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Volumn 179, Issue 1, 2008, Pages 59-68

Genome analysis of Chlamydomonas reinhardtii reveals the existence of multiple, compartmentalized iron-sulfur protein assembly machineries of different evolutionary origins

Author keywords

[No Author keywords available]

Indexed keywords

CYSTATHIONINE GAMMA LYASE; IRON HYDROGENASE; IRON SULFUR PROTEIN; SCAFFOLD PROTEIN;

EID: 52049116969     PISSN: 00166731     EISSN: 00166731     Source Type: Journal    
DOI: 10.1534/genetics.107.086033     Document Type: Article
Times cited : (29)

References (55)
  • 1
    • 21444455377 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur proteins in plants
    • BALK, J., and S. LOBRÉAUX, 2005 Biogenesis of iron-sulfur proteins in plants. Trends Plant Sci. 10: 324-331.
    • (2005) Trends Plant Sci , vol.10 , pp. 324-331
    • BALK, J.1    LOBRÉAUX, S.2
  • 2
    • 2942565619 scopus 로고    scopus 로고
    • The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins
    • BALK, J., A. J. PIERIK, D. J. AGUILAR NETZ, U. MÜHLENHOFF and R. LILL, 2004 The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins. EMBO J. 23: 2105-2115.
    • (2004) EMBO J , vol.23 , pp. 2105-2115
    • BALK, J.1    PIERIK, A.J.2    AGUILAR NETZ, D.J.3    MÜHLENHOFF, U.4    LILL, R.5
  • 3
    • 28544450863 scopus 로고    scopus 로고
    • The essential WD40 protein Cia1 is involved in a late step of cytosolic and nuclear iron-sulfur protein assembly
    • BALK, J., D. J. AGUILAR NETZ, K. TEPPER, A. J. PIERIK and R. LILL, 2005 The essential WD40 protein Cia1 is involved in a late step of cytosolic and nuclear iron-sulfur protein assembly. Mol. Cell. Biol. 25: 10833-10841.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 10833-10841
    • BALK, J.1    AGUILAR NETZ, D.J.2    TEPPER, K.3    PIERIK, A.J.4    LILL, R.5
  • 4
    • 26444455549 scopus 로고    scopus 로고
    • How Escherichia coli and Saccharomyces cerevisiae build Fe/S proteins
    • BARRAS, F., L. LOISEAU and B. PY, 2005 How Escherichia coli and Saccharomyces cerevisiae build Fe/S proteins. Adv. Microb. Physiol. 50: 41-101.
    • (2005) Adv. Microb. Physiol , vol.50 , pp. 41-101
    • BARRAS, F.1    LOISEAU, L.2    PY, B.3
  • 5
    • 0034003112 scopus 로고    scopus 로고
    • Iron-sulfur proteins: Ancient structures, still full of surprises
    • BEINERT, H., 2000 Iron-sulfur proteins: ancient structures, still full of surprises. J. Biol. Inorg. Chem. 5: 2-15.
    • (2000) J. Biol. Inorg. Chem , vol.5 , pp. 2-15
    • BEINERT, H.1
  • 6
    • 0346727529 scopus 로고    scopus 로고
    • Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme
    • BERKOVITCH, F., Y. NICOLET, J. T. WAN, J. T. JARRETT and C. L. DRENNAN, 2004 Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science 303: 76-79.
    • (2004) Science , vol.303 , pp. 76-79
    • BERKOVITCH, F.1    NICOLET, Y.2    WAN, J.T.3    JARRETT, J.T.4    DRENNAN, C.L.5
  • 8
    • 33644852344 scopus 로고    scopus 로고
    • The [Fe-Fe]-hydrogenase maturation protein HydF from Thermatoga maritima is a GTPase with an iron-sulfur cluster
    • BRAZZOLOTTO, Z., J. K. RUBACH, J. GAILLARD, S. GAMBARELLI, M. ATTA et al., 2006 The [Fe-Fe]-hydrogenase maturation protein HydF from Thermatoga maritima is a GTPase with an iron-sulfur cluster. J. Biol. Chem. 281: 769-774.
