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Volumn 30, Issue 3, 2005, Pages 133-141

Iron-sulfur-protein biogenesis in eukaryotes

Author keywords

[No Author keywords available]

Indexed keywords

IRON; PROTEIN; SULFUR;

EID: 14744294785     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2005.01.006     Document Type: Review
Times cited : (304)

References (86)
  • 1
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • H. Beinert Iron-sulfur clusters: nature's modular, multipurpose structures Science 277 1997 653 659
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1
  • 2
    • 0038670302 scopus 로고    scopus 로고
    • The interface between the biological and inorganic worlds: Iron-sulfur metalloclusters
    • D.C. Rees, and J.B. Howard The interface between the biological and inorganic worlds: iron-sulfur metalloclusters Science 300 2003 929 931
    • (2003) Science , vol.300 , pp. 929-931
    • Rees, D.C.1    Howard, J.B.2
  • 3
    • 27644466903 scopus 로고    scopus 로고
    • Iron-sulfur proteins
    • (Lennarz, W.J. and Lane, M.D., eds), Academic Press (in press)
    • Beinert, H. et al. Iron-sulfur proteins. In Encyclopedia of Biological Chemistry (Vol. 2) (Lennarz, W.J. and Lane, M.D., eds), Academic Press (in press)
    • Encyclopedia of Biological Chemistry , vol.2
    • Beinert, H.1
  • 4
    • 0037397764 scopus 로고    scopus 로고
    • Formation of iron-sulfur clusters in bacteria - An emerging field in bioinorganic chemistry
    • J. Frazzon, and D.R. Dean Formation of iron-sulfur clusters in bacteria - an emerging field in bioinorganic chemistry Curr. Opin. Chem. Biol. 7 2003 166 173
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 166-173
    • Frazzon, J.1    Dean, D.R.2
  • 5
    • 0036366682 scopus 로고    scopus 로고
    • Biosynthesis of the nitrogenase iron-molybdenum-cofactor from Azotobacter vinelandii
    • J. Frazzon, and D.R. Dean Biosynthesis of the nitrogenase iron-molybdenum-cofactor from Azotobacter vinelandii Met. Ions Biol. Syst. 39 2002 163 186
    • (2002) Met. Ions Biol. Syst. , vol.39 , pp. 163-186
    • Frazzon, J.1    Dean, D.R.2
  • 6
    • 0033777079 scopus 로고    scopus 로고
    • Nitrogenase: Standing at the crossroads
    • D.C. Rees, and J.B. Howard Nitrogenase: standing at the crossroads Curr. Opin. Chem. Biol. 4 2000 559 566
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 559-566
    • Rees, D.C.1    Howard, J.B.2
  • 7
    • 0032557666 scopus 로고    scopus 로고
    • Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii
    • L. Zheng Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii J. Biol. Chem. 273 1998 13264 13272
    • (1998) J. Biol. Chem. , vol.273 , pp. 13264-13272
    • Zheng, L.1
  • 8
    • 0034932337 scopus 로고    scopus 로고
    • DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide
    • M. Zheng DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide J. Bacteriol. 183 2001 4562 4570
    • (2001) J. Bacteriol. , vol.183 , pp. 4562-4570
    • Zheng, M.1
  • 9
    • 0037047411 scopus 로고    scopus 로고
    • A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids
    • Y. Takahashi, and U. Tokumoto A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids J. Biol. Chem. 277 2002 28380 28383
    • (2002) J. Biol. Chem. , vol.277 , pp. 28380-28383
    • Takahashi, Y.1    Tokumoto, U.2
  • 10
    • 0037415722 scopus 로고    scopus 로고
    • SufC: An unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress
    • L. Nachin SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress EMBO J. 22 2003 427 437
    • (2003) EMBO J. , vol.22 , pp. 427-437
    • Nachin, L.1
  • 11
    • 2442567822 scopus 로고    scopus 로고
