메뉴 건너뛰기




Volumn 86, Issue 3, 2005, Pages 391-407

Iron-sulfur cluster biosynthesis in photosynthetic organisms

Author keywords

Arabidopsis thaliana; Cyanobacteria; Desulfurase; Fe S cluster; L cysteine; Mitochondrion; Plastid; Saccharomyces cerevisiae

Indexed keywords

IRON; IRON SULFUR PROTEIN; SULFUR;

EID: 29944445891     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11120-005-5913-2     Document Type: Review
Times cited : (37)

References (82)
  • 2
    • 4544321137 scopus 로고    scopus 로고
    • The cell's cookbook for iron-sulfur clusters: Recipes for fool's gold
    • Balk J and Lill R (2004) The cell's cookbook for iron-sulfur clusters: recipes for fool's gold. Chembiochem 5: 1044-1049
    • (2004) Chembiochem , vol.5 , pp. 1044-1049
    • Balk, J.1    Lill, R.2
  • 3
    • 2942565619 scopus 로고    scopus 로고
    • The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins
    • Balk J, Pierik AJ, Netz DJ, Muhlenhoff U and Lill R (2004) The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins. EMBO J 23: 2105-2015
    • (2004) EMBO J , vol.23 , pp. 2105-12015
    • Balk, J.1    Pierik, A.J.2    Netz, D.J.3    Muhlenhoff, U.4    Lill, R.5
  • 4
    • 0036187913 scopus 로고    scopus 로고
    • Extensive feature detection of N-terminal protein sorting signals
    • Bannai H, Tamada Y, Maruyama O, Nakai K and Miyano S (2002) Extensive feature detection of N-terminal protein sorting signals. Bioinformatics 18: 298-305
    • (2002) Bioinformatics , vol.18 , pp. 298-305
    • Bannai, H.1    Tamada, Y.2    Maruyama, O.3    Nakai, K.4    Miyano, S.5
  • 5
    • 3042530231 scopus 로고    scopus 로고
    • Intracellular localization of sulfurtransferases from Arabidopsis thaliana
    • Bauer M, Dietrich C, Nowak K, Sierralta WD and Papenbrock J (2004) Intracellular localization of sulfurtransferases from Arabidopsis thaliana. Plant Physiol 135: 916-926
    • (2004) Plant Physiol , vol.135 , pp. 916-926
    • Bauer, M.1    Dietrich, C.2    Nowak, K.3    Sierralta, W.D.4    Papenbrock, J.5
  • 6
    • 4644301523 scopus 로고    scopus 로고
    • Mechanism of cysteine desulfurase Slr0387 from Synechocystis sp. PCC 6803: Kinetic analysis of cleavage of the persulfide intermediate by chemical reductants
    • Behshad E, Parkin SE and Bollinger JM (2004) Mechanism of cysteine desulfurase Slr0387 from Synechocystis sp. PCC 6803: kinetic analysis of cleavage of the persulfide intermediate by chemical reductants. Biochemistry 43: 12220-12226
    • (2004) Biochemistry , vol.43 , pp. 12220-12226
    • Behshad, E.1    Parkin, S.E.2    Bollinger, J.M.3
  • 7
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert H, Holm RH and Munck E (1997) Iron-sulfur clusters: nature's modular, multipurpose structures. Science 277: 653-659
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Munck, E.3
  • 8
    • 0034329310 scopus 로고    scopus 로고
    • Human ABC7 transporter: Gene structure and mutation causing X-linked sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur protein maturation
    • Bekri S, Kispal G, Lange H, Fitzsimons E, Tolmie J, Lill R and Bishop DF (2000) Human ABC7 transporter: gene structure and mutation causing X-linked sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur protein maturation. Blood 96: 3256-3264
    • (2000) Blood , vol.96 , pp. 3256-3264
    • Bekri, S.1    Kispal, G.2    Lange, H.3    Fitzsimons, E.4    Tolmie, J.5    Lill, R.6    Bishop, D.F.7
  • 9
    • 4944240979 scopus 로고    scopus 로고
    • Functional and molecular characterization of the frataxin homolog from Arabidopsis thaliana
    • Busi MV, Zabaleta EJ, Araya A and Gomez-Casati DF (2004) Functional and molecular characterization of the frataxin homolog from Arabidopsis thaliana. FEBS Lett 576: 141-144
    • (2004) FEBS Lett , vol.576 , pp. 141-144
    • Busi, M.V.1    Zabaleta, E.J.2    Araya, A.3    Gomez-Casati, D.F.4
  • 10