    • (2006) J. Biol. Chem , vol.281 , pp. 769-774
    • BRAZZOLOTTO, Z.1    RUBACH, J.K.2    GAILLARD, J.3    GAMBARELLI, S.4    ATTA, M.5
  • 9
    • 14844317304 scopus 로고    scopus 로고
    • Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: Both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide
    • CICCHILLO, R. M., and S. J. BOOKER, 2005 Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide. J. Am. Chem. Soc. 127: 2860-2861.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 2860-2861
    • CICCHILLO, R.M.1    BOOKER, S.J.2
  • 10
    • 33645456207 scopus 로고    scopus 로고
    • Eukaryotic evolution, changes and challenges
    • EMBLEY, T. M., and W. MARTIN, 2006 Eukaryotic evolution, changes and challenges. Nature 440: 623-630.
    • (2006) Nature , vol.440 , pp. 623-630
    • EMBLEY, T.M.1    MARTIN, W.2
  • 11
    • 40749086415 scopus 로고    scopus 로고
    • Mitochondrial Iba57p is required for Fe/S cluster formation on aconitase and activation of radical SAM enzymes
    • GELLING, C., I. W. DAWES, N. RICHHARDT, R. LILL and U. MÜHLENHOFF, 2008 Mitochondrial Iba57p is required for Fe/S cluster formation on aconitase and activation of radical SAM enzymes. Mol. Cell. Biol. 28: 1851-1861.
    • (2008) Mol. Cell. Biol , vol.28 , pp. 1851-1861
    • GELLING, C.1    DAWES, I.W.2    RICHHARDT, N.3    LILL, R.4    MÜHLENHOFF, U.5
  • 12
    • 21244449583 scopus 로고    scopus 로고
    • A mitochondrial half-size ABC transporter is involved in cadmium tolerance in Chlamydomonas reinhardtii
    • HANIKENNE, M., P. MOTTE, W. C. S. WU, T. WANG, R. LOPPES et al., 2005 A mitochondrial half-size ABC transporter is involved in cadmium tolerance in Chlamydomonas reinhardtii. Plant Cell Environ. 28: 863-873.
    • (2005) Plant Cell Environ , vol.28 , pp. 863-873
    • HANIKENNE, M.1    MOTTE, P.2    WU, W.C.S.3    WANG, T.4    LOPPES, R.5
  • 13
    • 34250731291 scopus 로고    scopus 로고
    • HERRERO, E., and M. A. DE LA TORRE-R UIZ, 2007 Monothiol glutaredoxins: a common domain for multiple functions. Cell. Mol. Life Sci. 64: 1518-1530.
    • HERRERO, E., and M. A. DE LA TORRE-R UIZ, 2007 Monothiol glutaredoxins: a common domain for multiple functions. Cell. Mol. Life Sci. 64: 1518-1530.
  • 14
    • 33846298869 scopus 로고    scopus 로고
    • IOP1, a novel hydrogenase-like protein that modulates hypoxia-inducible factor1-alpha activity
    • HUANG, J., D. SONG, A. FLORES, Q. ZHAO, S. M. MOONEY et al., 2007 IOP1, a novel hydrogenase-like protein that modulates hypoxia-inducible factor1-alpha activity. Biochem. J. 401: 341-352.
    • (2007) Biochem. J , vol.401 , pp. 341-352
    • HUANG, J.1    SONG, D.2    FLORES, A.3    ZHAO, Q.4    MOONEY, S.M.5
  • 15
    • 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
  • 16
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • JOHNSON, D. C., D. R. DEAN, A. D. SMITH and M. K. JOHNSON, 2005 Structure, function, and formation of biological iron-sulfur clusters. Annu. Rev. Biochem. 74: 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
  • 17
    • 0034330209 scopus 로고    scopus 로고
    • Gene cloning, purification, and characterization of two cyanobacterial NifS homologs driving iron-sulfur cluster formation
    • KATO, S., H. MIHARA, T. KURIHARA, T. YOSHIMURA and N. ESAKI, 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
  • 18
    • 29944445891 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis in photosynthetic organisms
    • KESSLER, D., and J. PAPENBROCK, 2005 Iron-sulfur cluster biosynthesis in photosynthetic organisms. Photosynth. Res. 86: 391-407.
