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Volumn 49, Issue 43, 2010, Pages 9132-9139

Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC ACTIVATOR; CARDIO-VASCULAR DISEASE; CATALYTIC EFFICIENCIES; CLUSTER ASSEMBLY; COMPLEX FORMATIONS; CYSTEINE DESULFURASE; FERROUS IRON; FRATAXIN; FRIEDREICH'S ATAXIAS; HUMAN PROTEINS; IN-VITRO; MITOCHONDRIAL DYSFUNCTION; NEURODEGENERATIVE; NEURODEGENERATIVE DISEASE; OXIDATIVE STRESS RESPONSE; OXIDIZING CONDITIONS;

EID: 78049305276     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1013062     Document Type: Article
Times cited : (258)

References (60)
  • 1
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert, H., Holm, R. H., and Münck, E. (1997) Iron-sulfur clusters: Nature's modular, multipurpose structures Science 277, 653-659
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Münck, E.3
  • 2
    • 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. (2005) Structure, function, and formation of biological iron-sulfur clusters Annu. Rev. Biochem. 74, 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.4
  • 3
    • 77952813340 scopus 로고    scopus 로고
    • Building Fe-S proteins: Bacterial strategies
    • Py, B. and Barras, F. (2010) Building Fe-S proteins: Bacterial strategies Nat. Rev. Microbiol. 8, 436-446
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 436-446
    • Py, B.1    Barras, F.2
  • 4
    • 47249142777 scopus 로고    scopus 로고
    • Iron-sulfur cluster biogenesis and human disease
    • Rouault, T. A. and Tong, W.-H. (2008) Iron-sulfur cluster biogenesis and human disease Trends Genet. 24, 398-407
    • (2008) Trends Genet. , vol.24 , pp. 398-407
    • Rouault, T.A.1    Tong, W.-H.2
  • 5
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • Lill, R. (2009) Function and biogenesis of iron-sulphur proteins Nature 460, 831-838
    • (2009) Nature , vol.460 , pp. 831-838
    • Lill, R.1
  • 6
    • 77953669993 scopus 로고    scopus 로고
    • Human iron-sulfur cluster assembly, cellular iron homeostasis and disease
    • Ye, H. and Rouault, T. A. (2010) Human iron-sulfur cluster assembly, cellular iron homeostasis and disease Biochemistry 49, 4945-4956
    • (2010) Biochemistry , vol.49 , pp. 4945-4956
    • Ye, H.1    Rouault, T.A.2
  • 7
    • 67549136242 scopus 로고    scopus 로고
    • Mitochondrial dysfunction leads to nuclear genome instability via an iron-sulfur cluster defect
    • Veatch, J. R., McMurray, M. A., Nelson, Z. W., and Gottschling, D. E. (2009) Mitochondrial dysfunction leads to nuclear genome instability via an iron-sulfur cluster defect Cell 137, 1247-1258
    • (2009) Cell , vol.137 , pp. 1247-1258
    • Veatch, J.R.1    McMurray, M.A.2    Nelson, Z.W.3    Gottschling, D.E.4
  • 9
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis
    • Zheng, L., White, R. H., Cash, V. L., Jack, R. F., and Dean, D. R. (1993) Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis Proc. Natl. Acad. Sci. U.S.A. 90, 2754-2758
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 2754-2758
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Jack, R.F.4    Dean, D.R.5
  • 10
    • 0028265941 scopus 로고
    • Mechanism for the desulfurization of l -cysteine catalyzed by the nifS gene product
    • Zheng, L., White, R. H., Cash, V. L., and Dean, D. R. (1994) Mechanism for the desulfurization of l -cysteine catalyzed by the nifS gene product Biochemistry 33, 4714-4720
    • (1994) Biochemistry , vol.33 , pp. 4714-4720
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Dean, D.R.4
  • 11
    • 4644301523 scopus 로고    scopus 로고
    • Mechanism of cysteine desulfurase Slr0387 from Synechocystis sp. PCC 6803: Kinetic analysis of cleavage of the persulfide intermediate by chemical reductants
    • Behshad, E., Parkin, S. E., and Bollinger, J. M. (2004) Mechanism of cysteine desulfurase Slr0387 from Synechocystis sp. PCC 6803: Kinetic analysis of cleavage of the persulfide intermediate by chemical reductants Biochemistry 43, 12220-12226
    • (2004) Biochemistry , vol.43 , pp. 12220-12226
    • Behshad, E.1    Parkin, S.E.2    Bollinger, J.M.3
