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Volumn 288, Issue 52, 2013, Pages 36773-36786

Frataxin directly stimulates mitochondrial cysteine desulfurase by exposing substrate-binding sites, and a mutant Fe-S cluster scaffold protein with frataxin-bypassing ability acts similarly

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL CHANGE; CYSTEINE DESULFURASE; FRATAXIN; SCAFFOLD PROTEIN; SUBSTRATE-BINDING SITES;

EID: 84891379841     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.525857     Document Type: Article
Times cited : (84)

References (41)
  • 1
    • 77956248535 scopus 로고    scopus 로고
    • Frataxin and mitochondrial Fe-S cluster biogenesis
    • Stemmler, T. L., Lesuisse, E., Pain, D., and Dancis, A. (2010) Frataxin and mitochondrial Fe-S cluster biogenesis. J. Biol. Chem. 285, 26737-26743
    • (2010) J. Biol. Chem. , vol.285 , pp. 26737-26743
    • Stemmler, T.L.1    Lesuisse, E.2    Pain, D.3    Dancis, A.4
  • 2
    • 84858015433 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur clusters in mammalian cells: New insights and relevance to human disease
    • Rouault, T. A. (2012) Biogenesis of iron-sulfur clusters in mammalian cells: new insights and relevance to human disease. Dis. Model. Mech. 5, 155-164
    • (2012) Dis. Model. Mech. , vol.5 , pp. 155-164
    • Rouault, T.A.1
  • 6
    • 0017031971 scopus 로고
    • Pathology of the heart in Friedreich's ataxia: Review of the literature and report of one case
    • Sanchez-Casis, G., Cote, M., and Barbeau, A. (1976) Pathology of the heart in Friedreich's ataxia: review of the literature and report of one case. Can. J. Neurol. Sci. 3, 349-354
    • (1976) Can. J. Neurol. Sci. , vol.3 , pp. 349-354
    • Sanchez-Casis, G.1    Cote, M.2    Barbeau, A.3
  • 9
    • 0032800601 scopus 로고    scopus 로고
    • Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain
    • Foury, F. (1999) Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain. FEBS Lett. 456, 281-284
    • (1999) FEBS Lett. , vol.456 , pp. 281-284
    • Foury, F.1
  • 10
    • 0037101845 scopus 로고    scopus 로고
    • The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins
    • Mühlenhoff, 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
    • Mühlenhoff, U.1    Richhardt, N.2    Ristow, M.3    Kispal, G.4    Lill, R.5
  • 11
    • 0030825723 scopus 로고    scopus 로고
    • Respiratory deficiency due to loss of mitochondrial DNA in yeast lacking the frataxin homologue
    • Wilson, R. B., and Roof, D. M. (1997) Respiratory deficiency due to loss of mitochondrial DNA in yeast lacking the frataxin homologue. Nat. Genet. 16, 352-357
    • (1997) Nat. Genet. , vol.16 , pp. 352-357
    • Wilson, R.B.1    Roof, D.M.2
  • 12
    • 0034641851 scopus 로고    scopus 로고
    • Human frataxin maintains mitochondrial iron homeostasis in Saccharomyces cerevisiae
    • Cavadini, P., Gellera, C., Patel, P. I., and Isaya, G. (2000) Human frataxin maintains mitochondrial iron homeostasis in Saccharomyces cerevisiae. Hum. Mol. Genet. 9, 2523-2530
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2523-2530
    • Cavadini, P.1    Gellera, C.2    Patel, P.I.3    Isaya, G.4
  • 13
    • 77957676909 scopus 로고    scopus 로고
    • Molecular details of the yeast frataxin-Isu1 interaction during mitochondrial Fe-S cluster assembly
    • Cook, J. D., Kondapalli, K. C., Rawat, S., Childs, W. C., Murugesan, Y., Dancis, A., and Stemmler, T. L. (2010) Molecular details of the yeast frataxin-Isu1 interaction during mitochondrial Fe-S cluster assembly. Biochemistry 49, 8756-8765
    • (2010) Biochemistry , vol.49 , pp. 8756-8765