    • 0038161214 scopus 로고    scopus 로고
    • MDL1 is a high copy suppressor of ATM1: Evidence for a role in resistance to oxidative stress
    • Chloupková M, LeBard LS and Koeller DM (2003) MDL1 is a high copy suppressor of ATM1: evidence for a role in resistance to oxidative stress. J Mol Biol 331: 155-165
    • (2003) J Mol Biol , vol.331 , pp. 155-165
    • Chloupková, M.1    LeBard, L.S.2    Koeller, D.M.3
  • 11
    • 0034636007 scopus 로고    scopus 로고
    • Crystal structure of the cystine C-S lyase from Synechocystis: Stabilization of cysteine persulfide for FeS cluster biosynthesis
    • USA
    • Clausen T, Kaiser JT, Steegborn C, Huber R and Kessler D (2000) Crystal structure of the cystine C-S lyase from Synechocystis: stabilization of cysteine persulfide for FeS cluster biosynthesis. Proc Natl Acad Sci USA 97: 3856-3861
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 3856-3861
    • Clausen, T.1    Kaiser, J.T.2    Steegborn, C.3    Huber, R.4    Kessler, D.5
  • 12
    • 0038351831 scopus 로고    scopus 로고
    • Crystal structure of IscS, a cysteine desulfurase from Escherichia coli
    • Cupp-Vickery JR, Urbina H and Vickery LE (2003) Crystal structure of IscS, a cysteine desulfurase from Escherichia coli. J Mol Biol 330: 1049-1059
    • (2003) J Mol Biol , vol.330 , pp. 1049-1059
    • Cupp-Vickery, J.R.1    Urbina, H.2    Vickery, L.E.3
  • 13
    • 7244239273 scopus 로고    scopus 로고
    • Repair of oxidized iron-sulfur clusters in Escherichia coli
    • Djaman O, Outten FW and Imlay JA (2004) Repair of oxidized iron-sulfur clusters in Escherichia coli. J Biol Chem 279: 44590-44599
    • (2004) J Biol Chem , vol.279 , pp. 44590-44599
    • Djaman, O.1    Outten, F.W.2    Imlay, J.A.3
  • 14
    • 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
    • Dutkiewicz R, Schilke B, Knieszner H, Walter W, Craig EA and Marszalek J (2003) Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart. J Biol Chem 278: 29719-29727
    • (2003) J Biol Chem , vol.278 , pp. 29719-29727
    • Dutkiewicz, R.1    Schilke, B.2    Knieszner, H.3    Walter, W.4    Craig, E.A.5    Marszalek, J.6
  • 16
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson O, Nielsen H, Brunak S and Heijne Gvon (2000) Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J Mol Biol 300: 1005-1016
    • (2000) J Mol Biol , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Gvon, H.4
  • 17
    • 0035896520 scopus 로고    scopus 로고
    • Mitochondrial control of iron homeostasis
    • Foury F and Talibi D (2001) Mitochondrial control of iron homeostasis. J Biol Chem 276: 7762-7768
    • (2001) J Biol Chem , vol.276 , pp. 7762-7768
    • Foury, F.1    Talibi, D.2
  • 18
    • 0037397764 scopus 로고    scopus 로고
    • Formation of iron-sulfur clusters in bacteria - An emerging field in bioinorganic chemistry
    • Frazzon J and Dean DR (2003) Formation of iron-sulfur clusters in bacteria - an emerging field in bioinorganic chemistry. Curr Opin Chem Biol 7: 166-173
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 166-173
    • Frazzon, J.1    Dean, D.R.2
  • 19
    • 0141623560 scopus 로고    scopus 로고
    • An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1
    • Gerber J, Muhlenhoff U and Lill R (2003) An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1. EMBO Rep 49: 906-911
    • (2003) EMBO Rep , vol.49 , pp. 906-911
    • Gerber, J.1    Muhlenhoff, U.2    Lill, R.3
  • 20
    • 2442707887 scopus 로고    scopus 로고
    • The yeast scaffold proteins Isulp and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteins
    • Gerber J, Neumann K, Prohl C, Muhlenhoff U and Lill R (2004) The yeast scaffold proteins Isulp and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteins. Mol Cell Biol 24: 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
  • 21
    • 13844300091 scopus 로고    scopus 로고
