메뉴 건너뛰기




Volumn 3, Issue 3, 2006, Pages 199-210

Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; IRON REGULATORY FACTOR; IRON SULFUR PROTEIN; PROTEIN ISCU; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 33644623262     PISSN: 15504131     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cmet.2006.02.003     Document Type: Article
Times cited : (262)

References (63)
  • 1
    • 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 C. Krebs J. Frazzon B.H. Huynh D.R. Dean M.K. Johnson 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    Krebs, C.2    Frazzon, J.3    Huynh, B.H.4    Dean, D.R.5    Johnson, M.K.6
  • 3
    • 0038725739 scopus 로고    scopus 로고
    • Iron regulatory proteins as NO signal transducers
    • C. Bouton J.C. Drapiers Iron regulatory proteins as NO signal transducers Sci. STKE 182 2003 pe17
    • (2003) Sci. STKE , vol.182 , pp. 17
    • Bouton, C.1    Drapiers, J.C.2
  • 4
    • 0033618254 scopus 로고    scopus 로고
    • Human cytoplasmic aconitase (Iron regulatory protein 1) is converted into its [3Fe-4S] form by hydrogen peroxide in vitro but is not activated for iron-responsive element binding
    • X. Brazzolotto J. Gaillard K. Pantopoulos M.W. Hentze J.M. Moulis Human cytoplasmic aconitase (Iron regulatory protein 1) is converted into its [3Fe-4S] form by hydrogen peroxide in vitro but is not activated for iron-responsive element binding J. Biol. Chem. 274 1999 21625-21630
    • (1999) J. Biol. Chem. , vol.274 , pp. 21625-21630
    • Brazzolotto, X.1    Gaillard, J.2    Pantopoulos, K.3    Hentze, M.W.4    Moulis, J.M.5
  • 5
    • 0346365099 scopus 로고    scopus 로고
    • Redox-dependent modulation of aconitase activity in intact mitochondria
    • A.L. Bulteau M. Ikeda-Saito L.I. Szweda Redox-dependent modulation of aconitase activity in intact mitochondria Biochemistry 42 2003 14846-14855
    • (2003) Biochemistry , vol.42 , pp. 14846-14855
    • Bulteau, A.L.1    Ikeda-Saito, M.2    Szweda, L.I.3
  • 6
    • 0037096190 scopus 로고    scopus 로고
    • The iron regulatory proteins: Targets and modulators of free radical reactions and oxidative damage
    • G. Cairo S. Recalcati A. Pietrangelo G. Minotti The iron regulatory proteins: Targets and modulators of free radical reactions and oxidative damage Free Radic. Biol. Med. 32 2002 1237-1243
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1237-1243
    • Cairo, G.1    Recalcati, S.2    Pietrangelo, A.3    Minotti, G.4
  • 7
    • 0035827697 scopus 로고    scopus 로고
    • Modulation of cellular iron metabolism by hydrogen peroxide. Effects of H2O2 on the expression and function of iron-responsive element-containing mRNAs in B6 fibroblasts
    • A. Caltagirone G. Weiss K. Pantopoulos Modulation of cellular iron metabolism by hydrogen peroxide. Effects of H2O2 on the expression and function of iron-responsive element-containing mRNAs in B6 fibroblasts J. Biol. Chem. 276 2001 19738-19745
    • (2001) J. Biol. Chem. , vol.276 , pp. 19738-19745
    • Caltagirone, A.1    Weiss, G.2    Pantopoulos, K.3
  • 8
    • 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 B. Schilke S. Cheng H. Knieszner E.A. Craig J. Marszalek 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    Schilke, B.2    Cheng, S.3    Knieszner, H.4    Craig, E.A.5    Marszalek, J.6
  • 9
    • 0036351317 scopus 로고    scopus 로고
    • Analysis of gene function in somatic mammalian cells using small interfering RNAs
    • S.M. Elbashir J. Harborth K. Weber T. Tuschl Analysis of gene function in somatic mammalian cells using small interfering RNAs Methods 26 2002 199-213
    • (2002) Methods , vol.26 , pp. 199-213
    • Elbashir, S.M.1    Harborth, J.2    Weber, K.3    Tuschl, T.4
  • 10
    • 0035896520 scopus 로고    scopus 로고
    • Mitochondrial control of iron homeostasis. A genome wide analysis of gene expression in a yeast frataxin-deficient strain
    • F. Foury D. Talibi Mitochondrial control of iron homeostasis. A genome wide analysis of gene expression in a yeast frataxin-deficient strain J. Biol. Chem. 276 2001 7762-7768
    • (2001) J. Biol. Chem. , vol.276 , pp. 7762-7768
    • Foury, F.1    Talibi, D.2
  • 11
    • 0030993117 scopus 로고    scopus 로고
    • Superoxide-driven aconitase FE-S center cycling
    • P.R. Gardner Superoxide-driven aconitase FE-S center cycling Biosci. Rep. 17 1997 33-42