  • 12
    • 0037613459 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins
    • Yoon, T. and Cowan, J. (2003) Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins J. Am. Chem. Soc. 125, 6078-6084
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6078-6084
    • Yoon, T.1    Cowan, J.2
  • 13
    • 33745217828 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis: Characterization of Escherichia coli CYaY as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU
    • Layer, G., Ollagnier de Choudens, S., Sanakis, Y., and Fontecave, M. (2006) Iron-sulfur cluster biosynthesis: Characterization of Escherichia coli CYaY as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU J. Biol. Chem. 281, 16256-16263
    • (2006) J. Biol. Chem. , vol.281 , pp. 16256-16263
    • Layer, G.1    Ollagnier De Choudens, S.2    Sanakis, Y.3    Fontecave, M.4
  • 15
    • 4444317589 scopus 로고    scopus 로고
    • IscA mediates iron delivery for assembly of iron-sulfur clusters in IscU under the limited accessible free iron conditions
    • Ding, H., Clark, R. J., and Ding, B. (2004) IscA mediates iron delivery for assembly of iron-sulfur clusters in IscU under the limited accessible free iron conditions J. Biol. Chem. 279, 37499-37504
    • (2004) J. Biol. Chem. , vol.279 , pp. 37499-37504
    • Ding, H.1    Clark, R.J.2    Ding, B.3
  • 16
    • 0033953353 scopus 로고    scopus 로고
    • A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins
    • Lange, H., Kaut, A., Kispal, G., and Lill, R. (2000) A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins Proc. Natl. Acad. Sci. U.S.A. 97, 1050-1055
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 1050-1055
    • Lange, H.1    Kaut, A.2    Kispal, G.3    Lill, R.4
  • 18
    • 0034608935 scopus 로고    scopus 로고
    • Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli
    • Hoff, K. G., Silberg, J. J., and Vickery, L. (2000) Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 97, 7790-7795
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 7790-7795
    • Hoff, K.G.1    Silberg, J.J.2    Vickery, L.3
  • 19
    • 38349136202 scopus 로고    scopus 로고
    • GTP is required for iron-sulfur cluster biogenesis in mitochondria
    • Amutha, B., Gordon, D. M., Gu, Y., Lyver, E. R., Dancis, A., and Pain, D. (2007) GTP is required for iron-sulfur cluster biogenesis in mitochondria J. Biol. Chem. 283, 1362-1371
    • (2007) J. Biol. Chem. , vol.283 , pp. 1362-1371
    • Amutha, B.1    Gordon, D.M.2    Gu, Y.3    Lyver, E.R.4    Dancis, A.5    Pain, D.6
  • 20
    • 0037101845 scopus 로고    scopus 로고
    • The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins
    • Muhlenhoff, U., Richhardt, N., Ristow, M., Kispal, G., and Lill, R. (2002) The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins Hum. Mol. Genet. 11, 2025-2036
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2025-2036
    • Muhlenhoff, U.1    Richhardt, N.2    Ristow, M.3    Kispal, G.4    Lill, R.5
  • 21
    • 9744248303 scopus 로고    scopus 로고
    • Iron-sulfur protein maturation in human cells: Evidence for a function of frataxin
    • Stehling, O., Elsässer, H., Brückel, B., Muhlenhoff, U., and Lill, R. (2004) Iron-sulfur protein maturation in human cells: Evidence for a function of frataxin Hum. Mol. Genet. 13, 3007-3015
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 3007-3015
    • Stehling, O.1    Elsässer, H.2    Brückel, B.3    Muhlenhoff, U.4    Lill, R.5
  • 22
    • 0042232045 scopus 로고    scopus 로고
    • Yeast frataxin sequentially chaperones and stores iron by coupling protein assembly with iron oxidation
    • Park, S., Gakh, O., O'Neill, H., Mangravita, A., Nichol, H., Ferreira, G., and Isaya, G. (2003) Yeast frataxin sequentially chaperones and stores iron by coupling protein assembly with iron oxidation J. Biol. Chem. 278, 31340-31351
    • (2003) J. Biol. Chem. , vol.278 , pp. 31340-31351
    • Park, S.1    Gakh, O.2    O'Neill, H.3    Mangravita, A.4    Nichol, H.5    Ferreira, G.6    Isaya, G.7
  • 23
    • 0036472291 scopus 로고    scopus 로고
    • Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia
    • Cavadini, P., O'Neill, H., Benada, O., and Isaya, G. (2002) Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia Hum. Mol. Genet. 11, 217-227
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 217-227
    • Cavadini, P.1    O'Neill, H.2    Benada, O.3    Isaya, G.4
  • 24
    • 9644279682 scopus 로고    scopus 로고
    • Iron-induced oligomerization of yeast frataxin homologue Yfh1 is dispensable in vivo
    • Aloria, K., Schilke, B., Andrew, A. J., and Craig, E. A. (2004) Iron-induced oligomerization of yeast frataxin homologue Yfh1 is dispensable in vivo EMBO Rep. 5, 1096-1101
    • (2004) EMBO Rep. , vol.5 , pp. 1096-1101
    • Aloria, K.1    Schilke, B.2    Andrew, A.J.3    Craig, E.A.4
  • 27
    • 0036799372 scopus 로고    scopus 로고
    • A non-essential function for yeast frataxin in iron-sulfur cluster assembly
    • Duby, G., Foury, F., Ramazzotti, A., Herrmann, J., and Lutz, T. (2002) A non-essential function for yeast frataxin in iron-sulfur cluster assembly Hum. Mol. Genet. 11, 2635-2643
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2635-2643
    • Duby, G.1    Foury, F.2    Ramazzotti, A.3    Herrmann, J.4    Lutz, T.5
  • 28
    • 0141623560 scopus 로고    scopus 로고
    • An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1
    • Gerber, J., Muhlenhoff, U., and Lill, R. (2003) An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1 EMBO Rep. 4, 906-911
    • (2003) EMBO Rep. , vol.4 , pp. 906-911
    • Gerber, J.1    Muhlenhoff, U.2    Lill, R.3
  • 30
    • 34447316711 scopus 로고    scopus 로고
    • Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones
    • Shan, Y., Napoli, E., and Cortopassi, G. A. (2007) Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones Hum. Mol. Genet. 16, 929-941
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 929-941
    • Shan, Y.1    Napoli, E.2    Cortopassi, G.A.3
  • 31
    • 1642573170 scopus 로고    scopus 로고
    • Mitochondrial functional interactions between frataxin and Isu1p, the iron-sulfur cluster scaffold protein, in Saccharomyces cerevisiae
    • Ramazzotti, A., Vanmansart, V., and Foury, F. (2004) Mitochondrial functional interactions between frataxin and Isu1p, the iron-sulfur cluster scaffold protein, in Saccharomyces cerevisiae FEBS Lett. 557, 215-220
    • (2004) FEBS Lett. , vol.557 , pp. 215-220
    • Ramazzotti, A.1    Vanmansart, V.2    Foury, F.3
  • 33
    • 30444433568 scopus 로고    scopus 로고
    • The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria
    • Adam, A. C., Bornhövd, C., Prokisch, H., Neupert, W., and Hell, K. (2006) The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria EMBO J. 25, 174-183
    • (2006) EMBO J. , vol.25 , pp. 174-183
    • Adam, A.C.1    Bornhövd, C.2    Prokisch, H.3    Neupert, W.4    Hell, K.5
  • 34
    • 68049086933 scopus 로고    scopus 로고
    • Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis
    • Shi, Y., Ghosh, M., Tong, W.-H., and Rouault, T. A. (2009) Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis Hum. Mol. Genet. 18, 3014-3025
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 3014-3025
    • Shi, Y.1    Ghosh, M.2    Tong, W.-H.3    Rouault, T.A.4
  • 36
    • 0141737067 scopus 로고    scopus 로고
    • Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p
    • Muhlenhoff, U., Gerber, J., Richhardt, N., and Lill, R. (2003) Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p EMBO J. 22, 4815-4825
    • (2003) EMBO J. , vol.22 , pp. 4815-4825
    • Muhlenhoff, U.1    Gerber, J.2    Richhardt, N.3    Lill, R.4
  • 37
    • 54449085541 scopus 로고    scopus 로고
    • A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis
    • Marelja, Z., Stöcklein, W., Nimtz, M., and Leimkühler, S. (2008) A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis J. Biol. Chem. 283, 25178-25185
    • (2008) J. Biol. Chem. , vol.283 , pp. 25178-25185
    • Marelja, Z.1    Stöcklein, W.2    Nimtz, M.3    Leimkühler, S.4
  • 38
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 39