    • Unique genetic compartmentalization of the SUF system in cryptophytes and characterization of a SufD mutant in Arabidopsis thaliana
    • Hjorth E, Hadfi K, Zauner S and Maier UG (2005) Unique genetic compartmentalization of the SUF system in cryptophytes and characterization of a SufD mutant in Arabidopsis thaliana. FEBS Lett 579: 1129-1135
    • (2005) FEBS Lett , vol.579 , pp. 1129-1135
    • Hjorth, E.1    Hadfi, K.2    Zauner, S.3    Maier, U.G.4
  • 22
    • 0034608935 scopus 로고    scopus 로고
    • Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli
    • USA
    • Hoff KG, Silberg JJ and Vickery LE (2000) Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli. Proc Natl Acad Sci USA 97: 7790-7795
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 7790-7795
    • Hoff, K.G.1    Silberg, J.J.2    Vickery, L.E.3
  • 23
    • 0032967295 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Formation, perturbation, and physiological functions
    • Imsande J (1999) Iron-sulfur clusters: Formation, perturbation, and physiological functions. Plant Physiol Biochem 37: 87-97
    • (1999) Plant Physiol Biochem , vol.37 , pp. 87-97
    • Imsande, J.1
  • 25
    • 0034724259 scopus 로고    scopus 로고
    • Role of a NifS-like protein from the cyanobacterium Synechocystis PCC 6803 in the maturation of FeS proteins
    • Jaschkowitz K and Seidler A (2000) Role of a NifS-like protein from the cyanobacterium Synechocystis PCC 6803 in the maturation of FeS proteins. Biochemistry 39: 3416-3423
    • (2000) Biochemistry , vol.39 , pp. 3416-3423
    • Jaschkowitz, K.1    Seidler, A.2
  • 26
    • 0034107324 scopus 로고    scopus 로고
    • Role of Saccharomyces cerevisiae ISA1 and ISA2 in iron homeostasis
    • Jensen LT and Culotta VC (2000) Role of Saccharomyces cerevisiae ISA1 and ISA2 in iron homeostasis. Mol Cell Biol 20: 3918-3927
    • (2000) Mol Cell Biol , vol.20 , pp. 3918-3927
    • Jensen, L.T.1    Culotta, V.C.2
  • 28
    • 0034330209 scopus 로고    scopus 로고
    • Gene cloning, purification, and characterization of two cyanobacterial NifS homologs driving iron-sulfur cluster formation
    • Kato S, Mihara H, Kurihara T, Yoshimura T and Esaki N (2000) Gene cloning, purification, and characterization of two cyanobacterial NifS homologs driving iron-sulfur cluster formation. Biosci Biotechnol Biochem 64: 2412-2419
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 2412-2419
    • Kato, S.1    Mihara, H.2    Kurihara, T.3    Yoshimura, T.4    Esaki, N.5
  • 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
    • USA
    • Kato S, Mihara H, Kurihara T, Takahashi Y, Tokumoto U, Yoshimura T and Esaki N (2002) 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 USA 99: 5948-5952
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 5948-5952
    • Kato, S.1    Mihara, H.2    Kurihara, T.3    Takahashi, Y.4    Tokumoto, U.5    Yoshimura, T.6    Esaki, N.7
  • 30
    • 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
    • Kaut A, Lange H, Diekert K, Kispal G and Lill R (2000) 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: 15955-15961
    • (2000) J Biol Chem , vol.275 , pp. 15955-15961
    • Kaut, A.1    Lange, H.2    Diekert, K.3    Kispal, G.4    Lill, R.5
  • 31
    • 2942726264 scopus 로고    scopus 로고
    • Slr0077 of Synechocystis has cysteine desulfurase as well as cystine lyase activity
    • Kessler D (2004) Slr0077 of Synechocystis has cysteine desulfurase as well as cystine lyase activity. Biochem Biophys Res Commun 320: 571-577
    • (2004) Biochem Biophys Res Commun , vol.320 , pp. 571-577
    • Kessler, D.1
  • 32
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atm1p and Nifs1p are essential for biogenesis of cytosolic Fe/S proteins
    • Kispal G, Csere P, Prohl C and Lill R (1999) The mitochondrial proteins Atm1p and Nifs1p are essential for biogenesis of cytosolic Fe/S proteins. EMBO J 18: 3941-3989
