메뉴 건너뛰기




Volumn 4, Issue 5, 2009, Pages 753-766

Analysis of iron-sulfur protein maturation in eukaryotes

Author keywords

[No Author keywords available]

Indexed keywords

IRON; IRON SULFUR PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 69849113825     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2009.39     Document Type: Article
Times cited : (77)

References (74)
  • 1
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert, H., Holm, R.H. & Munck, E. Iron-sulfur clusters: nature's modular, multipurpose structures. Science 277, 653-659 (1997).
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Munck, 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. & Johnson, M.K. Structure, function and formation of biological iron-sulfur clusters. Ann. Rev. Biochem. 74, 247-281 (2005).
    • (2005) Ann. Rev. Biochem , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 3
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: Mechanisms, connected processes, and diseases
    • Lill, R. & Muhlenhoff, U. Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases. Annu. Rev. Biochem. 77, 669-700 (2008).
    • (2008) Annu. Rev. Biochem , vol.77 , pp. 669-700
    • Lill, R.1    Muhlenhoff, U.2
  • 5
    • 33751177803 scopus 로고    scopus 로고
    • Iron-sulfur protein biogenesis in eukaryotes: Components and mechanisms
    • Lill, R. & Muhlenhoff, U. Iron-sulfur protein biogenesis in eukaryotes: components and mechanisms. Annu. Rev. Cell Dev. Biol. 22, 457-486 (2006).
    • (2006) Annu. Rev. Cell Dev. Biol , vol.22 , pp. 457-486
    • Lill, R.1    Muhlenhoff, U.2
  • 6
    • 34247124148 scopus 로고    scopus 로고
    • Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation
    • Vickery, L.E. & Cupp-Vickery, J.R. Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation. Cnt. Rev. Biochem. Mol. Biol. 42, 95-111 (2007).
    • (2007) Cnt. Rev. Biochem. Mol. Biol , vol.42 , pp. 95-111
    • Vickery, L.E.1    Cupp-Vickery, J.R.2
  • 7
    • 40749086415 scopus 로고    scopus 로고
    • Mitochondrial Iba57p is required for Fe/S cluster formation on aconitase and activation of radical SAM enzymes
    • Gelling, C., Dawes, I.W., Richhardt, N., Lill, R. & Muhlenhoff, U. Mitochondrial Iba57p is required for Fe/S cluster formation on aconitase and activation of radical SAM enzymes. Mol. Cell Biol. 28, 1851-1861 (2008).
    • (2008) Mol. Cell Biol , vol.28 , pp. 1851-1861
    • Gelling, C.1    Dawes, I.W.2    Richhardt, N.3    Lill, R.4    Muhlenhoff, U.5
  • 8
    • 38349136202 scopus 로고    scopus 로고
    • GTP is required for iron-sulfur cluster biogenesis in mitochondria
    • Amutha, B. et al. GTP is required for iron-sulfur cluster biogenesis in mitochondria. J. Biol. Chem. 283, 1362-1371 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 1362-1371
    • Amutha, B.1
  • 9
    • 33746868343 scopus 로고    scopus 로고
    • Mechanisms of iron-sulfur protein maturation in mitochondria, cytosol and nucleus of eukaryotes
    • Lill, R. et al. Mechanisms of iron-sulfur protein maturation in mitochondria, cytosol and nucleus of eukaryotes. Biochim. Biophys. Acta 1763, 652-667 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 652-667
    • Lill, R.1
  • 10
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atm1p and Nfs1p are required for biogenesis of cytosolic Fe/S proteins
    • Kispal, G., Csere, P., Prohl, C. & Lill, R. The mitochondrial proteins Atm1p and Nfs1p are required for biogenesis of cytosolic Fe/S proteins. EMBO J. 18, 3981-3989 (1999).
    • (1999) EMBO J , vol.18 , pp. 3981-3989
    • Kispal, G.1    Csere, P.2    Prohl, C.3    Lill, R.4
  • 11
    • 4544321137 scopus 로고    scopus 로고
    • The cell's cookbook for iron-sulfur clusters: Recipes for fool's gold
    • Balk, J. & Lill, R. The cell's cookbook for iron-sulfur clusters: recipes for fool's gold? Chem. Biol. Chem. 5,1044-1049 (2004).