    • A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli
    • F.W. Outten A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli Mol. Microbiol. 52 2004 861 872
    • (2004) Mol. Microbiol. , vol.52 , pp. 861-872
    • Outten, F.W.1
  • 12
    • 1942490139 scopus 로고    scopus 로고
    • An intestinal parasitic protist, Entamoeba histolytica, possesses a non-redundant nitrogen fixation-like system for iron-sulfur cluster assembly under anaerobic conditions
    • V. Ali An intestinal parasitic protist, Entamoeba histolytica, possesses a non-redundant nitrogen fixation-like system for iron-sulfur cluster assembly under anaerobic conditions J. Biol. Chem. 279 2004 16863 16874
    • (2004) J. Biol. Chem. , vol.279 , pp. 16863-16874
    • Ali, V.1
  • 13
    • 0034255836 scopus 로고    scopus 로고
    • Maturation of cellular Fe/S proteins: The essential function of mitochondria
    • R. Lill, and G. Kispal Maturation of cellular Fe/S proteins: the essential function of mitochondria Trends Biochem. Sci. 25 2000 352 356
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 352-356
    • Lill, R.1    Kispal, G.2
  • 14
    • 2942659075 scopus 로고    scopus 로고
    • AtNAP7 is a plastidic SufC-like ATP-binding cassette/ATPase essential for Arabidopsis embryogenesis
    • X.M. Xu, and S.G. Moller AtNAP7 is a plastidic SufC-like ATP-binding cassette/ATPase essential for Arabidopsis embryogenesis Proc. Natl. Acad. Sci. U. S. A. 101 2004 9143 9148
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 9143-9148
    • Xu, X.M.1    Moller, S.G.2
  • 15
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atm1p and Nfs1p are required for biogenesis of cytosolic Fe/S proteins
    • G. Kispal The mitochondrial proteins Atm1p and Nfs1p are required for biogenesis of cytosolic Fe/S proteins EMBO J. 18 1999 3981 3989
    • (1999) EMBO J. , vol.18 , pp. 3981-3989
    • Kispal, G.1
  • 16
    • 4344595102 scopus 로고    scopus 로고
    • Functional characterization of the eukaryotic cysteine desulfurase Nfs1p from Saccharomyces cerevisiae
    • U. Mühlenhoff Functional characterization of the eukaryotic cysteine desulfurase Nfs1p from Saccharomyces cerevisiae J. Biol. Chem. 279 2004 36906 36915
    • (2004) J. Biol. Chem. , vol.279 , pp. 36906-36915
    • Mühlenhoff, U.1
  • 17
    • 0032553445 scopus 로고    scopus 로고
    • Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly
    • J. Strain Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly J. Biol. Chem. 273 1998 31138 31144
    • (1998) J. Biol. Chem. , vol.273 , pp. 31138-31144
    • Strain, J.1
  • 18
    • 0033621156 scopus 로고    scopus 로고
    • Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
    • B. Schilke Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae Proc. Natl. Acad. Sci. U. S. A. 96 1999 10206 10211
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 10206-10211
    • Schilke, B.1
  • 19
    • 0032722872 scopus 로고    scopus 로고
    • Yeast mitochondrial protein Nfs1p coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution
    • J. Li 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
  • 20
    • 0034681155 scopus 로고    scopus 로고
    • NifS-directed assembly of a transient [2Fe-2S] cluster within the NifU protein
    • P. Yuvaniyama NifS-directed assembly of a transient [2Fe-2S] cluster within the NifU protein Proc. Natl. Acad. Sci. U. S. A. 97 2000 599 604
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 599-604
    • Yuvaniyama, P.1
  • 21
    • 0027450059 scopus 로고
    • Cysteine desulfurase acitivity indicates a role for NifS in metallocluster biosynthesis