    • (1999) EMBO J , vol.18 , pp. 3941-3989
    • Kispal, G.1    Csere, P.2    Prohl, C.3    Lill, R.4
  • 34
    • 0032923527 scopus 로고    scopus 로고
    • Evidence for cysteine persulfide as reaction product of L-cyst(e)ine C-S-lyase (C-DES) from Synechocystis
    • Lang T and Kessler D (1999) Evidence for cysteine persulfide as reaction product of L-cyst(e)ine C-S-lyase (C-DES) from Synechocystis. J Biol Chem 274: 189-195
    • (1999) J Biol Chem , vol.274 , pp. 189-195
    • Lang, T.1    Kessler, D.2
  • 35
    • 0034866458 scopus 로고    scopus 로고
    • An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins
    • Lange H, Lisowsky T, Gerber J, Muhlenhoff U, Kispal G and Lill R (2001) An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins. EMBO Rep 2: 715-720
    • (2001) EMBO Rep , vol.2 , pp. 715-720
    • Lange, H.1    Lisowsky, T.2    Gerber, J.3    Muhlenhoff, U.4    Kispal, G.5    Lill, R.6
  • 36
    • 0030978491 scopus 로고    scopus 로고
    • A novel L-cysteine/cystine C-S-lyase directing [2Fe-2S] cluster formation of Synechocystis ferredoxin
    • Leibrecht I and Kessler D (1997) A novel L-cysteine/cystine C-S-lyase directing [2Fe-2S] cluster formation of Synechocystis ferredoxin. J Biol Chem 272: 10442-10447
    • (1997) J Biol Chem , vol.272 , pp. 10442-10447
    • Leibrecht, I.1    Kessler, D.2
  • 37
    • 0036714247 scopus 로고    scopus 로고
    • The AtNFS2 gene from Arabidopsis thaliana encodes a NifS-like plastidial cysteine desulphurase
    • Leon S, Touraine B, Briat JF and Lobreaux S (2002) The AtNFS2 gene from Arabidopsis thaliana encodes a NifS-like plastidial cysteine desulphurase. Biochem J 366: 557-564
    • (2002) Biochem J , vol.366 , pp. 557-564
    • Leon, S.1    Touraine, B.2    Briat, J.F.3    Lobreaux, S.4
  • 38
    • 0037570578 scopus 로고    scopus 로고
    • Iron-sulphur cluster assembly in plants: Distinct NFU proteins in mitochondria and plastids from Arabidopsis thaliana
    • Leon S, Touraine B, Ribot C, Briat JF and Lobreaux S (2003) Iron-sulphur cluster assembly in plants: distinct NFU proteins in mitochondria and plastids from Arabidopsis thaliana. Biochem J 371: 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
  • 39
    • 2442567796 scopus 로고    scopus 로고
    • Unique features of plant mitochondrial sulfhydryl oxidase
    • Levitan A, Danon A and Lisowsky T (2004) Unique features of plant mitochondrial sulfhydryl oxidase. J Biol Chem 279: 20002-20008
    • (2004) J Biol Chem , vol.279 , pp. 20002-20008
    • Levitan, A.1    Danon, A.2    Lisowsky, T.3
  • 40
    • 1642441937 scopus 로고    scopus 로고
    • The universally conserved HCF101 protein is involved in assembly of [4Fe-4S]-cluster-containing complexes in Arabidopsis thaliana chloroplasts
    • Lezhneva L, Amann K and Meurer J (2004) The universally conserved HCF101 protein is involved in assembly of [4Fe-4S]-cluster-containing complexes in Arabidopsis thaliana chloroplasts. Plant J 37: 174-185
    • (2004) Plant J , vol.37 , pp. 174-185
    • Lezhneva, L.1    Amann, K.2    Meurer, J.3
  • 41
    • 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 SAB, Pain D and Dancis A (1999) Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution. J Biol Chem 274: 33025-33034
    • (1999) J Biol Chem , vol.274 , pp. 33025-33034
    • Li, J.1    Kogan, M.2    Knight, S.A.B.3    Pain, D.4    Dancis, A.5
  • 42
    • 0025009780 scopus 로고
    • Metal-ion-center assembly of ferredoxin and plastocyanin in isolated chloroplasts
    • USA
    • Li HM, Theg SM, Bauerle CM and Keegstra K (1990) Metal-ion-center assembly of ferredoxin and plastocyanin in isolated chloroplasts. Proc Natl Acad Sci USA 87: 6748-6752
    • (1990) Proc Natl Acad Sci , vol.87 , pp. 6748-6752
    • Li, H.M.1    Theg, S.M.2    Bauerle, C.M.3    Keegstra, K.4
  • 43
    • 0034255836 scopus 로고    scopus 로고
    • Maturation of cellular Fe-S proteins: An essential function of mitochondria
