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Volumn 80, Issue , 2007, Pages 261-280

Methods for Studying Iron Metabolism in Yeast Mitochondria

Author keywords

[No Author keywords available]

Indexed keywords

2 (5 NITRO 2 PYRIDYLAZO) 5 (N PROPYL N SULFOPROPYLAMINO)PHENOL; 2-(5-NITRO-2-PYRIDYLAZO)-5-(N-PROPYL-N-SULFOPROPYLAMINO)PHENOL; AZO COMPOUND; BATHOPHENANTHROLINE; HEME; ION EXCHANGE RESIN; IRON; IRON SULFUR PROTEIN; PHENANTHROLINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 34147109189     PISSN: 0091679X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0091-679X(06)80013-0     Document Type: Review
Times cited : (34)

References (31)
  • 1
    • 4544321137 scopus 로고    scopus 로고
    • The cell's cookbook for iron-sulfur clusters: Recipes for fool's gold?
    • Balk J., and Lill R. The cell'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
  • 2
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert H., Holm R.H., and Munck 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    Munck, E.3
  • 3
    • 0035235373 scopus 로고    scopus 로고
    • Isolation and subfractionation of mitochondria from the yeast Saccharomyces cerevisiae
    • Diekert K., de Kroon A.I., 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.2    Kispal, G.3    Lill, R.4
  • 5
    • 0042703890 scopus 로고    scopus 로고
    • An in vivo dual-luciferase assay system for studying translational recoding in the yeast Saccharomyces cerevisiae
    • Harger J.W., and Dinman J.D. An in vivo dual-luciferase assay system for studying translational recoding in the yeast Saccharomyces cerevisiae. RNA 9 (2003) 1019-1024
    • (2003) RNA , vol.9 , pp. 1019-1024
    • Harger, J.W.1    Dinman, J.D.2
  • 6
    • 0034107324 scopus 로고    scopus 로고
    • Role of Saccharomyces cerevisiae ISA1 and ISA2 in iron homeostasis
    • Jensen L.T., and Culotta V.C. Role of Saccharomyces cerevisiae ISA1 and ISA2 in iron homeostasis. Mol. Cell. Biol. 20 (2000) 3918-3927
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3918-3927
    • Jensen, L.T.1    Culotta, V.C.2
  • 7
    • 34147144155 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • Johnson D., and Dean D.R. Structure, function, and formation of biological iron-sulfur clusters. Annu. Rev. Biochem. 19 (2004) 19
    • (2004) Annu. Rev. Biochem. , vol.19 , pp. 19
    • Johnson, D.1    Dean, D.R.2
  • 8
    • 0030608677 scopus 로고    scopus 로고
    • The ABC transporter Atm1p is required for mitochondrial iron homeostasis
    • Kispal G., Csere P., Guiard B., and Lill R. The ABC transporter Atm1p is required for mitochondrial iron homeostasis. FEBS Lett. 418 (1997) 346-350
    • (1997) FEBS Lett. , vol.418 , pp. 346-350
    • Kispal, G.1    Csere, P.2    Guiard, B.3    Lill, R.4
  • 9
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
    • Kispal G., Csere P., Prohl C., and Lill R. The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins. EMBO J. 18 (1999) 3981-3989
    • (1999) EMBO J. , vol.18 , pp. 3981-3989
    • Kispal, G.1    Csere, P.2    Prohl, C.3    Lill, R.4
  • 11
    • 3142722152 scopus 로고    scopus 로고
    • The heme synthesis defect of mutants impaired in mitochondrial iron-sulfur protein biogenesis is caused by reversible inhibition of ferrochelatase
    • Lange H., Muhlenhoff U., Denzel M., Kispal G., and Lill R. The heme synthesis defect of mutants impaired in mitochondrial iron-sulfur protein biogenesis is caused by reversible inhibition of ferrochelatase. J. Biol. Chem. 279 (2004) 29101-29108
    • (2004) J. Biol. Chem. , vol.279 , pp. 29101-29108