    • (1997) Biosci. Rep. , vol.17 , pp. 33-42
    • Gardner, P.R.1
  • 12
    • 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 K. Hoff L.E. Vickery V.C. Culotta 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    Hoff, K.2    Vickery, L.E.3    Culotta, V.C.4
  • 13
    • 0141623560 scopus 로고    scopus 로고
    • An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1
    • J. Gerber U. Muhlenhoff R. Lill 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    Muhlenhoff, U.2    Lill, R.3
  • 14
    • 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 K. Neumann C. Prohl U. Muhlenhoff R. Lill 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    Neumann, K.2    Prohl, C.3    Muhlenhoff, U.4    Lill, R.5
  • 15
    • 0141890273 scopus 로고    scopus 로고
    • Oxygen and iron regulation of iron regulatory protein 2
    • E.S. Hanson M.L. Rawlins E.A. Leibold Oxygen and iron regulation of iron regulatory protein 2 J. Biol. Chem. 278 2003 40337-40342
    • (2003) J. Biol. Chem. , vol.278 , pp. 40337-40342
    • Hanson, E.S.1    Rawlins, M.L.2    Leibold, E.A.3
  • 16
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • M.W. Hentze M.U. Muckenthaler N.C. Andrews Balancing acts: Molecular control of mammalian iron metabolism Cell 117 2004 285-297
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 18
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • D.C. Johnson D.R. Dean A.D. Smith M.K. Johnson Structure, function, and formation of biological iron-sulfur clusters Annu. Rev. Biochem. 74 2005 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
  • 19
    • 0027081042 scopus 로고
    • Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein
    • M.C. Kennedy L. Mende-Mueller G.A. Blondin H. Beinert Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein Proc. Natl. Acad. Sci. USA 89 1992 11730-11734
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11730-11734
    • Kennedy, M.C.1    Mende-Mueller, L.2    Blondin, G.A.3    Beinert, H.4
  • 20
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
    • G. Kispal P. Csere C. Prohl R. Lill 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
  • 21
    • 0032540929 scopus 로고    scopus 로고
    • Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis
    • S.A. Knight N.B. Sepuri D. Pain A. Dancis Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis J. Biol. Chem. 273 1998 18389-18393
    • (1998) J. Biol. Chem. , vol.273 , pp. 18389-18393
    • Knight, S.A.1    Sepuri, N.B.2    Pain, D.3    Dancis, A.4
  • 23
    • 0032245425 scopus 로고    scopus 로고
    • Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization
    • T. Land T.A. Rouault Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization Mol. Cell 2 1998 807-815
    • (1998) Mol. Cell , vol.2 , pp. 807-815
    • Land, T.1    Rouault, T.A.2
  • 24
    • 0033953353 scopus 로고    scopus 로고
    • A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins
    • H. Lange A. Kaut G. Kispal R. Lill A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins Proc. Natl. Acad. Sci. USA 97 2000 1050-1055
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1050-1055
    • Lange, H.1    Kaut, A.2    Kispal, G.3    Lill, R.4
  • 25
    • 0035138456 scopus 로고    scopus 로고
    • Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice
    • T. LaVaute S. Smith S. Cooperman K. Iwai W. Land E. Meyron-Holtz S.K. Drake G. Miller M. Abu-Asab M. Tsokos et. al. Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice Nat. Genet. 27 2001 209-214
    • (2001) Nat. Genet. , vol.27 , pp. 209-214
    • LaVaute, T.1    Smith, S.2    Cooperman, S.3    Iwai, K.4    Land, W.5    Meyron-Holtz, E.6    Drake, S.K.7    Miller, G.8    Abu-Asab, M.9    Tsokos, M.10
  • 26
    • 0037570578 scopus 로고    scopus 로고
    • Iron-sulphur cluster assembly in plants: Distinct NFU proteins in mitochondria and plastids from Arabidopsis thaliana
    • S. Leon B. Touraine C. Ribot J.F. Briat S. Lobreaux 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    Touraine, B.2    Ribot, C.3    Briat, J.F.4    Lobreaux, S.5
  • 27
    • 0032722872 scopus 로고    scopus 로고
    • Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution
    • J. Li M. Kogan S.A.B. Knight D. Pain A. Dancis 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.B.3    Pain, D.4    Dancis, A.5