    • Lill R and Kispal G (2000) Maturation of cellular Fe-S proteins: an essential function of mitochondria. Trends Biochem Sci 25: 352-356
    • (2000) Trends Biochem Sci , vol.25 , pp. 352-356
    • Lill, R.1    Kispal, G.2
  • 44
    • 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
    • Loiseau L, Ollagnier-de-Choudens S, Nachin L, Fontecave M and Barras F (2003) Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase. J Biol Chem 278: 38352-38359
    • (2003) J Biol Chem , vol.278 , pp. 38352-38359
    • Loiseau, L.1    Ollagnier-de-Choudens, S.2    Nachin, L.3    Fontecave, M.4    Barras, F.5
  • 45
    • 0030963659 scopus 로고    scopus 로고
    • Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities
    • Mihara H, Kurihara T, Yoshimura T, Soda K and Esaki N (1997) Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. J Biol Chem 272: 22417-22424
    • (1997) J Biol Chem , vol.272 , pp. 22417-22424
    • Mihara, H.1    Kurihara, T.2    Yoshimura, T.3    Soda, K.4    Esaki, N.5
  • 46
    • 0035190234 scopus 로고    scopus 로고
    • A plastidic ABC protein involved in intercompartmental communication of light signaling
    • Moller SG, Kunkel T and Chua N-H (2001) A plastidic ABC protein involved in intercompartmental communication of light signaling. Genes Dev 15: 90-103
    • (2001) Genes Dev , vol.15 , pp. 90-103
    • Moller, S.G.1    Kunkel, T.2    Chua, N.-H.3
  • 47
    • 0037157163 scopus 로고    scopus 로고
    • Identification of a novel prokaryotic HEAT-repeats-containing protein which interacts with a cyanobacterial IscA homolog
    • Morimoto K, Nishio K and Nakai M (2002) Identification of a novel prokaryotic HEAT-repeats-containing protein which interacts with a cyanobacterial IscA homolog. FEBS Lett 519: 123-127
    • (2002) FEBS Lett , vol.519 , pp. 123-127
    • Morimoto, K.1    Nishio, K.2    Nakai, M.3
  • 48
    • 0041893905 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur proteins in eukaryotes: A novel task of mitochondria that is inherited from bacteria
    • Muhlenhoff U and Lill R (2000) Biogenesis of iron-sulfur proteins in eukaryotes: a novel task of mitochondria that is inherited from bacteria. Biochim Biophys Acta 1459: 370-382
    • (2000) Biochim Biophys Acta , vol.1459 , pp. 370-382
    • Muhlenhoff, U.1    Lill, R.2
  • 49
    • 2242453224 scopus 로고    scopus 로고
    • Characterization of iron-sulfur protein assembly in isolated mitochondria. A requirement for ATP, NADH, and reduced iron
    • Muhlenhoff U, Richhardt N, Gerber J and Lill R (2002a) Characterization of iron-sulfur protein assembly in isolated mitochondria. A requirement for ATP, NADH, and reduced iron. J Biol Chem 277: 29810-29816
    • (2002) J Biol Chem , vol.277 , pp. 29810-29816
    • Muhlenhoff, U.1    Richhardt, N.2    Gerber, J.3    Lill, R.4
  • 50
    • 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 (2002b) The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins. Hum Mol Genet 11: 2025-2036
    • (2002) Hum Mol Genet , vol.11 , pp. 2025-2036
    • Muhlenhoff, U.1    Richhardt, N.2    Ristow, M.3    Kispal, G.4    Lill, R.5
  • 51
    • 4344595102 scopus 로고    scopus 로고
    • Functional characterisation of the eukaryotic cysteine desulfurase Nfs1p from S. cerevisiae
    • Muhlenhoff U, Balk J, Richhardt N, Kaiser JT, Sipos K, Kispal G and Lill R (2004) Functional characterisation of the eukaryotic cysteine desulfurase Nfs1p from S. cerevisiae. J Biol Chem 279: 36906-36015
    • (2004) J Biol Chem , vol.279 , pp. 36906-136015
    • Muhlenhoff, U.1    Balk, J.2    Richhardt, N.3    Kaiser, J.T.4    Sipos, K.5    Kispal, G.6    Lill, R.7
  • 52
    • 0035116079 scopus 로고    scopus 로고
    • SoxR-dependent response to oxidative stress and virulence of Erwinia chrysanthemi: The key role of SufC, an orphan ABC ATPase