    • (2005) Photosynth. Res , vol.86 , pp. 391-407
    • KESSLER, D.1    PAPENBROCK, J.2
  • 19
    • 33646905391 scopus 로고    scopus 로고
    • AtATM3 is involved in heavy metal resistance in Arabidopsis
    • KIM, D. Y., L. BOVET, S. KUSHNIR, E. W. NOH, E. MARTINOIA et al., 2006 AtATM3 is involved in heavy metal resistance in Arabidopsis. Plant Physiol. 140: 922-932.
    • (2006) Plant Physiol , vol.140 , pp. 922-932
    • KIM, D.Y.1    BOVET, L.2    KUSHNIR, S.3    NOH, E.W.4    MARTINOIA, E.5
  • 20
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
    • KISPAL, G., P. CSERE, C. PROHL and R. LILL, 1999 The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins. EMBO J. 18: 3981-3989.
    • (1999) EMBO J , vol.18 , pp. 3981-3989
    • KISPAL, G.1    CSERE, P.2    PROHL, C.3    LILL, R.4
  • 21
    • 0037570578 scopus 로고    scopus 로고
    • Iron-sulphur cluster assembly in plants: Distinct NFU proteins in mitochondria and plastids from Arabidopsis thaliana
    • LÉON, S., B. TOURAINE, C. RIBOT, J. F. BRIAT and S. LOBRÉAUX, 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
    • LÉON, S.1    TOURAINE, B.2    RIBOT, C.3    BRIAT, J.F.4    LOBRÉAUX, S.5
  • 22
    • 15544363027 scopus 로고    scopus 로고
    • Mitochondrial localization of Arabidopsis thaliana Isu Fe-S scaffold proteins
    • LÉON, S., B. TOURAINE, J.-F. BRIAT and S. LOBRÉAUX, 2005 Mitochondrial localization of Arabidopsis thaliana Isu Fe-S scaffold proteins. FEBS Lett. 28: 1930-1934.
    • (2005) FEBS Lett , vol.28 , pp. 1930-1934
    • LÉON, S.1    TOURAINE, B.2    BRIAT, J.-F.3    LOBRÉAUX, S.4
  • 23
    • 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., K. AMANN and J. MEURER, 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
  • 24
    • 0025009780 scopus 로고
    • Metalion-center assembly of ferredoxin and plastocyanin in isolated chloroplasts
    • LI, H.-M., S. M. THEG, C. M. BAUERLE and K. KEEGSTRA, 1990 Metalion-center assembly of ferredoxin and plastocyanin in isolated chloroplasts. Proc. Natl. Acad. Sci. USA 87: 6748-6752.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6748-6752
    • LI, H.-M.1    THEG, S.M.2    BAUERLE, C.M.3    KEEGSTRA, K.4
  • 25
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: Mechanisms, connected processes, and diseases
    • in press
    • LILL, R., and U. MÜHLENHOFF, 2008 Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases. Annu. Rev. Biochem. 77: (in press).
    • (2008) Annu. Rev. Biochem , vol.77
    • LILL, R.1    MÜHLENHOFF, U.2
  • 26
    • 35348876543 scopus 로고    scopus 로고
    • ErpA, an iron-sulfur (Fe-S) protein of the A-type essential for respiratory metabolism in Escherichia coli
    • LOISEAU, L., C. GEREZ, M. BEKKER, S. OLLAGNIER-DE-CHOUDENS, B. PY et al., 2007 ErpA, an iron-sulfur (Fe-S) protein of the A-type essential for respiratory metabolism in Escherichia coli. Proc. Natl. Acad. Sci. USA 104: 13626-13631.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 13626-13631
    • LOISEAU, L.1    GEREZ, C.2    BEKKER, M.3    OLLAGNIER-DE-CHOUDENS, S.4    PY, B.5
  • 27
    • 35348896591 scopus 로고    scopus 로고
    • The Chlamydomonas genome reveals the evolution of key animal and plant functions
    • MERCHANT, S. S., S. E. PROCHNIK, O. VALLON, E. H. HARRIS, S. J. KARPOWICZ et al., 2007 The Chlamydomonas genome reveals the evolution of key animal and plant functions. Science 318: 245-250.