    • (2004) Chem. Biol. Chem , vol.5 , pp. 1044-1049
    • Balk, J.1    Lill, R.2
  • 12
    • 34247247617 scopus 로고    scopus 로고
    • The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol
    • Netz, D.J., Pierik, A.J., Stumpfig, M., Muhlenhoff, U. & Lill, R. The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol. Nat. Chem. Biol. 3, 278-286 (2007).
    • (2007) Nat. Chem. Biol , vol.3 , pp. 278-286
    • Netz, D.J.1    Pierik, A.J.2    Stumpfig, M.3    Muhlenhoff, U.4    Lill, R.5
  • 13
    • 2942565619 scopus 로고    scopus 로고
    • The hydrogenase- like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins
    • Balk, J., Pierik, A.J., Aguilar Netz, D., Muhlenhoff, U. & Lill, R. The hydrogenase- like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins. EMBO J. 23, 2105-2115 (2004).
    • (2004) EMBO J , vol.23 , pp. 2105-2115
    • Balk, J.1    Pierik, A.J.2    Aguilar Netz, D.3    Muhlenhoff, U.4    Lill, R.5
  • 14
    • 28544450863 scopus 로고    scopus 로고
    • The essential WD40 protein Cia1 is involved in a late step of cytosolic and nuclear iron-sulfur protein assembly
    • Balk, J., Aguilar Netz, D.J., Tepper, K., Pierik, A.J. & Lill, R. The essential WD40 protein Cia1 is involved in a late step of cytosolic and nuclear iron-sulfur protein assembly. Mol. Cell Biol. 25, 10833-10841 (2005).
    • (2005) Mol. Cell Biol , vol.25 , pp. 10833-10841
    • Balk, J.1    Aguilar Netz, D.J.2    Tepper, K.3    Pierik, A.J.4    Lill, R.5
  • 15
    • 51349089178 scopus 로고    scopus 로고
    • Dre2, a conserved eukaryotic Fe/S cluster protein, functions in cytosolic Fe/S protein biogenesis
    • Zhang, Y. et al. Dre2, a conserved eukaryotic Fe/S cluster protein, functions in cytosolic Fe/S protein biogenesis. Mol. Cell Biol. 28, 5569-5582 (2008).
    • (2008) Mol. Cell Biol , vol.28 , pp. 5569-5582
    • Zhang, Y.1
  • 16
    • 14744294785 scopus 로고    scopus 로고
    • Iron-sulfur protein biogenesis in eukaryotes
    • Lill, R. & Muhlenhoff, U. Iron-sulfur protein biogenesis in eukaryotes. Trends Biochem. Sci. 30, 133-141 (2005).
    • (2005) Trends Biochem. Sci , vol.30 , pp. 133-141
    • Lill, R.1    Muhlenhoff, U.2
  • 17
    • 9744248303 scopus 로고    scopus 로고
    • Iron-sulfur protein maturation in human cells: Evidence fora function offrataxin
    • Stehling, O., Elsasser, H.P., Bnickel, B., Muhlenhoff, U. & Lill, R. Iron-sulfur protein maturation in human cells: evidence fora function offrataxin. Hum. Mol. Genet. 13, 3007-3015 (2004).
    • (2004) Hum. Mol. Genet , vol.13 , pp. 3007-3015
    • Stehling, O.1    Elsasser, H.P.2    Bnickel, B.3    Muhlenhoff, U.4    Lill, R.5
  • 18
    • 23944500052 scopus 로고    scopus 로고
    • Deficiency ofglutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis
    • Wingert, R.A. et al. Deficiency ofglutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis. Nature 436, 1035-1039 (2005).
    • (2005) Nature , vol.436 , pp. 1035-1039
    • Wingert, R.A.1
  • 19
    • 33746509655 scopus 로고    scopus 로고
    • Role of human mitochondrial Nfs1 in cytosolic iron-sulfur protein biogenesis and iron regulation
    • Biederbick, A. et al. Role of human mitochondrial Nfs1 in cytosolic iron-sulfur protein biogenesis and iron regulation. Mol. Cell Biol. 26, 5675-5687 (2006).