    • L. Zheng Cysteine desulfurase acitivity indicates a role for NifS in metallocluster biosynthesis Proc. Natl. Acad. Sci. U. S. A. 90 1993 2754 2758
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 2754-2758
    • Zheng, L.1
  • 22
    • 0034255455 scopus 로고    scopus 로고
    • The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli
    • C.J. Schwartz The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli Proc. Natl. Acad. Sci. U. S. A. 97 2000 9009 9014
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 9009-9014
    • Schwartz, C.J.1
  • 23
    • 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
    • L. Loiseau Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase J. Biol. Chem. 278 2003 38352 38359
    • (2003) J. Biol. Chem. , vol.278 , pp. 38352-38359
    • Loiseau, L.1
  • 24
    • 0028265941 scopus 로고
    • Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product
    • L. Zheng Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product Biochemistry 33 1994 4714 4720
    • (1994) Biochemistry , vol.33 , pp. 4714-4720
    • Zheng, L.1
  • 25
    • 0034708346 scopus 로고    scopus 로고
    • Crystal structure of a NifS-like protein from Thermotoga maritima: Implications for iron-sulfur cluster assembly
    • J.T. Kaiser Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron-sulfur cluster assembly J. Mol. Biol. 297 2000 451 464
    • (2000) J. Mol. Biol. , vol.297 , pp. 451-464
    • Kaiser, J.T.1
  • 26
    • 0033544704 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae ISU1 and ISU2: Members of a well-conserved gene family for iron-sulfur cluster assembly
    • S.A. Garland Saccharomyces cerevisiae ISU1 and ISU2: members of a well-conserved gene family for iron-sulfur cluster assembly J. Mol. Biol. 294 1999 897 907
    • (1999) J. Mol. Biol. , vol.294 , pp. 897-907
    • Garland, S.A.1
  • 27
    • 0035823859 scopus 로고    scopus 로고
    • Sulfur transfer from IscS to IscU: The first step in iron-sulfur cluster biosynthesis
    • A.D. Smith Sulfur transfer from IscS to IscU: the first step in iron-sulfur cluster biosynthesis J. Am. Chem. Soc. 123 2001 11103 11104
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11103-11104
    • Smith, A.D.1
  • 28
    • 0035977015 scopus 로고    scopus 로고
    • Transfer of sulfur from IscS to IscU during Fe/S cluster assembly
    • H.D. Urbina Transfer of sulfur from IscS to IscU during Fe/S cluster assembly J. Biol. Chem. 276 2001 44521 44526
    • (2001) J. Biol. Chem. , vol.276 , pp. 44521-44526
    • Urbina, H.D.1
  • 29
    • 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
    • S. Kato 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 2002 5948 5952
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 5948-5952
    • Kato, S.1
  • 30
    • 0141737067 scopus 로고    scopus 로고
    • Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p
    • U. Mühlenhoff 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
  • 31
    • 7444266901 scopus 로고    scopus 로고
    • Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site
    • T.A. Ramelot Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site J. Mol. Biol. 344 2004 567 583
    • (2004) J. Mol. Biol. , vol.344 , pp. 567-583
    • Ramelot, T.A.1
  • 32
    • 2942602702 scopus 로고    scopus 로고
    • Bacterial IscU is a well folded and functional single domain protein
    • S. Adinolfi Bacterial IscU is a well folded and functional single domain protein Eur. J. Biochem. 271 2004 2093 2100
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2093-2100
    • Adinolfi, S.1
  • 33
    • 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
    • J.N. Agar IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU Biochemistry 39 2000 7856 7862