    • (2007) Science , vol.318 , pp. 245-250
    • MERCHANT, S.S.1    PROCHNIK, S.E.2    VALLON, O.3    HARRIS, E.H.4    KARPOWICZ, S.J.5
  • 28
    • 34247577593 scopus 로고    scopus 로고
    • FeFe] hydrogenases and their evolution: A genomic perspective
    • MEYER, J., 2007 [FeFe] hydrogenases and their evolution: a genomic perspective. Cell. Mol. Life Sci. 64: 1063-1084.
    • (2007) Cell. Mol. Life Sci , vol.64 , pp. 1063-1084
    • MEYER, J.1
  • 29
    • 0037209757 scopus 로고    scopus 로고
    • Bacterial cysteine desulfurases: Their function and mechanisms
    • MIHARA, H., and N. ESAKI, 2002 Bacterial cysteine desulfurases: their function and mechanisms. Appl. Microbiol. Biotechnol. 60: 12-23.
    • (2002) Appl. Microbiol. Biotechnol , vol.60 , pp. 12-23
    • MIHARA, H.1    ESAKI, N.2
  • 30
    • 0041893905 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur proteins in eukaryotes: A novel task of mitochondria that is inherited from bacteria
    • MÜHLENHOFF, U., and R. LILL, 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
    • MÜHLENHOFF, U.1    LILL, R.2
  • 31
    • 33947624626 scopus 로고    scopus 로고
    • The ISC proteins Isa1 and Isa2 are required for the function but not the de novo synthesis of the Fe/S clusters of biotin synthase in Saccharomyces cerevisiae
    • MÜHLENHOFF, U., M. J. GERL, B. FLAUGER, H. M. PIRNER, S. BALSER et al., 2007 The ISC proteins Isa1 and Isa2 are required for the function but not the de novo synthesis of the Fe/S clusters of biotin synthase in Saccharomyces cerevisiae. Eukaryot. Cell 6: 495-504.
    • (2007) Eukaryot. Cell , vol.6 , pp. 495-504
    • MÜHLENHOFF, U.1    GERL, M.J.2    FLAUGER, B.3    PIRNER, H.M.4    BALSER, S.5
  • 32
    • 34547098851 scopus 로고    scopus 로고
    • Characterization of Arabidopsis thaliana SufE2 and SufE3: Functions in chloroplast iron-sulfur cluster assembly and Nad synthesis
    • MURTHY, U. N. M., S. OLLAGNIER-DE-CHOUDENS, Y. SANAKIS, S. E. ABDEL-GHANY, C. ROUSSET et al., 2007 Characterization of Arabidopsis thaliana SufE2 and SufE3: functions in chloroplast iron-sulfur cluster assembly and Nad synthesis. J. Biol. Chem. 282: 18254-18264.
    • (2007) J. Biol. Chem , vol.282 , pp. 18254-18264
    • MURTHY, U.N.M.1    OLLAGNIER-DE-CHOUDENS, S.2    SANAKIS, Y.3    ABDEL-GHANY, S.E.4    ROUSSET, C.5
  • 33
    • 0037415722 scopus 로고    scopus 로고
    • NACHIN, L., L. LOISEAU, D. EXPERT and Y. BARRAS, 2003 SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress. EMBO J. 22: 427-437.
    • NACHIN, L., L. LOISEAU, D. EXPERT and Y. BARRAS, 2003 SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress. EMBO J. 22: 427-437.
  • 34
    • 34247247617 scopus 로고    scopus 로고
    • The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol
    • NETZ, D. J., A. J. PIERIK, M. STÜMPFIG, U. MÜHLENHOFF and R. LILL, 2007 The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol. Nat. Chem. Biol. 3: 278-286.