    • (2006) Mol. Cell Biol , vol.26 , pp. 5675-5687
    • Biederbick, A.1
  • 20
    • 33644772614 scopus 로고    scopus 로고
    • The mitochondrial ATP-binding cassette transporter Abcb7 is essential in mice and participates in cytosolic iron-sulphur cluster biogenesis
    • Pondarre, C. et al. The mitochondrial ATP-binding cassette transporter Abcb7 is essential in mice and participates in cytosolic iron-sulphur cluster biogenesis. Hum. Mol. Genet. 15, 953-964 (2006).
    • (2006) Hum. Mol. Genet , vol.15 , pp. 953-964
    • Pondarre, C.1
  • 21
    • 33644623262 scopus 로고    scopus 로고
    • Functions ofmitochondriallSCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis
    • Tong, W.H. & Rouault, T.A. Functions ofmitochondriallSCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis. Cell Metab. 3, 199-210 (2006).
    • (2006) Cell Metab , vol.3 , pp. 199-210
    • Tong, W.H.1    Rouault, T.A.2
  • 22
    • 44049094146 scopus 로고    scopus 로고
    • A role for IOP1 in mammalian cytosolic iron-sulfur protein biogenesis
    • Song, D. & Lee, F.S. A role for IOP1 in mammalian cytosolic iron-sulfur protein biogenesis. J. Biol. Chem. 283, 9231-9238 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 9231-9238
    • Song, D.1    Lee, F.S.2
  • 23
    • 50249156530 scopus 로고    scopus 로고
    • Human Nbp35 is essentialfor both cytosolic iron-sulfur protein assembly and iron homeostasis
    • Stehling, O. etal. Human Nbp35 is essentialfor both cytosolic iron-sulfur protein assembly and iron homeostasis. Mol. Cell Biol. 28, 5517-5528 (2008).
    • (2008) Mol. Cell Biol , vol.28 , pp. 5517-5528
    • Stehling, O.1
  • 24
    • 47249142777 scopus 로고    scopus 로고
    • Iron-sulfur cluster biogenesis and human disease
    • Rouault, T.A. & Tong, W.H. Iron-sulfur cluster biogenesis and human disease. Trends Genet. 24, 398-407 (2008).
    • (2008) Trends Genet , vol.24 , pp. 398-407
    • Rouault, T.A.1    Tong, W.H.2
  • 25
    • 13344270899 scopus 로고    scopus 로고
    • Friedreich's ataxia: Autosomal recessive disease caused byan intronic GAA triplet repeat expansion
    • Campuzano, V. etal. Friedreich's ataxia: autosomal recessive disease caused byan intronic GAA triplet repeat expansion. Science 271, 1423-1427 (1996).
    • (1996) Science , vol.271 , pp. 1423-1427
    • Campuzano, V.1
  • 26
    • 34548013116 scopus 로고    scopus 로고
    • The human counterpart of zebrafish shiraz shows sideroblastic-like microcytic anemia and iron overload
    • Camaschella, C. et al. The human counterpart of zebrafish shiraz shows sideroblastic-like microcytic anemia and iron overload. Blood 110, 1353-1358.
    • Blood , vol.110 , pp. 1353-1358
    • Camaschella, C.1
  • 27
    • 41149169596 scopus 로고    scopus 로고
    • Splice mutation in the iron-sulfur cluster scaffold protein ISCU causes myopathy with exercise intolerance
    • Mochel, F. et al. Splice mutation in the iron-sulfur cluster scaffold protein ISCU causes myopathy with exercise intolerance. Am. J. Hum. Genet. 82, 652-660.
    • Am. J. Hum. Genet , vol.82 , pp. 652-660
    • Mochel, F.1
  • 28
    • 44349149346 scopus 로고    scopus 로고
    • Myopathy with lactic acidosis is linked to chromosome 12q23.3-24.11 and caused by an intron mutation in the ISCU gene resulting in a splicing defect
    • Olsson, A., Lind, L., Thornell, L.E. & Holmberg, M. Myopathy with lactic acidosis is linked to chromosome 12q23.3-24.11 and caused by an intron mutation in the ISCU gene resulting in a splicing defect. Hum. Mol. Genet. 17, 1666-1672 (2008).