    • (2000) Biochemistry , vol.39 , pp. 7856-7862
    • Agar, J.N.1
  • 34
    • 0035138072 scopus 로고    scopus 로고
    • Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits
    • H. Puccio Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits Nat. Genet. 27 2001 181 186
    • (2001) Nat. Genet. , vol.27 , pp. 181-186
    • Puccio, H.1
  • 35
    • 0037101845 scopus 로고    scopus 로고
    • The yeast frataxin homologue Yfh1p plays a specific role in the maturation of cellular Fe/S proteins
    • U. Mühlenhoff The yeast frataxin homologue 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
    • Mühlenhoff, U.1
  • 36
    • 0036799372 scopus 로고    scopus 로고
    • A non-essential function for yeast frataxin in iron-sulfur cluster assembly
    • G. Duby A non-essential function for yeast frataxin in iron-sulfur cluster assembly Hum. Mol. Genet. 11 2002 2635 2643
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2635-2643
    • Duby, G.1
  • 37
    • 0037126057 scopus 로고    scopus 로고
    • Inhibition of Fe-S cluster biosynthesis decreases mitochondrial iron export: Evidence that Yfh1p affects Fe-S cluster synthesis
    • O.S. Chen Inhibition of Fe-S cluster biosynthesis decreases mitochondrial iron export: evidence that Yfh1p affects Fe-S cluster synthesis Proc. Natl. Acad. Sci. U. S. A. 99 2002 12321 12326
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12321-12326
    • Chen, O.S.1
  • 38
    • 9744248303 scopus 로고    scopus 로고
    • Iron-sulfur protein maturation in human cells: Evidence for a function of frataxin
    • O. Stehling Iron-sulfur protein maturation in human cells: evidence for a function of frataxin Hum. Mol. Genet. 13 2004 3007 3015
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 3007-3015
    • Stehling, O.1
  • 39
    • 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
    • H. Lange 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
  • 40
    • 9644279682 scopus 로고    scopus 로고
    • Iron-induced oligomerization of yeast frataxin homologue Yfh1 is dispensable in vivo
    • K. Aloria Iron-induced oligomerization of yeast frataxin homologue Yfh1 is dispensable in vivo EMBO Rep. 5 2004 1096 1101
    • (2004) EMBO Rep. , vol.5 , pp. 1096-1101
    • Aloria, K.1
  • 41
    • 0141623560 scopus 로고    scopus 로고
    • An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1
    • J. Gerber An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1 EMBO Rep. 4 2003 906 911
    • (2003) EMBO Rep. , vol.4 , pp. 906-911
    • Gerber, J.1
  • 42
    • 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
    • T. Yoon, and J.A. Cowan 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 2003 6078 6084
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6078-6084
    • Yoon, T.1    Cowan, J.A.2
  • 43
    • 0036603021 scopus 로고    scopus 로고
    • Friedreich ataxia: A paradigm for mitochondrial diseases
    • H. Puccio, and M. Koenig Friedreich ataxia: a paradigm for mitochondrial diseases Curr. Opin. Genet. Dev. 12 2002 272 277
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 272-277
    • Puccio, H.1    Koenig, M.2
  • 44
    • 0033953353 scopus 로고    scopus 로고
    • A mitochondrial ferredoxin is essential for biogenesis of intra- and extra-mitochondrial Fe/S proteins
    • H. Lange A mitochondrial ferredoxin is essential for biogenesis of intra- and extra-mitochondrial Fe/S proteins Proc. Natl. Acad. Sci. U. S. A. 97 2000 1050 1055
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 1050-1055
    • Lange, H.1
  • 45
    • 0035846961 scopus 로고    scopus 로고
    • Adrenodoxin reductase homolog (Arh1p) of yeast mitochondria required for iron homeostasis