    • Cook, J.D.1    Kondapalli, K.C.2    Rawat, S.3    Childs, W.C.4    Murugesan, Y.5    Dancis, A.6    Stemmler, T.L.7
  • 15
    • 84875582275 scopus 로고    scopus 로고
    • Iron-sulfur cluster synthesis, iron homeostasis, and oxidative stress in Friedreich ataxia
    • Vaubel, R. A., and Isaya, G. (2013) Iron-sulfur cluster synthesis, iron homeostasis, and oxidative stress in Friedreich ataxia. Mol. Cell. Neurosci. 55, 50-61
    • (2013) Mol. Cell. Neurosci. , vol.55 , pp. 50-61
    • Vaubel, R.A.1    Isaya, G.2
  • 16
    • 78049305276 scopus 로고    scopus 로고
    • Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex
    • Tsai, C.-L., and Barondeau, D. P. (2010) Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex. Biochemistry 49, 9132-9139
    • (2010) Biochemistry , vol.49 , pp. 9132-9139
    • Tsai, C.-L.1    Barondeau, D.P.2
  • 17
    • 79551514731 scopus 로고    scopus 로고
    • Mammalian frataxin: An essential function for cellular viability through an interaction with a preformed ISCU/NFS1/ISD11 iron-sulfur assembly complex
    • Schmucker, S., Martelli, A., Colin, F., Page, A., Wattenhofer- Donzé, M., Reutenauer, L., and Puccio, H. (2011) Mammalian frataxin: An essential function for cellular viability through an interaction with a preformed ISCU/NFS1/ISD11 iron-sulfur assembly complex. PLoS One 6, e16199
    • (2011) PLoS One , vol.6
    • Schmucker, S.1    Martelli, A.2    Colin, F.3    Page, A.4    Wattenhofer-Donzé, M.5    Reutenauer, L.6    Puccio, H.7
  • 18
    • 45549107531 scopus 로고    scopus 로고
    • Binding of yeast frataxin to the scaffold for Fe-S cluster biogenesis, Isu
    • Wang, T., and Craig, E. A. (2008) Binding of yeast frataxin to the scaffold for Fe-S cluster biogenesis, Isu. J. Biol. Chem. 283, 12674-12679
    • (2008) J. Biol. Chem. , vol.283 , pp. 12674-12679
    • Wang, T.1    Craig, E.A.2
  • 19
    • 0141623560 scopus 로고    scopus 로고
    • An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S-cluster synthesis on Isu1
    • Gerber, J., Mühlenhoff, 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    Mühlenhoff, U.2    Lill, R.3
  • 20
    • 0032722872 scopus 로고    scopus 로고
    • Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution
    • Li, J., Kogan, M., Knight, S. A., Pain, D., and Dancis, A. (1999) Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution. J. Biol. Chem. 274, 33025-33034
    • (1999) J. Biol. Chem. , vol.274 , pp. 33025-33034
    • Li, J.1    Kogan, M.2    Knight, S.A.3    Pain, D.4    Dancis, A.5
  • 21
    • 84869029429 scopus 로고    scopus 로고
    • Persulfide formation on mitochondrial cysteine desulfurase: Enzyme activation by a eukaryote-specific interacting protein and Fe-S cluster synthesis
    • Pandey, A., Golla, R., Yoon, H., Dancis, A., and Pain, D. (2012) Persulfide formation on mitochondrial cysteine desulfurase: Enzyme activation by a eukaryote-specific interacting protein and Fe-S cluster synthesis. Biochem. J. 448, 171-187
    • (2012) Biochem. J. , vol.448 , pp. 171-187
    • Pandey, A.1    Golla, R.2    Yoon, H.3    Dancis, A.4    Pain, D.5
  • 23
    • 71049136017 scopus 로고    scopus 로고
    • Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55
    • Naamati, A., Regev-Rudzki, N., Galperin, S., Lill, R., and Pines, O. (2009) Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55. J. Biol. Chem. 284, 30200-30208
    • (2009) J. Biol. Chem. , vol.284 , pp. 30200-30208
    • Naamati, A.1    Regev-Rudzki, N.2    Galperin, S.3    Lill, R.4    Pines, O.5
  • 24
    • 0035253385 scopus 로고    scopus 로고
    • Distinct roles for two N-terminal cleaved domains in mitochondrial import of the yeast frataxin homolog, Yfh1p