    • (2008) Hum. Mol. Genet , vol.17 , pp. 1666-1672
    • Olsson, A.1    Lind, L.2    Thornell, L.E.3    Holmberg, M.4
  • 29
    • 20044391418 scopus 로고    scopus 로고
    • Biogenesis of cytosolic ribosomes requires the essential iron- sulphur protein Rli1p and mitochondria
    • Kispal, G. et al. Biogenesis of cytosolic ribosomes requires the essential iron- sulphur protein Rli1p and mitochondria. EMBO J. 24, 589-598 (2005).
    • (2005) EMBO J , vol.24 , pp. 589-598
    • Kispal, G.1
  • 30
    • 34548492954 scopus 로고    scopus 로고
    • An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis
    • Klinge, S., Hirst, J., Maman, J.D., Krude, T. & Pellegrini, L. An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis. Nat. Struct. Mol. Biol. 14, 875-877 (2007).
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 875-877
    • Klinge, S.1    Hirst, J.2    Maman, J.D.3    Krude, T.4    Pellegrini, L.5
  • 31
    • 33748428875 scopus 로고    scopus 로고
    • The DNA repair helicases XPD and FancJ have essential iron-sulfur domains
    • Rudolf, J., Makrantoni, V., Ingledew, W.J., Stark, M.J. & White, M.F. The DNA repair helicases XPD and FancJ have essential iron-sulfur domains. Mol. Cell 23, 801-808 (2006).
    • (2006) Mol. Cell , vol.23 , pp. 801-808
    • Rudolf, J.1    Makrantoni, V.2    Ingledew, W.J.3    Stark, M.J.4    White, M.F.5
  • 32
    • 14744301484 scopus 로고    scopus 로고
    • Functional link between ribosome formation and biogenesis of iron-sulfur proteins
    • Yarunin, A., Panse, V., Petfalski, E., Tollervey, D. & Hurt, E. Functional link between ribosome formation and biogenesis of iron-sulfur proteins. EMBO J. 24, 580-588 (2005).
    • (2005) EMBO J , vol.24 , pp. 580-588
    • Yarunin, A.1    Panse, V.2    Petfalski, E.3    Tollervey, D.4    Hurt, E.5
  • 33
    • 0027364921 scopus 로고
    • Human xeroderma pigmentosum group D gene encodes a DNA helicase
    • Sung, P. et al. Human xeroderma pigmentosum group D gene encodes a DNA helicase. Nature 365, 852-855 (1993).
    • (1993) Nature , vol.365 , pp. 852-855
    • Sung, P.1
  • 34
    • 44149094083 scopus 로고    scopus 로고
    • XPD helicase structures and activities: Insights into the cancer and aging phenotypes from XPD mutations
    • Fan, L. et al. XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations. Cell 133, 789-800 (2008).
    • (2008) Cell , vol.133 , pp. 789-800
    • Fan, L.1
  • 35
    • 0027732943 scopus 로고
    • Analysis, by electrospray ionization mass spectrometry, of several forms of Clostridium pasteurianum rubredoxin
    • Petillot, Y., Forest, E., Mathieu, I., Meyer, J. & Moulis, J.-M. Analysis, by electrospray ionization mass spectrometry, of several forms of Clostridium pasteurianum rubredoxin. Biochem. J. 296, 657-661 (1993).
    • (1993) Biochem. J , vol.296 , pp. 657-661
    • Petillot, Y.1    Forest, E.2    Mathieu, I.3    Meyer, J.4    Moulis, J.-M.5
  • 36
    • 7444266901 scopus 로고    scopus 로고
    • Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site
    • Ramelot, T.A. et al. Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site. J. Mol. Biol. 344, 567-583 (2004).
    • (2004) J. Mol. Biol , vol.344 , pp. 567-583
    • Ramelot, T.A.1
  • 37
    • 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. & Lill, R. Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. EMBO J. 22, 4815-4825 (2003).