    • J. Li Adrenodoxin reductase homolog (Arh1p) of yeast mitochondria required for iron homeostasis J. Biol. Chem. 276 2001 1503 1509
    • (2001) J. Biol. Chem. , vol.276 , pp. 1503-1509
    • Li, J.1
  • 46
    • 2242453224 scopus 로고    scopus 로고
    • Characterization of iron-sulfur protein assembly in isolated mitochondria: A requirement for ATP, NADH and reduced iron
    • U. Mühlenhoff Characterization of iron-sulfur protein assembly in isolated mitochondria: a requirement for ATP, NADH and reduced iron J. Biol. Chem. 277 2002 29810 29816
    • (2002) J. Biol. Chem. , vol.277 , pp. 29810-29816
    • Mühlenhoff, U.1
  • 47
    • 0037155866 scopus 로고    scopus 로고
    • Mitochondrial ferredoxin is required for heme a synthesis in Saccharomyces cerevisiae
    • M.H. Barros Mitochondrial ferredoxin is required for heme A synthesis in Saccharomyces cerevisiae J. Biol. Chem. 277 2002 9997 10002
    • (2002) J. Biol. Chem. , vol.277 , pp. 9997-10002
    • Barros, M.H.1
  • 48
    • 0042531776 scopus 로고    scopus 로고
    • Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis: Similarities to and differences from its bacterial counterpart
    • R. Dutkiewicz Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis: similarities to and differences from its bacterial counterpart J. Biol. Chem. 278 2003 29719 29727
    • (2003) J. Biol. Chem. , vol.278 , pp. 29719-29727
    • Dutkiewicz, R.1
  • 49
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes
    • M.T. Rodriguez-Manzaneque Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes Mol. Biol. Cell 13 2002 1109 1121
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1109-1121
    • Rodriguez-Manzaneque, M.T.1
  • 50
    • 0034608935 scopus 로고    scopus 로고
    • Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli
    • K.G. Hoff 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 2000 7790 7795
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 7790-7795
    • Hoff, K.G.1
  • 51
    • 0036809412 scopus 로고    scopus 로고
    • A specialized mitochondrial molecular chaperone system: A role in formation of Fe/S centers
    • E.A. Craig, and J. Marszalek A specialized mitochondrial molecular chaperone system: a role in formation of Fe/S centers Cell. Mol. Life Sci. 59 2002 1658 1665
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1658-1665
    • Craig, E.A.1    Marszalek, J.2
  • 52
    • 0141844533 scopus 로고    scopus 로고
    • Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system
    • K.G. Hoff Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system J. Biol. Chem. 278 2003 37582 37589
    • (2003) J. Biol. Chem. , vol.278 , pp. 37582-37589
    • Hoff, K.G.1
  • 53
    • 3142716203 scopus 로고    scopus 로고
    • Sequence-specific interaction between mitochondrial Fe-S scaffold protein Isu and Hsp70 Ssq1 is essential for their in vivo function
    • R. Dutkiewicz Sequence-specific interaction between mitochondrial Fe-S scaffold protein Isu and Hsp70 Ssq1 is essential for their in vivo function J. Biol. Chem. 279 2004 29167 29174
    • (2004) J. Biol. Chem. , vol.279 , pp. 29167-29174
    • Dutkiewicz, R.1
  • 54
    • 0034717132 scopus 로고    scopus 로고
    • Isa1p is a component of the mitochondrial machinery for maturation of cellular iron-sulfur proteins and requires conserved cysteine residues for function
    • A. Kaut Isa1p is a component of the mitochondrial machinery for maturation of cellular iron-sulfur proteins and requires conserved cysteine residues for function J. Biol. Chem. 275 2000 15955 15961
    • (2000) J. Biol. Chem. , vol.275 , pp. 15955-15961
    • Kaut, A.1
  • 55
    • 0343628833 scopus 로고    scopus 로고