    • Nachin L, El Hassouni M, Loiseau L, Expert D and Barras F (2001) SoxR-dependent response to oxidative stress and virulence of Erwinia chrysanthemi: the key role of SufC, an orphan ABC ATPase. Mol Mic 39: 960-972
    • (2001) Mol Mic , vol.39 , pp. 960-972
    • Nachin, L.1    El Hassouni, M.2    Loiseau, L.3    Expert, D.4    Barras, F.5
  • 53
    • 0037415722 scopus 로고    scopus 로고
    • SufC: An unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress
    • Nachin L, Loiseau L, Expert D and Barras F (2003) SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress. EMBO J 22: 427-437
    • (2003) EMBO J , vol.22 , pp. 427-437
    • Nachin, L.1    Loiseau, L.2    Expert, D.3    Barras, F.4
  • 54
    • 0027105007 scopus 로고
    • A knowledge base for predicting protein localization sites in eukaryotic cells
    • Nakai K and Kanehisa M (1992) A knowledge base for predicting protein localization sites in eukaryotic cells. Genomics 14: 897-911
    • (1992) Genomics , vol.14 , pp. 897-911
    • Nakai, K.1    Kanehisa, M.2
  • 55
    • 0034725582 scopus 로고    scopus 로고
    • Transfer of iron-sulfur cluster from NifU to apoferredoxin
    • Nishio K and Nakai M (2000) Transfer of iron-sulfur cluster from NifU to apoferredoxin. J Biol Chem 275: 22615-22618
    • (2000) J Biol Chem , vol.275 , pp. 22615-22618
    • Nishio, K.1    Nakai, M.2
  • 56
    • 0345303679 scopus 로고    scopus 로고
    • Mechanistic studies of the SufS-SufE cysteine desulfurase: Evidence for sulfur transfer from SufS to SufE
    • Ollagnier-de-Choudens S, Lascoux D, Loiseau L, Barras F, Forest E and Fontecave M (2003a) Mechanistic studies of the SufS-SufE cysteine desulfurase: evidence for sulfur transfer from SufS to SufE. FEBS Lett 555: 263-267
    • (2003) FEBS Lett , vol.555 , pp. 263-267
    • Ollagnier-de-Choudens, S.1    Lascoux, D.2    Loiseau, L.3    Barras, F.4    Forest, E.5    Fontecave, M.6
  • 57
    • 0038381472 scopus 로고    scopus 로고
    • SufA from Erwinia chrysanthemi. Characterization of a scaffold protein required for iron-sulfur cluster assembly
    • Ollagnier-de-Choudens S, Nachin L, Sanakis Y, Loiseau L, Barras F and Fontecave M (2003b) SufA from Erwinia chrysanthemi. Characterization of a scaffold protein required for iron-sulfur cluster assembly. J Biol Chem 278: 17993-18001
    • (2003) J Biol Chem , vol.278 , pp. 17993-18001
    • Ollagnier-de-Choudens, S.1    Nachin, L.2    Sanakis, Y.3    Loiseau, L.4    Barras, F.5    Fontecave, M.6
  • 58
    • 2442567822 scopus 로고    scopus 로고
    • A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli
    • Outten FW, Djaman O and Storz G (2004) A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli. Mol Microbiol 52: 861-872
    • (2004) Mol Microbiol , vol.52 , pp. 861-872
    • Outten, F.W.1    Djaman, O.2    Storz, G.3
  • 59
    • 0242664733 scopus 로고    scopus 로고
    • The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli
    • Outten FW, Wood MJ, Muñoz FM and Storz G (2003) The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli. J Biol Chem 278: 45713-45719
    • (2003) J Biol Chem , vol.278 , pp. 45713-45719
    • Outten, F.W.1    Wood, M.J.2    Muñoz, F.M.3    Storz, G.4
  • 60
    • 0042090350 scopus 로고    scopus 로고
    • The plant biotin synthase reaction. Identification and characterization of essential mitochondrial accessory protein components
    • Picciocchi A, Douce R and Alban C (2003) The plant biotin synthase reaction. Identification and characterization of essential mitochondrial accessory protein components. J Biol Chem 278: 24966-24975
    • (2003) J Biol Chem , vol.278 , pp. 24966-24975
    • Picciocchi, A.1    Douce, R.2    Alban, C.3
  • 63
    • 0033621156 scopus 로고    scopus 로고
    • Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
    • USA
    • Schilke B, Voisine C, Beinert H and Craig E (1999) Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae. Proc Natl Acad Sci USA 96: 10206-10211