    • (2003) EMBO J , vol.22 , pp. 4815-4825
    • Muhlenhoff, U.1    Gerber, J.2    Richhardt, N.3    Lill, R.4
  • 38
    • 34147109189 scopus 로고    scopus 로고
    • Methods forstudying iron metabolism in yeast mitochondria
    • Molik, S., Lill, R. & Muhlenhoff, U. Methods forstudying iron metabolism in yeast mitochondria. Methods Cell Biol. 80, 261-280 (2007).
    • (2007) Methods Cell Biol , vol.80 , pp. 261-280
    • Molik, S.1    Lill, R.2    Muhlenhoff, U.3
  • 39
    • 40949138258 scopus 로고    scopus 로고
    • Investigation of iron-sulfur protein maturation in eukaryotes
    • (eds. Leister, D. & Herrmann, J.M., Humana Press Inc., Totowa, NJ
    • Stehling, O. etal. Investigation of iron-sulfur protein maturation in eukaryotes. In Methods in Molecular Biology (eds. Leister, D. & Herrmann, J.M.) 325-342 (Humana Press Inc., Totowa, NJ, 2007).
    • (2007) Methods in Molecular Biology , pp. 325-342
    • Stehling, O.E.1
  • 40
    • 0035970292 scopus 로고    scopus 로고
    • The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria
    • Lutz, T., Westermann, B., Neupert, W. & Herrmann, J.M. The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria. J. Mol. Biol. 307, 815-825 (2001).
    • (2001) J. Mol. Biol , vol.307 , pp. 815-825
    • Lutz, T.1    Westermann, B.2    Neupert, W.3    Herrmann, J.M.4
  • 41
    • 34147189950 scopus 로고    scopus 로고
    • Controlled expression of nif and isc iron-sulfur protein maturation components reveals target specificity and limited functional replacement between the two systems
    • Dos Santos, P.C., Johnson, D.C., Ragle, B.E., Unciuleac, M.-C. & Dean, D.R. Controlled expression of nif and isc iron-sulfur protein maturation components reveals target specificity and limited functional replacement between the two systems. J. Bacteriol. 189, 2854-2862 (2007).
    • (2007) J. Bacteriol , vol.189 , pp. 2854-2862
    • Dos Santos, P.C.1    Johnson, D.C.2    Ragle, B.E.3    Unciuleac, M.-C.4    Dean, D.R.5
  • 43
    • 0027050315 scopus 로고
    • Cellular regulation of the iron-responsive element binding protein: Disassembly ofthe cubane iron-sulfur cluster results in high-affinity RNA binding
    • Haile, D.J. et al. Cellular regulation of the iron-responsive element binding protein: disassembly ofthe cubane iron-sulfur cluster results in high-affinity RNA binding. Proc. Natl. Acad. Sci. USA 89, 11735-11739 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11735-11739
    • Haile, D.J.1
  • 44
    • 0032553445 scopus 로고    scopus 로고
    • Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron- sulfur cluster assembly
    • Strain, J. et al. Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron- sulfur cluster assembly. J. Biol. Chem. 273, 31138-31144 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 31138-31144
    • Strain, J.1
  • 45
    • 0018116463 scopus 로고
    • Analysis of acid-labile sulfide and sulfhydryl groups
    • Rabinowitz, J.C. Analysis of acid-labile sulfide and sulfhydryl groups. Methods Enzymol. 53, 275-277 (1978).
    • (1978) Methods Enzymol , vol.53 , pp. 275-277
    • Rabinowitz, J.C.1
  • 46
    • 0026640677 scopus 로고
    • Physiological analysis of mutants of Saccharomyces cerevisiae impaired in sulphate assimilation
    • Thomas, D., Barbey, R., Henry, D. & Surdin-Kerjan, Y. Physiological analysis of mutants of Saccharomyces cerevisiae impaired in sulphate assimilation. J. Gen. Microbiol. 138, 2021-2028 (1992).
    • (1992) J. Gen. Microbiol , vol.138 , pp. 2021-2028
    • Thomas, D.1    Barbey, R.2    Henry, D.3    Surdin-Kerjan, Y.4
  • 47
    • 0027481943 scopus 로고
    • Global regulation of mitochondrial biogenesis in Saccharomyces cerevisiae
    • De Winde, J.H. & Grivell, L.A. Global regulation of mitochondrial biogenesis in Saccharomyces cerevisiae. Prog. Nucleic Acid Res. Mol. Biol. 46, 51-91 (1993).