    • Lange, H.1    Muhlenhoff, U.2    Denzel, M.3    Kispal, G.4    Lill, R.5
  • 12
    • 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. Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution. J. Biol. Chem. 274 (1999) 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
  • 13
    • 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
  • 14
    • 33751177803 scopus 로고    scopus 로고
    • Iron-sulfur protein biogenesis in eukaryotes: Components and mechanisms
    • Lill R., and Mühlenhoff U. Iron-sulfur protein biogenesis in eukaryotes: Components and mechanisms. Annu. Rev. Cell Dev. Biol. 22 (2006) 457-486
    • (2006) Annu. Rev. Cell Dev. Biol. , vol.22 , pp. 457-486
    • Lill, R.1    Mühlenhoff, U.2
  • 15
    • 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., and Herrmann J.M. The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron-sulfur clusters in mitochondria. J. Mol. Biol. 307 (2001) 815-825
    • (2001) J. Mol. Biol. , vol.307 , pp. 815-825
    • Lutz, T.1    Westermann, B.2    Neupert, W.3    Herrmann, J.M.4
  • 16
    • 0023868794 scopus 로고
    • A sensitive, direct colorimetric assay of serum iron using the chromogen, nitro-PAPS
    • Makino T., Kiyonaga M., and Kina K. A sensitive, direct colorimetric assay of serum iron using the chromogen, nitro-PAPS. Clin. Chim. Acta 171 (1988) 19-27
    • (1988) Clin. Chim. Acta , vol.171 , pp. 19-27
    • Makino, T.1    Kiyonaga, M.2    Kina, K.3
  • 17
    • 25144443146 scopus 로고    scopus 로고
    • Dual luciferase assay system for rapid assessment of gene expression in Saccharomyces cerevisiae
    • McNabb D.S., Reed R., and Marciniak R.A. Dual luciferase assay system for rapid assessment of gene expression in Saccharomyces cerevisiae. Eukaryot. Cell 4 (2005) 1539-1549
    • (2005) Eukaryot. Cell , vol.4 , pp. 1539-1549
    • McNabb, D.S.1    Reed, R.2    Marciniak, R.A.3
  • 18
    • 0022490417 scopus 로고
    • High-yield chemical assembly of [2Fe-2X] (X = S, Se) clusters into spinach apoferredoxin, product characterisation by Raman spectroscopy
    • Meyer J., Moulis J.M., and Lutz M. High-yield chemical assembly of [2Fe-2X] (X = S, Se) clusters into spinach apoferredoxin, product characterisation by Raman spectroscopy. Biochim. Biophys. Acta 871 (1986) 243-249
    • (1986) Biochim. Biophys. Acta , vol.871 , pp. 243-249
    • Meyer, J.1    Moulis, J.M.2    Lutz, M.3
  • 19
    • 2242453224 scopus 로고    scopus 로고
    • Characterization of iron-sulfur protein assembly in isolated mitochondria. A requirement for ATP, NADH, and reduced iron
    • . Epub 2002 Jun 13
    • Muhlenhoff U., Richhardt N., Gerber J., and Lill R. Characterization of iron-sulfur protein assembly in isolated mitochondria. A requirement for ATP, NADH, and reduced iron. J. Biol. Chem. 277 (2002) 29810-29816 . Epub 2002 Jun 13
    • (2002) J. Biol. Chem. , vol.277 , pp. 29810-29816
    • Muhlenhoff, U.1    Richhardt, N.2    Gerber, J.3    Lill, R.4
  • 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. The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins. Hum. Mol. Genet. 11 (2002) 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
    • 1242277806 scopus 로고    scopus 로고
    • Metal-responsive transcription factors that regulate iron, zinc, and copper homeostasis in eukaryotic cells
    • Rutherford J.C., and Bird A.J. Metal-responsive transcription factors that regulate iron, zinc, and copper homeostasis in eukaryotic cells. Eukaryot. Cell 3 (2004) 1-13
    • (2004) Eukaryot. Cell , vol.3 , pp. 1-13
    • Rutherford, J.C.1    Bird, A.J.2
  • 22