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 10206-10211
    • Schilke, B.1    Voisine, C.2    Beinert, H.3    Craig, E.4
  • 64
    • 0034859174 scopus 로고    scopus 로고
    • Incorporation of iron-sulphur clusters in membrane-bound proteins
    • Seidler A, Jaschkowitz K and Wollenberg M (2001) Incorporation of iron-sulphur clusters in membrane-bound proteins. Biochem Soc Trans 29: 418-421
    • (2001) Biochem Soc Trans , vol.29 , pp. 418-421
    • Seidler, A.1    Jaschkowitz, K.2    Wollenberg, M.3
  • 65
    • 0037178843 scopus 로고    scopus 로고
    • Maturation of cytosolic iron-sulfur proteins requires glutathione
    • Sipos K, Lange H, Fekete Z, Ullmann P, Lill R and Kispal G (2002) Maturation of cytosolic iron-sulfur proteins requires glutathione. J Biol Chem 277: 26944-26949
    • (2002) J Biol Chem , vol.277 , pp. 26944-26949
    • Sipos, K.1    Lange, H.2    Fekete, Z.3    Ullmann, P.4    Lill, R.5    Kispal, G.6
  • 66
    • 1642418871 scopus 로고    scopus 로고
    • A novel protein for Photosystem I biogenesis
    • Stöckel J and Oelmüller R (2004) A novel protein for Photosystem I biogenesis. J Biol Chem 279: 10243-10251
    • (2004) J Biol Chem , vol.279 , pp. 10243-10251
    • Stöckel, J.1    Oelmüller, R.2
  • 67
    • 0034804608 scopus 로고    scopus 로고
    • Mitochondrial type iron-sulfur cluster assembly in the amitochondriate eukaryotes Trichomonas vaginalis and Giardia intestinalis, as indicated by the phylogeny of IscS
    • Tachezy J, Sánchez LB and Müller M (2001) Mitochondrial type iron-sulfur cluster assembly in the amitochondriate eukaryotes Trichomonas vaginalis and Giardia intestinalis, as indicated by the phylogeny of IscS. Mol Biol Evol 18: 1919-1928
    • (2001) Mol Biol Evol , vol.18 , pp. 1919-1928
    • Tachezy, J.1    Sánchez, L.B.2    Müller, M.3
  • 68
    • 0037047411 scopus 로고    scopus 로고
    • A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids
    • Takahashi Y and Tokumoto U (2002) A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids. J Biol Chem 277: 28380-28383
    • (2002) J Biol Chem , vol.277 , pp. 28380-28383
    • Takahashi, Y.1    Tokumoto, U.2
  • 69
    • 4644275046 scopus 로고    scopus 로고
    • Kinetic and structural characterization of Slr0077/SufS, the essential cysteine desulfurase from Synechocystis sp. PCC 6803
    • Tirupati B, Lynn Vey J, Drennan CL and Bollinger JM (2004) Kinetic and structural characterization of Slr0077/SufS, the essential cysteine desulfurase from Synechocystis sp. PCC 6803. Biochemistry 43: 12210-12219
    • (2004) Biochemistry , vol.43 , pp. 12210-12219
    • Tirupati, B.1    Lynn Vey, J.2    Drennan, C.L.3    Bollinger, J.M.4
  • 70
    • 5144230341 scopus 로고    scopus 로고
    • Nfu2: A scaffold protein required for [4Fe-4S] and ferredoxin iron-sulphur cluster assembly in Arabidopsis chloroplasts
    • Touraine B, Boutin JP, Marion-Poll A, Briat JF, Peltier G and Lobreaux S (2004) Nfu2: a scaffold protein required for [4Fe-4S] and ferredoxin iron-sulphur cluster assembly in Arabidopsis chloroplasts. Plant J 40: 101-111
    • (2004) Plant J , vol.40 , pp. 101-111
    • Touraine, B.1    Boutin, J.P.2    Marion-Poll, A.3    Briat, J.F.4    Peltier, G.5    Lobreaux, S.6
  • 72
    • 1142298511 scopus 로고    scopus 로고
    • The sufR gene (sll0088 in Synechocystis sp. strain PCC 6803) functions as a repressor of the sufBCDS operon in iron-sulfur cluster biogenesis in cyanobacteria
    • Wang T, Shen G, Balasubramanian R, McIntosh L, Bryant DA and Golbeck JH (2004) The sufR gene (sll0088 in Synechocystis sp. strain PCC 6803) functions as a repressor of the sufBCDS operon in iron-sulfur cluster biogenesis in cyanobacteria. J Bacteriol 186: 956-967
    • (2004) J Bacteriol , vol.186 , pp. 956-967
    • Wang, T.1    Shen, G.2    Balasubramanian, R.3    McIntosh, L.4    Bryant, D.A.5    Golbeck, J.H.6
  • 73