    • (1993) Prog. Nucleic Acid Res. Mol. Biol , vol.46 , pp. 51-91
    • De Winde, J.H.1    Grivell, L.A.2
  • 49
    • 39149142997 scopus 로고    scopus 로고
    • The X-ray crystal structure of RNA polymerase from Archaea
    • Hirata, A., Klein, B.J. & Murakami, K.S. The X-ray crystal structure of RNA polymerase from Archaea. Nature 451, 851-854 (2008).
    • (2008) Nature , vol.451 , pp. 851-854
    • Hirata, A.1    Klein, B.J.2    Murakami, K.S.3
  • 50
    • 0141848663 scopus 로고    scopus 로고
    • A novel eukaryotic factor for cytosolic Fe-S cluster assembly
    • Roy, A., Solodovnikova, N., Nicholson, T., Antholine, W. & Walden, W.E. A novel eukaryotic factor for cytosolic Fe-S cluster assembly. EMBO J. 22, 4826-4835 (2003).
    • (2003) EMBO J , vol.22 , pp. 4826-4835
    • Roy, A.1    Solodovnikova, N.2    Nicholson, T.3    Antholine, W.4    Walden, W.E.5
  • 51
    • 0033953353 scopus 로고    scopus 로고
    • Mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins
    • Lange, H., Kaut, A., Kispal, G. & Lill, R. A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins. Proc. Natl. Acad. Sci. USA 97, 1050-1055 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1050-1055
    • Lange, H.1    Kaut, A.2    Kispal, G.3    Lill, R.A.4
  • 52
    • 2242453224 scopus 로고    scopus 로고
    • Characterization ofiron-sulfur protein assembly in isolated mitochondria: A requirement for ATP, NADH and reduced iron
    • Muhlenhoff, U., Richhardt, N., Gerber, J. & Lill, R. Characterization ofiron-sulfur protein assembly in isolated mitochondria: a requirement for ATP, NADH and reduced iron. J. Biol. Chem. 277, 29810-29816 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 29810-29816
    • Muhlenhoff, U.1    Richhardt, N.2    Gerber, J.3    Lill, R.4
  • 53
    • 33751073661 scopus 로고    scopus 로고
    • Half-life measurement of 55Fe. Appl. Radiat
    • Van Ammel, R., Pomme, S. & Sibbens, G. Half-life measurement of 55Fe. Appl. Radiat. Isot. 64, 1412-1416 (2006).
    • (2006) Isot , vol.64 , pp. 1412-1416
    • Van Ammel, R.1    Pomme, S.2    Sibbens, G.3
  • 54
    • 0142215475 scopus 로고    scopus 로고
    • Global analysis of protein expression in yeast
    • Ghaemmaghami, S. et al. Global analysis of protein expression in yeast. Nature 425, 737-741 (2003).
    • (2003) Nature , vol.425 , pp. 737-741
    • Ghaemmaghami, S.1
  • 55
    • 14744279245 scopus 로고    scopus 로고
    • The eukaryotic P-loop NTPase Nbp35: An essential component of the cytosolic and nuclear iron-sulfur protein assembly machinery
    • Hausmann, A. et al. The eukaryotic P-loop NTPase Nbp35: an essential component of the cytosolic and nuclear iron-sulfur protein assembly machinery. Proc. Natl. Acad. Sci. USA 102, 3266-3271 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3266-3271
    • Hausmann, A.1
  • 56
    • 0036277153 scopus 로고    scopus 로고
    • Vector systems for heterologous expression of proteins in Saccharomyces cerevisiae
    • Funk, M. et al. Vector systems for heterologous expression of proteins in Saccharomyces cerevisiae. Methods Enzymol. 350, 248-257 (2002).