    • Mitochondrial Isa2p plays a crucial role in the maturation of cellular iron-sulfur proteins
    • W. Pelzer Mitochondrial Isa2p plays a crucial role in the maturation of cellular iron-sulfur proteins FEBS Lett. 476 2000 134 139
    • (2000) FEBS Lett. , vol.476 , pp. 134-139
    • Pelzer, W.1
  • 56
    • 0034107324 scopus 로고    scopus 로고
    • Role of Saccharomyces cerevisiae ISA1 and ISA2 in iron homeostasis
    • L.T. Jensen, and V.C. Culotta 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
  • 57
    • 0035933791 scopus 로고    scopus 로고
    • Iron-sulfur cluster assembly: Characterization of IscA and evidence for a specific and functional complex with ferredoxin
    • S. Ollagnier-de-Choudens Iron-sulfur cluster assembly: characterization of IscA and evidence for a specific and functional complex with ferredoxin J. Biol. Chem. 276 2001 22604 22607
    • (2001) J. Biol. Chem. , vol.276 , pp. 22604-22607
    • Ollagnier-De-Choudens, S.1
  • 58
    • 0035923420 scopus 로고    scopus 로고
    • IscA, an alternate scaffold for Fe-S cluster biosynthesis
    • C. Krebs IscA, an alternate scaffold for Fe-S cluster biosynthesis Biochemistry 40 2001 14069 14080
    • (2001) Biochemistry , vol.40 , pp. 14069-14080
    • Krebs, C.1
  • 59
    • 0346727446 scopus 로고    scopus 로고
    • Crystal structure of the ancient, Fe-S scaffold IscA reveals a novel protein fold
    • P.W. Bilder Crystal structure of the ancient, Fe-S scaffold IscA reveals a novel protein fold Biochemistry 43 2004 133 139
    • (2004) Biochemistry , vol.43 , pp. 133-139
    • Bilder, P.W.1
  • 60
    • 1842526422 scopus 로고    scopus 로고
    • Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli
    • J.R. Cupp-Vickery Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli J. Mol. Biol. 338 2004 127 137
    • (2004) J. Mol. Biol. , vol.338 , pp. 127-137
    • Cupp-Vickery, J.R.1
  • 61
    • 4444317589 scopus 로고    scopus 로고
    • IscA mediates iron delivery for assembly of iron-sulfur clusters in IscU under the limited accessible free iron conditions
    • H. Ding IscA mediates iron delivery for assembly of iron-sulfur clusters in IscU under the limited accessible free iron conditions J. Biol. Chem. 279 2004 37499 37504
    • (2004) J. Biol. Chem. , vol.279 , pp. 37499-37504
    • Ding, H.1
  • 62
    • 0037570578 scopus 로고    scopus 로고
    • Iron-sulphur cluster assembly in plants: Distinct NFU proteins in mitochondria and plastids from Arabidopsis thaliana
    • S. Leon Iron-sulphur cluster assembly in plants: distinct NFU proteins in mitochondria and plastids from Arabidopsis thaliana Biochem. J. 371 2003 823 830
    • (2003) Biochem. J. , vol.371 , pp. 823-830
    • Leon, S.1
  • 63
    • 1842762970 scopus 로고    scopus 로고
    • The Arabidopsis chloroplastic NifU-like protein CnfU, which can act as an iron-sulfur cluster scaffold protein, is required for biogenesis of ferredoxin and photosystem I
    • T. Yabe The Arabidopsis chloroplastic NifU-like protein CnfU, which can act as an iron-sulfur cluster scaffold protein, is required for biogenesis of ferredoxin and photosystem I Plant Cell 16 2004 993 1007
    • (2004) Plant Cell , vol.16 , pp. 993-1007
    • Yabe, T.1
  • 64
    • 0034725582 scopus 로고    scopus 로고
    • Transfer of iron-sulfur cluster from NifU to apoferredoxin
    • K. Nishio, and M. Nakai Transfer of iron-sulfur cluster from NifU to apoferredoxin J. Biol. Chem. 275 2000 22615 22618
    • (2000) J. Biol. Chem. , vol.275 , pp. 22615-22618
    • Nishio, K.1    Nakai, M.2
  • 65
    • 0035896587 scopus 로고    scopus 로고
    • Nuclear localization of yeast Nfs1p is required for cell survival