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C. and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182, 319-326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 40
    • 0000904065 scopus 로고
    • A direct microdetermination for sulfide
    • Siegel, L. M. (1965) A direct microdetermination for sulfide Anal. Biochem. 11, 126-132
    • (1965) Anal. Biochem. , vol.11 , pp. 126-132
    • Siegel, L.M.1
  • 41
    • 0034636795 scopus 로고    scopus 로고
    • IscU as a scaffold for iron-sulfur cluster biosynthesis: Sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU
    • Agar, J., Krebs, C., Frazzon, J., Huynh, B. H., Dean, D. R., and Johnson, M. (2000) 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) Biochemistry , vol.39 , pp. 7856-7862
    • Agar, J.1    Krebs, C.2    Frazzon, J.3    Huynh, B.H.4    Dean, D.R.5    Johnson, M.6
  • 42
    • 0035222647 scopus 로고    scopus 로고
    • Blue-native gels to isolate protein complexes from mitochondria
    • Schägger, H. (2001) Blue-native gels to isolate protein complexes from mitochondria Methods Cell Biol. 65, 231-244
    • (2001) Methods Cell Biol. , vol.65 , pp. 231-244
    • Schägger, H.1
  • 43
    • 57349171934 scopus 로고    scopus 로고
    • Whole tissue hydrogen sulfide concentrations are orders of magnitude lower than presently accepted values
    • Furne, J., Saeed, A., and Levitt, M. D. (2008) Whole tissue hydrogen sulfide concentrations are orders of magnitude lower than presently accepted values Am. J. Physiol. 295, R1479-R1485
    • (2008) Am. J. Physiol. , vol.295
    • Furne, J.1    Saeed, A.2    Levitt, M.D.3
  • 44
    • 0032700091 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae cultured under aerobic and anaerobic conditions: Air-level oxygen stress and protection against stress
    • Ohmori, S., Nawata, Y., Kiyono, K., Murata, H., Tsuboi, S., Ikeda, M., Akagi, R., Morohashi, K. I., and Ono, B. (1999) Saccharomyces cerevisiae cultured under aerobic and anaerobic conditions: Air-level oxygen stress and protection against stress Biochim. Biophys. Acta 1472, 587-594
    • (1999) Biochim. Biophys. Acta , vol.1472 , pp. 587-594
    • Ohmori, S.1    Nawata, Y.2    Kiyono, K.3    Murata, H.4    Tsuboi, S.5    Ikeda, M.6    Akagi, R.7    Morohashi, K.I.8    Ono, B.9
  • 45
    • 65849236255 scopus 로고    scopus 로고
    • The mitochondrial pool of free amino acids reflects the composition of mitochondrial DNA-encoded proteins: Indication of a post-translational quality control for protein synthesis
    • Ross-Inta, C., Tsai, C.-Y., and Giulivi, C. (2008) The mitochondrial pool of free amino acids reflects the composition of mitochondrial DNA-encoded proteins: Indication of a post-translational quality control for protein synthesis Biosci. Rep. 28, 239-249
    • (2008) Biosci. Rep. , vol.28 , pp. 239-249
    • Ross-Inta, C.1    Tsai, C.-Y.2    Giulivi, C.3
  • 46
    • 46049102185 scopus 로고    scopus 로고
    • Drosophila Frataxin: An Iron Chaperone during Cellular Fe-S Cluster Bioassembly
    • Kondapalli, K., Kok, N., Dancis, A., and Stemmler, T. L. (2008) Drosophila Frataxin: An Iron Chaperone during Cellular Fe-S Cluster Bioassembly Biochemistry 47, 6917-6927
    • (2008) Biochemistry , vol.47 , pp. 6917-6927
    • Kondapalli, K.1    Kok, N.2    Dancis, A.3    Stemmler, T.L.4
  • 47
    • 69249084026 scopus 로고    scopus 로고
    • Oligomeric yeast frataxin drives assembly of core machinery for mitochondrial iron-sulfur cluster synthesis
    • Li, H., Gakh, O., Smith, D., and Isaya, G. (2009) Oligomeric yeast frataxin drives assembly of core machinery for mitochondrial iron-sulfur cluster synthesis J. Biol. Chem. 284, 21971-21980
    • (2009) J. Biol. Chem. , vol.284 , pp. 21971-21980
    • Li, H.1    Gakh, O.2    Smith, D.3    Isaya, G.4
  • 48
    • 14344266832 scopus 로고
    • Incorporation of amino acids into the protein of isolated mitochondria. A search for optimum conditions and a relationship to oxidative phosphorylation
    • Truman, D. E. S. and Korner, A. (1962) Incorporation of amino acids into the protein of isolated mitochondria. A search for optimum conditions and a relationship to oxidative phosphorylation Biochem. J. 83, 588-596