    • (2007) Nat. Chem. Biol , vol.3 , pp. 278-286
    • NETZ, D.J.1    PIERIK, A.J.2    STÜMPFIG, M.3    MÜHLENHOFF, U.4    LILL, R.5
  • 35
    • 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, F. W., M. J. WOOD, F. M. MUÑOZ and G. STORZ, 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
  • 36
    • 2442567822 scopus 로고    scopus 로고
    • A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli
    • OUTTEN, F. W., O. DJAMAN and G. STORZ, 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
  • 38
    • 0032483966 scopus 로고    scopus 로고
    • X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum at 1.8 angstrom resolution
    • PETERS, J. W., W. N. LANZILOTTA, B. J. LEMON and L. C. SEEFELDT, 1998 X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum at 1.8 angstrom resolution. Science 282: 1853-1858.
    • (1998) Science , vol.282 , pp. 1853-1858
    • PETERS, J.W.1    LANZILOTTA, W.N.2    LEMON, B.J.3    SEEFELDT, L.C.4
  • 39
    • 0042090350 scopus 로고    scopus 로고
    • The plant biotin synthase reaction. Identification and characterization of essential mitochondrial accessory protein components
    • PICCIOCCHI, A., R. DOUCE and C. ALBAN, 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
  • 40
    • 2942586665 scopus 로고    scopus 로고
    • Discovery of two novel radical S-adenosylmethionine proteins required for the assembly of an active [Fe] hydrogenase
    • POSEWITZ, M. C., P. W. KING, S. L. SMOLINSKI, L. ZHANG, M. SEIBERT et al., 2004 Discovery of two novel radical S-adenosylmethionine proteins required for the assembly of an active [Fe] hydrogenase. J. Biol. Chem. 279: 25711-25720.
    • (2004) J. Biol. Chem , vol.279 , pp. 25711-25720
    • POSEWITZ, M.C.1    KING, P.W.2    SMOLINSKI, S.L.3    ZHANG, L.4    SEIBERT, M.5
  • 41
  • 42
    • 33747170368 scopus 로고    scopus 로고
    • Evolution of mitochondrial chaperones utilized in Fe-S cluster biogenesis
    • SCHILKE, B., B. WILLIAMS, H. KNIESZNER, S. PUKSZTA, P. D'SILVA et al., 2006 Evolution of mitochondrial chaperones utilized in Fe-S cluster biogenesis. Curr. Biol. 16: 1660-1665.
    • (2006) Curr. Biol , vol.16 , pp. 1660-1665
    • SCHILKE, B.1    WILLIAMS, B.2    KNIESZNER, H.3    PUKSZTA, S.4    D'SILVA, P.5
  • 43
    • 0037178843 scopus 로고    scopus 로고
    • Maturation of cytosolic iron-sulfur proteins requires glutatione
    • SIPOS, K., H. LANGE, Z. FEKETE, P. ULLMANN, R. LILL et al., 2002 Maturation of cytosolic iron-sulfur proteins requires glutatione. 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
  • 44
    • 1642418871 scopus 로고    scopus 로고
    • A novel protein for photosystem I biogenesis
    • STÖCKEL, J., and R. OELMÜLLER, 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
  • 45
    • 0001158225 scopus 로고
    • Formation of the iron-sulfur cluster of ferredoxin in isolated chloroplasts
    • TAKAHASHI, Y., A. MITSUI, T. HASE and H. MATSUBARA, 1986 Formation of the iron-sulfur cluster of ferredoxin in isolated chloroplasts. Proc. Natl. Acad. Sci. USA 83: 2434-2437.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 2434-2437
    • TAKAHASHI, Y.1    MITSUI, A.2    HASE, T.3    MATSUBARA, H.4
  • 46
    • 0000580463 scopus 로고
    • Roles of ATP and NADPH in formation of the Fe-S cluster of spinach ferredoxin
    • TAKAHASHI, Y., A. MITSUI, Y. FUJITA and H. MATSUBARA, 1991a Roles of ATP and NADPH in formation of the Fe-S cluster of spinach ferredoxin. Plant Physiol. 95: 104-110.