    • 0038409882 scopus 로고    scopus 로고
    • A dimer of the FeS cluster biosynthesis protein IscA from cyanobacteria binds a [2Fe2S] cluster between two protomers and transfers it to [2Fe2S] and [4Fe4S] apo proteins
    • Wollenberg M, Berndt C, Bill E, Schwenn JD and Seidler A (2003) A dimer of the FeS cluster biosynthesis protein IscA from cyanobacteria binds a [2Fe2S] cluster between two protomers and transfers it to [2Fe2S] and [4Fe4S] apo proteins. Eur J Biochem 270: 1662-1671
    • (2003) Eur J Biochem , vol.270 , pp. 1662-1671
    • Wollenberg, M.1    Berndt, C.2    Bill, E.3    Schwenn, J.D.4    Seidler, A.5
  • 74
    • 2942659075 scopus 로고    scopus 로고
    • AtNAP7 is a plastidic SufC-like ATP-binding cassette/ATPase essential for Arabidopsis embryogenesis
    • USA
    • Xu XM and Moller SG (2004) AtNAP7 is a plastidic SufC-like ATP-binding cassette/ATPase essential for Arabidopsis embryogenesis. Proc Natl Acad Sci USA 101: 9143-9148
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 9143-9148
    • Xu, X.M.1    Moller, S.G.2
  • 75
    • 14844295427 scopus 로고    scopus 로고
    • AtNAP1 represents an atypical SufB protein in Arabidopsis plastids
    • Xu XM, Adams S, Chua NH and Moller SG (2005) AtNAP1 represents an atypical SufB protein in Arabidopsis plastids. J Biol Chem 280: 6648-6654
    • (2005) J Biol Chem , vol.280 , pp. 6648-6654
    • Xu, X.M.1    Adams, S.2    Chua, N.H.3    Moller, S.G.4
  • 76
    • 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
    • Yabe T, Morimoto K, Kikuchi S, Nishio K, Terashima I and Nakai M (2004) 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: 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
  • 77
    • 14644405007 scopus 로고    scopus 로고
    • The chloroplast NifS-like protein of Arabidopsis thaliana is required for iron-sulfur cluster formation in ferredoxin
    • Ye H, Garifullina GF, Abdel-Ghany SE, Zhang L, Pilon-Smits EA and Pilon M (2004) The chloroplast NifS-like protein of Arabidopsis thaliana is required for iron-sulfur cluster formation in ferredoxin. Planta 220: 602-608
    • (2004) 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
  • 78
    • 0035896360 scopus 로고    scopus 로고
    • Role of the ABC transporter Mdl1 in peptide export from mitochondria
    • Young L, Leonhard K, Tatsuta T, Trowsdale J and Langer T (2001) Role of the ABC transporter Mdl1 in peptide export from mitochondria. Science 291: 2135-2138
    • (2001) Science , vol.291 , pp. 2135-2138
    • Young, L.1    Leonhard, K.2    Tatsuta, T.3    Trowsdale, J.4    Langer, T.5
  • 79
    • 0034681155 scopus 로고    scopus 로고
    • NifS-directed assembly of a transient [2Fe-2S] cluster within the NifU protein
    • USA
    • Yuvaniyama P, Agar JN, Cash VL, Johnson MK and Dean DR (2000) NifS-directed assembly of a transient [2Fe-2S] cluster within the NifU protein. Proc Natl Acad Sci USA 97: 599-604
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 599-604
    • Yuvaniyama, P.1    Agar, J.N.2    Cash, V.L.3    Johnson, M.K.4    Dean, D.R.5
  • 80
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis
    • USA
    • Zheng L, White RH, Cash VL, Jack RF and Dean DR (1993) Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis. Proc Natl Acad Sci USA 90: 2754-2758
    • (1993) Proc Natl Acad Sci , vol.90 , pp. 2754-2758
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Jack, R.F.4    Dean, D.R.5
  • 82
    • 0034932337 scopus 로고    scopus 로고
    • DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide
    • Zheng M, Wang X, Templeton LJ, Smulski DR, LaRossa RA and Storz G (2001) DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide. J Bacteriol 183: 4562-4570
    • (2001) J Bacteriol , vol.183 , pp. 4562-4570
    • Zheng, M.1    Wang, X.2    Templeton, L.J.3    Smulski, D.R.4    LaRossa, R.A.5    Storz, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.