    • (1962) Biochem. J. , vol.83 , pp. 588-596
    • Truman, D.E.S.1    Korner, A.2
  • 49
    • 50549209526 scopus 로고
    • The release of amino acids from rat-liver mitochondrial extract
    • Baird, G. D. (1964) The release of amino acids from rat-liver mitochondrial extract Biochim. Biophys. Acta 93, 293-303
    • (1964) Biochim. Biophys. Acta , vol.93 , pp. 293-303
    • Baird, G.D.1
  • 50
    • 0037197897 scopus 로고    scopus 로고
    • Cys-328 of IscS and Cys-63 of IscU are the sites of disulfide bridge formation in a covalently bound IscS/IscU complex: Implications for the mechanism of iron-sulfur cluster assembly
    • Kato, S.-I., Mihara, H., Kurihara, T., Takahashi, Y., Tokumoto, U., Yoshimura, T., and Esaki, N. (2002) Cys-328 of IscS and Cys-63 of IscU are the sites of disulfide bridge formation in a covalently bound IscS/IscU complex: Implications for the mechanism of iron-sulfur cluster assembly Proc. Natl. Acad. Sci. U.S.A. 99, 5948-5952
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 5948-5952
    • Kato, S.-I.1    Mihara, H.2    Kurihara, T.3    Takahashi, Y.4    Tokumoto, U.5    Yoshimura, T.6    Esaki, N.7
  • 51
    • 0141532194 scopus 로고    scopus 로고
    • Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase
    • Loiseau, L., Ollagnier de Choudens, S., Nachin, L., Fontecave, M., and Barras, F. (2003) Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase J. Biol. Chem. 278, 38352-38359
    • (2003) J. Biol. Chem. , vol.278 , pp. 38352-38359
    • Loiseau, L.1    Ollagnier De Choudens, S.2    Nachin, L.3    Fontecave, M.4    Barras, F.5
  • 53
  • 55
    • 33646342998 scopus 로고    scopus 로고
    • The Hsp70 chaperone Ssq1p is dispensable for iron-sulfur cluster formation on the scaffold protein Isu1p
    • Dutkiewicz, R., Marszalek, J., Schilke, B., Craig, E. A., Lill, R., and Muhlenhoff, U. (2006) The Hsp70 chaperone Ssq1p is dispensable for iron-sulfur cluster formation on the scaffold protein Isu1p J. Biol. Chem. 281, 7801-7808
    • (2006) J. Biol. Chem. , vol.281 , pp. 7801-7808
    • Dutkiewicz, R.1    Marszalek, J.2    Schilke, B.3    Craig, E.A.4    Lill, R.5    Muhlenhoff, U.6
  • 56
    • 0033554855 scopus 로고    scopus 로고
    • IscS is a sulfurtransferase for the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA
    • Kambampati, R. and Lauhon, C. T. (1999) IscS is a sulfurtransferase for the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA Biochemistry 38, 16561-16568
    • (1999) Biochemistry , vol.38 , pp. 16561-16568
    • Kambampati, R.1    Lauhon, C.T.2
  • 57
    • 77449106447 scopus 로고    scopus 로고
    • IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli
    • Zhang, W., Urban, A., Mihara, H., Leimkühler, S., Kurihara, T., and Esaki, N. (2010) IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli J. Biol. Chem. 285, 2302-2308
    • (2010) J. Biol. Chem. , vol.285 , pp. 2302-2308
    • Zhang, W.1    Urban, A.2    Mihara, H.3    Leimkühler, S.4    Kurihara, T.5    Esaki, N.6
  • 59
    • 47249127786 scopus 로고    scopus 로고
    • Iron-dependent regulation of frataxin expression: Implications for treatment of Friedreich ataxia
    • Li, K., Besse, E., Ha, D., Kovtunovych, G., and Rouault, T. A. (2008) Iron-dependent regulation of frataxin expression: Implications for treatment of Friedreich ataxia Hum. Mol. Genet. 17, 2265-2273
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 2265-2273
    • Li, K.1    Besse, E.2    Ha, D.3    Kovtunovych, G.4    Rouault, T.A.5
  • 60
    • 70449705810 scopus 로고    scopus 로고
    • The conserved Trp155 in human frataxin as a hotspot for oxidative stress related chemical modifications
    • Correia, A., Ow, S., Wright, P., and Gomes, C. (2009) The conserved Trp155 in human frataxin as a hotspot for oxidative stress related chemical modifications Biochem. Biophys. Res. Commun. 390, 1007-1011
    • (2009) Biochem. Biophys. Res. Commun. , vol.390 , pp. 1007-1011
    • Correia, A.1    Ow, S.2    Wright, P.3    Gomes, C.4


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