    • (2002) Methods Enzymol , vol.350 , pp. 248-257
    • Funk, M.1
  • 57
    • 0033516467 scopus 로고    scopus 로고
    • Mechanism of iron transport to the site of heme synthesis inside yeast mitochondria
    • Lange, H., Kispal, G. & Lill, R. Mechanism of iron transport to the site of heme synthesis inside yeast mitochondria. J. Biol. Chem. 274, 18989-18996 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 18989-18996
    • Lange, H.1    Kispal, G.2    Lill, R.3
  • 58
    • 4444271170 scopus 로고    scopus 로고
    • A versatile toolbox for PCR-based tagging of yeast genes: New fluorescent proteins, more markersand promotersubstitution cassettes
    • Janke, C. et al. A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markersand promotersubstitution cassettes. Yeast 21, 947-962 (2004).
    • (2004) Yeast , vol.21 , pp. 947-962
    • Janke, C.1
  • 59
    • 0032519306 scopus 로고    scopus 로고
    • An activator/repressor dual system allows tight tetracycline-regulated gene expression in budding yeast
    • Belli, G., Gari, E., Piedrafita, L., Aldea, M. & Herrero, E. An activator/repressor dual system allows tight tetracycline-regulated gene expression in budding yeast. Nucleic Acids Res. 26, 942-947 (1998).
    • (1998) Nucleic Acids Res , vol.26 , pp. 942-947
    • Belli, G.1    Gari, E.2    Piedrafita, L.3    Aldea, M.4    Herrero, E.5
  • 60
    • 0038680253 scopus 로고    scopus 로고
    • Functional proteomic identification of DNA replication proteins by induced proteolysis in vivo
    • Kanemaki, M., Sanchez-Diaz, A., Gambus, A. & Labib, K. Functional proteomic identification of DNA replication proteins by induced proteolysis in vivo. Nature 423, 720-724 (2003).
    • (2003) Nature , vol.423 , pp. 720-724
    • Kanemaki, M.1    Sanchez-Diaz, A.2    Gambus, A.3    Labib, K.4
  • 61
    • 43049146539 scopus 로고    scopus 로고
    • Toward a comprehensive temperature-sensitive mutant repository of the essential genes of Saccharomyces cerevisiae
    • Ben-Aroya, S. et al. Toward a comprehensive temperature-sensitive mutant repository of the essential genes of Saccharomyces cerevisiae. Mol. Cell 30, 248-258 (2008).
    • (2008) Mol. Cell , vol.30 , pp. 248-258
    • Ben-Aroya, S.1
  • 62
    • 26844489762 scopus 로고    scopus 로고
    • Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile
    • Schuldiner, M. et al. Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile. Cell 123, 507-519 (2005).
    • (2005) Cell , vol.123 , pp. 507-519
    • Schuldiner, M.1
  • 63
    • 38149003098 scopus 로고    scopus 로고
    • Southwestern blotting in investigating transcriptional regulation
    • Siu, F.K., Lee, L.T. & Chow, B.K. Southwestern blotting in investigating transcriptional regulation. Nat. Protoc. 3, 51-58 (2008).
    • (2008) Nat. Protoc , vol.3 , pp. 51-58
    • Siu, F.K.1    Lee, L.T.2    Chow, B.K.3
  • 64
    • 0036275447 scopus 로고    scopus 로고
    • Getting started with yeast
    • Sherman, F. Getting started with yeast. Methods Enzymol. 350, 3-41 (2002).
    • (2002) Methods Enzymol , vol.350 , pp. 3-41
    • Sherman, F.1
  • 65
    • 0026664307 scopus 로고
    • Purification and biochemical characterization of a putative [6Fe-6S] prismane- cluster-containing protein from Desulfovibrio vulgaris (Hildenborough)
    • Pierik, A.J., Wolbert, R.B.G., Mutsaers, P.H.A., Hagen, W.R. & Veeger, C. Purification and biochemical characterization of a putative [6Fe-6S] prismane- cluster-containing protein from Desulfovibrio vulgaris (Hildenborough). Eur. J. Biochem. 206, 697-704 (1992).
    • (1992) Eur. J. Biochem , vol.206 , pp. 697-704
    • Pierik, A.J.1    Wolbert, R.B.G.2    Mutsaers, P.H.A.3    Hagen, W.R.4    Veeger, C.5
  • 66
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by lithium acetate/single- stranded carrier DNA/polyethylene glycol method
    • Gietz, R.D. & Woods, R.A. Transformation of yeast by lithium acetate/single- stranded carrier DNA/polyethylene glycol method. Methods Enzymol. 350, 87-96 (2002).