  • 28
    • 14744294785 scopus 로고    scopus 로고
    • Iron-sulfur-protein biogenesis in eukaryotes
    • R. Lill U. Muhlenhoff 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    Muhlenhoff, U.2
  • 29
    • 10844282789 scopus 로고    scopus 로고
    • Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo
    • E.G. Meyron-Holtz M.C. Ghosh T.A. Rouault Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo Science 306 2004 2087-2090
    • (2004) Science , vol.306 , pp. 2087-2090
    • Meyron-Holtz, E.G.1    Ghosh, M.C.2    Rouault, T.A.3
  • 32
    • 0035896587 scopus 로고    scopus 로고
    • Nuclear localization of yeast Nfs1p is required for cell survival
    • Y. Nakai M. Nakai H. Hayashi H. Kagamiyama 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    Nakai, M.2    Hayashi, H.3    Kagamiyama, H.4
  • 33
    • 14944387002 scopus 로고    scopus 로고
    • Iron trafficking in the mitochondrion: Novel pathways revealed by disease
    • I. Napier P. Ponka D.R. Richardson Iron trafficking in the mitochondrion: Novel pathways revealed by disease Blood 105 2005 1867-1874
    • (2005) Blood , vol.105 , pp. 1867-1874
    • Napier, I.1    Ponka, P.2    Richardson, D.R.3
  • 34
    • 0034725582 scopus 로고    scopus 로고
    • Transfer of iron-sulfur cluster from NifU to apoferredoxin
    • K. Nishio 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
  • 35
    • 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 T. Mattioli Y. Takahashi M. Fontecave 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    Mattioli, T.2    Takahashi, Y.3    Fontecave, M.4
  • 37
    • 1842608845 scopus 로고    scopus 로고
    • Iron metabolism and the IRE/IRP regulatory system: An update
    • K. Pantopoulos Iron metabolism and the IRE/IRP regulatory system: An update Ann. N Y Acad. Sci. 1012 2004 1-13
    • (2004) Ann. N Y Acad. Sci. , vol.1012 , pp. 1-13
    • Pantopoulos, K.1
  • 38
    • 0029055581 scopus 로고
    • Rapid responses to oxidative stress mediated by iron regulatory protein
    • K. Pantopoulos M.W. Hentze Rapid responses to oxidative stress mediated by iron regulatory protein EMBO J. 14 1995 2917-2924
    • (1995) EMBO J. , vol.14 , pp. 2917-2924
    • Pantopoulos, K.1    Hentze, M.W.2
  • 39
    • 11844257593 scopus 로고    scopus 로고
    • Coordinated remodeling of cellular metabolism during iron deficiency through targeted mRNA degradation
    • S. Puig E. Askeland D.J. Thiele Coordinated remodeling of cellular metabolism during iron deficiency through targeted mRNA degradation Cell 120 2005 99-110
    • (2005) Cell , vol.120 , pp. 99-110
    • Puig, S.1    Askeland, E.2    Thiele, D.J.3
  • 40
    • 1642573170 scopus 로고    scopus 로고
    • Mitochondrial functional interactions between frataxin and Isu1p, the iron-sulfur cluster scaffold protein, in Saccharomyces cerevisiae
    • A. Ramazzotti V. Vanmansart F. Foury Mitochondrial functional interactions between frataxin and Isu1p, the iron-sulfur cluster scaffold protein, in Saccharomyces cerevisiae FEBS Lett 557 2004 215-220
    • (2004) FEBS Lett , vol.557 , pp. 215-220
    • Ramazzotti, A.1    Vanmansart, V.2    Foury, F.3
  • 42
    • 17144378216 scopus 로고    scopus 로고
    • Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis
    • T.A. Rouault W.H. Tong Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis Nat. Rev. Mol. Cell Biol. 6 2005 345-351
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 345-351
    • Rouault, T.A.1    Tong, W.H.2
  • 44
    • 0033621156 scopus 로고    scopus 로고
    • Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
    • B. Schilke C. Voisine H. Beinert E. Craig Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae Proc. Natl. Acad. Sci. USA 96 1999 10206-10211
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10206-10211
    • Schilke, B.1    Voisine, C.2    Beinert, H.3    Craig, E.4
  • 46
    • 0034859174 scopus 로고    scopus 로고
    • Incorporation of iron-sulphur clusters in membrane-bound proteins
    • A. Seidler K. Jaschkowitz M. Wollenberg Incorporation of iron-sulphur clusters in membrane-bound proteins Biochem. Soc. Trans. 29 2001 418-421
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 418-421
    • Seidler, A.1    Jaschkowitz, K.2    Wollenberg, M.3
  • 48