    • Gordon, D. M., Kogan, M., Knight, S. A., Dancis, A., and Pain, D. (2001) Distinct roles for two N-terminal cleaved domains in mitochondrial import of the yeast frataxin homolog, Yfh1p. Hum. Mol. Genet. 10, 259-269
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 259-269
    • Gordon, D.M.1    Kogan, M.2    Knight, S.A.3    Dancis, A.4    Pain, D.5
  • 26
    • 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
  • 27
    • 84864805076 scopus 로고    scopus 로고
    • Identification of a Nfs1p-bound persulfide intermediate in Fe-S cluster synthesis by intact mitochondria
    • Pandey, A., Yoon, H., Lyver, E. R., Dancis, A., and Pain, D. (2012) Identification of a Nfs1p-bound persulfide intermediate in Fe-S cluster synthesis by intact mitochondria. Mitochondrion 12, 539-549
    • (2012) Mitochondrion , vol.12 , pp. 539-549
    • Pandey, A.1    Yoon, H.2    Lyver, E.R.3    Dancis, A.4    Pain, D.5
  • 29
    • 78649876722 scopus 로고    scopus 로고
    • Mitochondrial NADH kinase, Pos5p, is required for efficient iron-sulfur cluster biogenesis in Saccharomyces cerevisiae
    • Pain, J., Balamurali, M. M., Dancis, A., and Pain, D. (2010) Mitochondrial NADH kinase, Pos5p, is required for efficient iron-sulfur cluster biogenesis in Saccharomyces cerevisiae. J. Biol. Chem. 285, 39409-39424
    • (2010) J. Biol. Chem. , vol.285 , pp. 39409-39424
    • Pain, J.1    Balamurali, M.M.2    Dancis, A.3    Pain, D.4
  • 30
    • 63449102347 scopus 로고    scopus 로고
    • Nucleotidedependent iron-sulfur cluster biogenesis of endogenous and imported apoproteins in isolated intact mitochondria
    • Amutha, B., Gordon, D. M., Dancis, A., and Pain, D. (2009) Nucleotidedependent iron-sulfur cluster biogenesis of endogenous and imported apoproteins in isolated intact mitochondria. Methods Enzymol. 456, 247-266
    • (2009) Methods Enzymol. , vol.456 , pp. 247-266
    • Amutha, B.1    Gordon, D.M.2    Dancis, A.3    Pain, D.4
  • 31
    • 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. (2008) GTP is required for iron-sulfur cluster biogenesis in mitochondria. J. Biol. Chem. 283, 1362-1371
    • (2008) 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
  • 32
    • 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. (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.K.4
  • 33
    • 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
  • 36
    • 34548819035 scopus 로고    scopus 로고
    • S-Cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress
    • Hochgräfe, F., Mostertz, J., Pöther, D.-C., Becher, D., Helmann, J. D., and Hecker, M. (2007) S-Cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress. J. Biol. Chem. 282, 25981-25985
    • (2007) J. Biol. Chem. , vol.282 , pp. 25981-25985
    • Hochgräfe, F.1    Mostertz, J.2    Pöther, D.-C.3    Becher, D.4    Helmann, J.D.5    Hecker, M.6
  • 38
    • 1642396548 scopus 로고    scopus 로고
    • Role of YHM1, encoding a mitochondrial carrier protein, in iron distribution of yeast
    • Lesuisse, E., Lyver, E. R., Knight, S. A., and Dancis, A. (2004) Role of YHM1, encoding a mitochondrial carrier protein, in iron distribution of yeast. Biochem. J. 378, 599-607
    • (2004) Biochem. J. , vol.378 , pp. 599-607
    • Lesuisse, E.1    Lyver, E.R.2    Knight, S.A.3    Dancis, A.4
  • 39
    • 46049102185 scopus 로고    scopus 로고
    • Drosophila frataxin: An iron chaperone during cellular Fe-S cluster bioassembly
    • Kondapalli, K. C., Kok, N. M., 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.C.1    Kok, N.M.2    Dancis, A.3    Stemmler, T.L.4


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