    • Y. Nakai Nuclear localization of yeast Nfs1p is required for cell survival J. Biol. Chem. 276 2001 8314 8320
    • (2001) J. Biol. Chem. , vol.276 , pp. 8314-8320
    • Nakai, Y.1
  • 66
    • 1842582668 scopus 로고    scopus 로고
    • Yeast Nfs1p is involved in thio-modification of both mitochondrial and cytoplasmic tRNAs
    • Y. Nakai Yeast Nfs1p is involved in thio-modification of both mitochondrial and cytoplasmic tRNAs J. Biol. Chem. 279 2004 12363 12368
    • (2004) J. Biol. Chem. , vol.279 , pp. 12363-12368
    • Nakai, Y.1
  • 67
    • 2442707887 scopus 로고    scopus 로고
    • The yeast scaffold proteins Isu1p and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteins
    • J. Gerber The yeast scaffold proteins Isu1p and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteins Mol. Cell. Biol. 24 2004 4848 4857
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4848-4857
    • Gerber, J.1
  • 68
    • 0041691163 scopus 로고    scopus 로고
    • Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster
    • W.H. Tong Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster Proc. Natl. Acad. Sci. U. S. A. 100 2003 9762 9767
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 9762-9767
    • Tong, W.H.1
  • 69
    • 0034329310 scopus 로고    scopus 로고
    • Human ABC7 transporter: Gene structure and mutation causing X-linked sideroblastic anemia with ataxia (XLSA/A) with disruption of cytosolic iron-sulfur protein maturation
    • S. Bekri Human ABC7 transporter: gene structure and mutation causing X-linked sideroblastic anemia with ataxia (XLSA/A) with disruption of cytosolic iron-sulfur protein maturation Blood 96 2000 3256 3264
    • (2000) Blood , vol.96 , pp. 3256-3264
    • Bekri, S.1
  • 70
    • 0035104780 scopus 로고    scopus 로고
    • A mutation of the mitochondrial ABC transporter Sta1 leads to dwarfism and chlorosis in the Arabidopsis mutant starik
    • S. Kushnir A mutation of the mitochondrial ABC transporter Sta1 leads to dwarfism and chlorosis in the Arabidopsis mutant starik Plant Cell 13 2001 89 100
    • (2001) Plant Cell , vol.13 , pp. 89-100
    • Kushnir, S.1
  • 71
    • 33746912629 scopus 로고    scopus 로고
    • ABC transporters in mitochondria
    • B.I. Holland Academic Press*et al.
    • R. Lill, and G. Kispal ABC transporters in mitochondria B.I. Holland ABC Proteins: From Bacteria to Man 2003 Academic Press 515 531
    • (2003) ABC Proteins: From Bacteria to Man , pp. 515-531
    • Lill, R.1    Kispal, G.2
  • 72
    • 4544321137 scopus 로고    scopus 로고
    • The cell's cookbook for iron-sulfur clusters: Recipes for fool's gold?
    • J. Balk, and R. Lill 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
  • 73
    • 0034866458 scopus 로고    scopus 로고
    • An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins
    • H. Lange An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins EMBO Rep. 2 2001 715 720
    • (2001) EMBO Rep. , vol.2 , pp. 715-720
    • Lange, H.1
  • 74
    • 0037178843 scopus 로고    scopus 로고
    • Maturation of cytosolic iron-sulfur proteins requires glutathione
    • K. Sipos Maturation of cytosolic iron-sulfur proteins requires glutathione J. Biol. Chem. 277 2002 26944 26949
    • (2002) J. Biol. Chem. , vol.277 , pp. 26944-26949
    • Sipos, K.1
  • 75
    • 3142667831 scopus 로고    scopus 로고
    • Transcription of the yeast iron regulon responds not directly to iron but rather to iron-sulfur cluster biosynthesis
    • O.S. Chen Transcription of the yeast iron regulon responds not directly to iron but rather to iron-sulfur cluster biosynthesis J. Biol. Chem. 279 2004 29513 29518
    • (2004) J. Biol. Chem. , vol.279 , pp. 29513-29518