    • (2002) Methods Enzymol , vol.350 , pp. 87-96
    • Gietz, R.D.1    Woods, R.A.2
  • 67
    • 0015372792 scopus 로고
    • The counting efficiency for 55Fe and other E.C. nuclides in liquid scintillator solutions
    • Gibson, J.A. & Marshall, M. The counting efficiency for 55Fe and other E.C. nuclides in liquid scintillator solutions. Int. J. Appl. Radiat Isot. 23, 321-328 (1972).
    • (1972) Int. J. Appl. Radiat Isot , vol.23 , pp. 321-328
    • Gibson, J.A.1    Marshall, M.2
  • 68
    • 0037101845 scopus 로고    scopus 로고
    • The yeast frataxin homologue Yfh1p plays a specific role in the maturation of cellular Fe/S proteins. Hum. Mol
    • Muhlenhoff, U., Richhardt, N., Ristow, M., Kispal, G. & Lill, R. The yeast frataxin homologue Yfh1p plays a specific role in the maturation of cellular Fe/S proteins. Hum. Mol. Genet. 11, 2025-2036 (2002).
    • (2002) Genet , vol.11 , pp. 2025-2036
    • Muhlenhoff, U.1    Richhardt, N.2    Ristow, M.3    Kispal, G.4    Lill, R.5
  • 69
    • 3542993226 scopus 로고    scopus 로고
    • Superoxide inhibits 4Fe-4S clusterenzymes involved in amino acid biosynthesis. Cross-compartment protection by CuZn-superoxide dismutase
    • Wallace, M.A. etal. Superoxide inhibits 4Fe-4S clusterenzymes involved in amino acid biosynthesis. Cross-compartment protection by CuZn-superoxide dismutase. J. Biol. Chem. 279, 32055-32062 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 32055-32062
    • Wallace, M.A.1
  • 70
    • 0032448052 scopus 로고    scopus 로고
    • Regulation of expression of GLT1, the gene encoding glutamate synthase in Saccharomyces cerevisiae
    • Valenzuela, L., Ballario, P., Aranda, C., Filetici, P. & Gonzalez, A. Regulation of expression of GLT1, the gene encoding glutamate synthase in Saccharomyces cerevisiae. J. Bacteriol. 180, 3533-3540 (1998).
    • (1998) J. Bacteriol , vol.180 , pp. 3533-3540
    • Valenzuela, L.1    Ballario, P.2    Aranda, C.3    Filetici, P.4    Gonzalez, A.5
  • 71
    • 0343628833 scopus 로고    scopus 로고
    • Mitochondrial Isa2p plays a crucial role in the maturation of cellular iron-sulfur proteins
    • Pelzer, W. et al. Mitochondrial Isa2p plays a crucial role in the maturation of cellular iron-sulfur proteins. FEBS Lett. 476, 134-139 (2000).
    • (2000) FEBS Lett , vol.476 , pp. 134-139
    • Pelzer, W.1
  • 72
    • 0037155866 scopus 로고    scopus 로고
    • Mitochondrialferredoxin is required for heme A synthesis in Saccharomyces cerevisiae
    • Barros, M.H., Nobrega, F.G. & Tzagoloff, A. Mitochondrialferredoxin is required for heme A synthesis in Saccharomyces cerevisiae. J. Biol. Chem. 277, 9997-10002 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 9997-10002
    • Barros, M.H.1    Nobrega, F.G.2    Tzagoloff, A.3
  • 73
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford, M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72, 248-254 (1976).
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 74
    • 0035235373 scopus 로고    scopus 로고
    • Isolation and sub-fractionation of mitochondria from the yeast Saccharomyces cerevisiae
    • Diekert, K., deKroon, A.I.P.M., Kispal, G. & Lill, R. Isolation and sub-fractionation of mitochondria from the yeast Saccharomyces cerevisiae. Methods Cell Biol. 65, 37-51 (2001).
    • (2001) Methods Cell Biol , vol.65 , pp. 37-51
    • Diekert, K.1    Dekroon, A.I.P.M.2    Kispal, G.3    Lill, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.