    • 0042847393 scopus 로고    scopus 로고
    • Aft1p and Aft2p mediate iron-responsive gene expression in yeast through related promoter elements
    • Rutherford J.C., Jaron S., and Winge D.R. Aft1p and Aft2p mediate iron-responsive gene expression in yeast through related promoter elements. J. Biol. Chem. 278 (2003) 27636-27643
    • (2003) J. Biol. Chem. , vol.278 , pp. 27636-27643
    • Rutherford, J.C.1    Jaron, S.2    Winge, D.R.3
  • 23
    • 15444371876 scopus 로고    scopus 로고
    • Activation of the iron regulon by the yeast Aft1/Aft2 transcription factors depends on mitochondrial but not cytosolic iron-sulfur protein biogenesis
    • Rutherford J.C., Ojeda L., Balk J., Muhlenhoff U., Lill R., and Winge D.R. Activation of the iron regulon by the yeast Aft1/Aft2 transcription factors depends on mitochondrial but not cytosolic iron-sulfur protein biogenesis. J. Biol. Chem. 280 (2005) 10135-10140
    • (2005) J. Biol. Chem. , vol.280 , pp. 10135-10140
    • Rutherford, J.C.1    Ojeda, L.2    Balk, J.3    Muhlenhoff, U.4    Lill, R.5    Winge, D.R.6
  • 25
    • 0036275447 scopus 로고    scopus 로고
    • Getting started with yeast
    • Sherman F. Getting started with yeast. Methods Enzymol. 350 (2002) 3-41
    • (2002) Methods Enzymol. , vol.350 , pp. 3-41
    • Sherman, F.1
  • 26
    • 0000619617 scopus 로고
    • Plastid import and iron-sulphur cluster assembly of photosynthetic and nonphotosynthetic ferredoxin isoproteins in maize
    • Suzuki S., Izumihara K., and Hase T. Plastid import and iron-sulphur cluster assembly of photosynthetic and nonphotosynthetic ferredoxin isoproteins in maize. Plant Physiol. 97 (1991) 375-380
    • (1991) Plant Physiol. , vol.97 , pp. 375-380
    • Suzuki, S.1    Izumihara, K.2    Hase, T.3
  • 28
    • 0002949415 scopus 로고
    • Formation of the Fe-S cluster of ferredoxin in lysed spinach chloroplasts
    • Takahashi Y., Mitsui A., and Matsubara H. Formation of the Fe-S cluster of ferredoxin in lysed spinach chloroplasts. Plant Physiol. 95 (1991) 97-103
    • (1991) Plant Physiol. , vol.95 , pp. 97-103
    • Takahashi, Y.1    Mitsui, A.2    Matsubara, H.3
  • 29
    • 0032560478 scopus 로고    scopus 로고
    • A member of the Ran-binding protein family, Yrb2p, is involved in nuclear protein export
    • Taura T., Krebber H., and Silver P.A. A member of the Ran-binding protein family, Yrb2p, is involved in nuclear protein export. Proc. Natl. Acad. Sci. USA 95 (1998) 7427-7432
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7427-7432
    • Taura, T.1    Krebber, H.2    Silver, P.A.3
  • 30
    • 0037166279 scopus 로고    scopus 로고
    • Subcellular localization of Aft1 transcription factor responds to iron status in Saccharomyces cerevisiae
    • Yamaguchi-Iwai Y., Ueta R., Fukunaka A., and Sasaki R. Subcellular localization of Aft1 transcription factor responds to iron status in Saccharomyces cerevisiae. J. Biol. Chem. 277 (2002) 18914-18918
    • (2002) J. Biol. Chem. , vol.277 , pp. 18914-18918
    • Yamaguchi-Iwai, Y.1    Ueta, R.2    Fukunaka, A.3    Sasaki, R.4
  • 31
    • 14744301484 scopus 로고    scopus 로고
    • Functional link between ribosome formation and biogenesis of iron-sulfur proteins
    • Yarunin A., Panse V.G., Petfalski E., Dez C., Tollervey D., and Hurt E.C. Functional link between ribosome formation and biogenesis of iron-sulfur proteins. EMBO J. 24 (2005) 580-588
    • (2005) EMBO J. , vol.24 , pp. 580-588
    • Yarunin, A.1    Panse, V.G.2    Petfalski, E.3    Dez, C.4    Tollervey, D.5    Hurt, E.C.6


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