    • 11144224094 scopus 로고    scopus 로고
    • Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU
    • J.J. Silberg T.L. Tapley K.G. Hoff L.E. Vickery Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU J. Biol. Chem. 279 2004 53924-53931
    • (2004) J. Biol. Chem. , vol.279 , pp. 53924-53931
    • Silberg, J.J.1    Tapley, T.L.2    Hoff, K.G.3    Vickery, L.E.4
  • 51
    • 14244254585 scopus 로고    scopus 로고
    • Down-regulation of iron regulatory protein 1 activities and expression in superoxide dismutase 1 knock-out mice is not associated with alterations in iron metabolism
    • R.R. Starzynski P. Lipinski J.-C. Drapier A. Diet E. Smuda T. Bartlomiejczyk M.A. Gralak M. Kruszewski Down-regulation of iron regulatory protein 1 activities and expression in superoxide dismutase 1 knock-out mice is not associated with alterations in iron metabolism J. Biol. Chem. 280 2005 4207
    • (2005) J. Biol. Chem. , vol.280 , pp. 4207
    • Starzynski, R.R.1    Lipinski, P.2    Drapier, J.-C.3    Diet, A.4    Smuda, E.5    Bartlomiejczyk, T.6    Gralak, M.A.7    Kruszewski, M.8
  • 54
    • 0034331239 scopus 로고    scopus 로고
    • Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells
    • W.-H. Tong T. Rouault Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells EMBO J. 19 2000 5692-5700
    • (2000) EMBO J. , vol.19 , pp. 5692-5700
    • Tong, W.-H.1    Rouault, T.2
  • 55
    • 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 G.N. Jameson B.H. Huynh T.A. Rouault Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster Proc. Natl. Acad. Sci. USA 100 2003 9762-9767
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9762-9767
    • Tong, W.H.1    Jameson, G.N.2    Huynh, B.H.3    Rouault, T.A.4
  • 57
    • 0035977015 scopus 로고    scopus 로고
    • Transfer of sulfur from IscS to IscU during Fe/S cluster assembly
    • H.D. Urbina J.J. Silberg K.G. Hoff L.E. Vickery 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    Silberg, J.J.2    Hoff, K.G.3    Vickery, L.E.4
  • 58
    • 3542993226 scopus 로고    scopus 로고
    • Superoxide inhibits 4Fe-4S cluster enzymes involved in amino acid biosynthesis.Cross-compartment protection by CuZn-superoxide dismutase
    • M.A. Wallace L.L. Liou J. Martins M.H. Clement S. Bailey V.D. Longo J.S. Valentine E.B. Gralla Superoxide inhibits 4Fe-4S cluster enzymes involved in amino acid biosynthesis.Cross-compartment protection by CuZn-superoxide dismutase J. Biol. Chem. 279 2004 32055-32062
    • (2004) J. Biol. Chem. , vol.279 , pp. 32055-32062
    • Wallace, M.A.1    Liou, L.L.2    Martins, J.3    Clement, M.H.4    Bailey, S.5    Longo, V.D.6    Valentine, J.S.7    Gralla, E.B.8
  • 60
    • 15544365805 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis. Molecular chaperone DnaK promotes IscU-bound [2Fe-2S] cluster stability and inhibits cluster transfer activity
    • S.P. Wu S.S. Mansy J.A. Cowan Iron-sulfur cluster biosynthesis. Molecular chaperone DnaK promotes IscU-bound [2Fe-2S] cluster stability and inhibits cluster transfer activity Biochemistry 44 2005 4284-4293
    • (2005) Biochemistry , vol.44 , pp. 4284-4293
    • Wu, S.P.1    Mansy, S.S.2    Cowan, J.A.3
  • 61
    • 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 K. Morimoto S. Kikuchi K. Nishio I. Terashima M. Nakai 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    Morimoto, K.2    Kikuchi, S.3    Nishio, K.4    Terashima, I.5    Nakai, M.6
  • 62
    • 14644405007 scopus 로고    scopus 로고
    • The chloroplast NifS-like protein of Arabidopsis thaliana is required for iron-sulfur cluster formation in ferredoxin
    • H. Ye G.F. Garifullina S.E. Abdel-Ghany L. Zhang E.A. Pilon-Smits M. Pilon The chloroplast NifS-like protein of Arabidopsis thaliana is required for iron-sulfur cluster formation in ferredoxin Planta 220 2005 602-608
    • (2005) Planta , vol.220 , pp. 602-608
    • Ye, H.1    Garifullina, G.F.2    Abdel-Ghany, S.E.3    Zhang, L.4    Pilon-Smits, E.A.5    Pilon, M.6
  • 63
    • 0032557666 scopus 로고    scopus 로고
    • Assembly of iron-sulfur clusters: Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii
    • L. Zheng V.L. Cash D.H. Flint D.R. Dean 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    Cash, V.L.2    Flint, D.H.3    Dean, D.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.