioredoxin and glutaredoxin modules
    • Isakov N., Witte S., and Altman A. PICOT-HD: a highly conserved oritein domain that is often associated with thioredoxin and glutaredoxin modules. Trends Biochem. Sci. 25 (2000) 537-539
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 537-539
    • Isakov, N.1    Witte, S.2    Altman, A.3
  • 18
    • 0037020228 scopus 로고    scopus 로고
    • Structure-function analysis of yeast Grx5 monothiol glutaredoxin defines essential amino acids for the function of the protein
    • Bellí G., Polaina J., Tamarit J., de la Torre M.A., Rodríguez-Manzaneque M.T., Ros J., and Herrero E. Structure-function analysis of yeast Grx5 monothiol glutaredoxin defines essential amino acids for the function of the protein. J. Biol. Chem. 277 (2002) 37590-37596
    • (2002) J. Biol. Chem. , vol.277 , pp. 37590-37596
    • Bellí, G.1    Polaina, J.2    Tamarit, J.3    de la Torre, M.A.4    Rodríguez-Manzaneque, M.T.5    Ros, J.6    Herrero, E.7
  • 20
    • 0034695550 scopus 로고    scopus 로고
    • Inhibition of the c-jun N-terminal kinase/AP-1 and J NF-κB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain.
    • Witte S., Villalba M., Bi K., Liu Y., Isakov N., and Altman A. Inhibition of the c-jun N-terminal kinase/AP-1 and J NF-κB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain. Biol. Chem. 275 (2000) 1902-1909
    • (2000) Biol. Chem. , vol.275 , pp. 1902-1909
    • Witte, S.1    Villalba, M.2    Bi, K.3    Liu, Y.4    Isakov, N.5    Altman, A.6
  • 21
    • 14944367451 scopus 로고    scopus 로고
    • Plasmodium falciparum glutaredoxin-like proteins
    • Deponte M., Becker K., and Rahlfs S. Plasmodium falciparum glutaredoxin-like proteins. Biol. Chem. 386 (2005) 33-40
    • (2005) Biol. Chem. , vol.386 , pp. 33-40
    • Deponte, M.1    Becker, K.2    Rahlfs, S.3
  • 23
    • 23944500052 scopus 로고    scopus 로고
    • Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis
    • Wingert R.A., Galloway J.L., Barut B., Foott H., Fraenkel P., Axe J.L., Weber G.J., Dooley K., et al. Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis. Nature 436 (2005) 1035-1039
    • (2005) Nature , vol.436 , pp. 1035-1039
    • Wingert, R.A.1    Galloway, J.L.2    Barut, B.3    Foott, H.4    Fraenkel, P.5    Axe, J.L.6    Weber, G.J.7    Dooley, K.8
  • 24
    • 0030798070 scopus 로고    scopus 로고
    • A set of vectors with a tetracycline-regulatable promoter system for modulated gene expression in Saccharomyces cerevisiae
    • Garí E., Piedrafita L., Aldea M., and Herrero E. A set of vectors with a tetracycline-regulatable promoter system for modulated gene expression in Saccharomyces cerevisiae. Yeast 13 (1997) 837-848
    • (1997) Yeast , vol.13 , pp. 837-848
    • Garí, E.1    Piedrafita, L.2    Aldea, M.3    Herrero, E.4
  • 25
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 26
    • 0029915525 scopus 로고    scopus 로고
    • Computational method to predict mitochondrially imported proteins and their targeting sequences
    • Claros M.G., and Vincens P. Computational method to predict mitochondrially imported proteins and their targeting sequences. Eur. J. Biochem. 241 (1996) 770-786
    • (1996) Eur. J. Biochem. , vol.241 , pp. 770-786
    • Claros, M.G.1    Vincens, P.2
  • 28
    • 84924926133 scopus 로고
    • A series of normal stages in the development of the chick embryo
    • Hamburger V., and Hamilton H.L. A series of normal stages in the development of the chick embryo. J. Morphol. 88 (1951) 49-92
    • (1951) J. Morphol. , vol.88 , pp. 49-92
    • Hamburger, V.1    Hamilton, H.L.2
  • 29
    • 0035235373 scopus 로고    scopus 로고
    • Isolation and subfractionation of mitochondria from the yeast Saccharomyces cerevisiae
    • Diekert K., de Kroon A.I.P.M., Kispal G., and Lill R. Isolation and subfractionation of mitochondria from the yeast Saccharomyces cerevisiae. Methods Cell Biol. 65 (2001) 37-51
    • (2001) Methods Cell Biol. , vol.65 , pp. 37-51
    • Diekert, K.1    de Kroon, A.I.P.M.2    Kispal, G.3    Lill, R.4
  • 30
    • 0001525440 scopus 로고
    • An enzymatic approach to the study of the Krebs tricarboxylic acid cycle
    • Darley-Usmar W.M., Rickwood D., and Wilson M.T. (Eds), IRL Press, Oxford, UK
    • Robinson Jr. J.B., Brent L.G., Sumegi B., and Srere P.A. An enzymatic approach to the study of the Krebs tricarboxylic acid cycle. In: Darley-Usmar W.M., Rickwood D., and Wilson M.T. (Eds). Mitochondria: A Practical Approach (1987), IRL Press, Oxford, UK 153-170
    • (1987) Mitochondria: A Practical Approach , pp. 153-170
    • Robinson Jr., J.B.1    Brent, L.G.2    Sumegi, B.3    Srere, P.A.4
  • 31
    • 24044536614 scopus 로고    scopus 로고
    • Thioredoxin reductase system mediates iron binding in IscA and iron delivery for the iron-sulfur cluster assembly in IscU
    • Ding H., Harrison K., and Lu J. Thioredoxin reductase system mediates iron binding in IscA and iron delivery for the iron-sulfur cluster assembly in IscU. J. Biol. Chem. 280 (2005) 30432-30437
    • (2005) J. Biol. Chem. , vol.280 , pp. 30432-30437
    • Ding, H.1    Harrison, K.2    Lu, J.3
  • 32
    • 2342605441 scopus 로고    scopus 로고
    • Stimulation of Fe-S cluster insertion into apoFNR by Escherichia coli glutaredoxins 1, 2 and 3 in vitro
    • Achebach S., Tran Q.H., Vlamis-Gardikas A., Müllner M., Holmgren A., and Unden G. Stimulation of Fe-S cluster insertion into apoFNR by Escherichia coli glutaredoxins 1, 2 and 3 in vitro. FEBS Lett. 565 (2004) 203-206
    • (2004) FEBS Lett. , vol.565 , pp. 203-206
    • Achebach, S.1    Tran, Q.H.2    Vlamis-Gardikas, A.3    Müllner, M.4    Holmgren, A.5    Unden, G.6


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