    • Chen, O.S.1
  • 76
    • 0141848663 scopus 로고    scopus 로고
    • A novel eukaryotic factor for cytosolic Fe-S cluster assembly
    • A. Roy A novel eukaryotic factor for cytosolic Fe-S cluster assembly EMBO J. 22 2003 4826 4835
    • (2003) EMBO J. , vol.22 , pp. 4826-4835
    • Roy, A.1
  • 77
    • 0037216551 scopus 로고    scopus 로고
    • Lack of the ApbC or ApbE protein results in a defect in Fe-S cluster metabolism in Salmonella enterica serovar Typhimurium
    • E. Skovran, and D.M. Downs Lack of the ApbC or ApbE protein results in a defect in Fe-S cluster metabolism in Salmonella enterica serovar Typhimurium J. Bacteriol. 185 2003 98 106
    • (2003) J. Bacteriol. , vol.185 , pp. 98-106
    • Skovran, E.1    Downs, D.M.2
  • 78
    • 2942565619 scopus 로고    scopus 로고
    • The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins
    • J. Balk The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins EMBO J. 23 2004 2105 2115
    • (2004) EMBO J. , vol.23 , pp. 2105-2115
    • Balk, J.1
  • 79
    • 1842429937 scopus 로고    scopus 로고
    • Ancient invasions: From endosymbionts to organelles
    • S.D. Dyall Ancient invasions: from endosymbionts to organelles Science 304 2004 253 257
    • (2004) Science , vol.304 , pp. 253-257
    • Dyall, S.D.1
  • 80
    • 0035936144 scopus 로고    scopus 로고
    • Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi
    • M.D. Katinka Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi Nature 414 2001 450 453
    • (2001) Nature , vol.414 , pp. 450-453
    • Katinka, M.D.1
  • 81
    • 0344633597 scopus 로고    scopus 로고
    • Mitochondrial remnant organelles of Giardia function in iron-sulphur protein maturation
    • J. Tovar Mitochondrial remnant organelles of Giardia function in iron-sulphur protein maturation Nature 426 2003 172 176
    • (2003) Nature , vol.426 , pp. 172-176
    • Tovar, J.1
  • 82
    • 3142746681 scopus 로고    scopus 로고
    • Mitochondrial-type assembly of FeS centers in the hydrogenosomes of the amitochondriate eukaryote Trichomonas vaginalis
    • R. Sutak Mitochondrial-type assembly of FeS centers in the hydrogenosomes of the amitochondriate eukaryote Trichomonas vaginalis Proc. Natl. Acad. Sci. U. S. A. 101 2004 10368 10373
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 10368-10373
    • Sutak, R.1
  • 83
    • 20044391418 scopus 로고    scopus 로고
    • Biogenesis of ribosomes requires the essential iron-sulfur protein Rli1p and mitochondria
    • Kispal, G. et al. (2005) Biogenesis of ribosomes requires the essential iron-sulfur protein Rli1p and mitochondria. EMBO J. 24, 589-598
    • (2005) EMBO J. , vol.24 , pp. 589-598
    • Kispal, G.1
  • 84
    • 14744301484 scopus 로고    scopus 로고
    • Functional link between ribosome formation and biogenesis of iron-sulfur proteins
    • Yarunin, A. et al. (2005) Functional link between ribosome formation and biogenesis of iron-sulfur proteins. EMBO J. 24, 580-588
    • (2005) EMBO J. , vol.24 , pp. 580-588
    • Yarunin, A.1
  • 85
    • 0036495241 scopus 로고    scopus 로고
    • Iron hydrogenases - Ancient enzymes in modern eukaryotes
    • D.S. Horner Iron hydrogenases - ancient enzymes in modern eukaryotes Trends Biochem. Sci. 27 2002 148 153
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 148-153
    • Horner, D.S.1
  • 86
    • 0037173571 scopus 로고    scopus 로고
    • Fe-only hydrogenases: Structure, function and evolution
    • Y. Nicolet Fe-only hydrogenases: structure, function and evolution J. Inorg. Biochem. 91 2002 1 8
    • (2002) J. Inorg. Biochem. , vol.91 , pp. 1-8
    • Nicolet, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.