    • (1991) Plant Physiol , vol.95 , pp. 104-110
    • TAKAHASHI, Y.1    MITSUI, A.2    FUJITA, Y.3    MATSUBARA, H.4
  • 47
    • 0002949415 scopus 로고
    • Formation of the Fe-S cluster of ferredoxin in lysed spinach chloroplasts
    • TAKAHASHI, Y., A. MITSUI and H. MATSUBARA, 1991b Formation of the Fe-S cluster of ferredoxin in lysed spinach chloroplasts. Plant Physiol. 95: 97-103.
    • (1991) Plant Physiol , vol.95 , pp. 97-103
    • TAKAHASHI, Y.1    MITSUI, A.2    MATSUBARA, H.3
  • 48
    • 5144230341 scopus 로고    scopus 로고
    • Nfu2: A scaffold protein required for [4Fe-4S] and ferredoxin iron-sulphur cluster assembly in Arabidopsis chloroplasts
    • TOURAINE, B., J. P. BOUTIN, A. MARION- POLL, J. F. BRIAT, G. PELTIER et al., 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
  • 49
    • 22144494670 scopus 로고    scopus 로고
    • Degenerate mitochondria
    • VAN DER GIEZEN, M., and J. TOVAR, 2005 Degenerate mitochondria. EMBO Rep. 6: 525-530.
    • (2005) EMBO Rep , vol.6 , pp. 525-530
    • VAN DER GIEZEN, M.1    TOVAR, J.2
  • 50
    • 34248379121 scopus 로고    scopus 로고
    • Chloroplast iron-sulfur cluster protein maturation requires the essential cysteine desulfurase CpNifS
    • VAN HOEWYK, D., S. E. ABDEL-GHANY, C. M. COHU, S. K. HERBERT, P. KUGRENS et al., 2007 Chloroplast iron-sulfur cluster protein maturation requires the essential cysteine desulfurase CpNifS. Proc. Natl. Acad. Sci. USA 104: 5686-5691.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 5686-5691
    • VAN HOEWYK, D.1    ABDEL-GHANY, S.E.2    COHU, C.M.3    HERBERT, S.K.4    KUGRENS, P.5
  • 51
    • 33644511398 scopus 로고    scopus 로고
    • AtSufE is an essential activator of plastidic and mitochondrial desulfurases in Arabidopsis
    • XU, X. M., and S. G. MøLLER, 2006 AtSufE is an essential activator of plastidic and mitochondrial desulfurases in Arabidopsis. EMBO J. 25: 900-909.
    • (2006) EMBO J , vol.25 , pp. 900-909
    • XU, X.M.1    MøLLER, S.G.2
  • 52
    • 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., K. MORIMOTO, S. KIKUCHI, K. NISHIO, I. TERASHIMA et al., 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
  • 53
    • 33646822978 scopus 로고    scopus 로고
    • CpSufE activates the cysteine desulfurase CpNifS for chloroplastic Fe-S cluster formation
    • YE, H., S. E. ABDEL-GHANY, T. D. ANDERSON, E. A. PILON-SMITS and M. PILON, 2006a CpSufE activates the cysteine desulfurase CpNifS for chloroplastic Fe-S cluster formation. J. Biol. Chem. 281: 8958-8969.
    • (2006) J. Biol. Chem , vol.281 , pp. 8958-8969
    • YE, H.1    ABDEL-GHANY, S.E.2    ANDERSON, T.D.3    PILON-SMITS, E.A.4    PILON, M.5
  • 54
    • 33745213111 scopus 로고    scopus 로고
    • CpNifS-dependent iron-sulfur cluster biogenesis in chloroplasts
    • YE, H., M. PILON and E. PILON-SMITS, 2006b CpNifS-dependent iron-sulfur cluster biogenesis in chloroplasts. New Phytol. 171: 285-292.
    • (2006) New Phytol , vol.171 , pp. 285-292
    • YE, H.1    PILON, M.2    PILON-SMITS, E.3
  • 55
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis
    • ZHENG, L., R. H. WHITE, V. L. CASH, R. F. JACK and D. R. DEAN, 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. USA , vol.90 , pp. 2754-2758
    • ZHENG, L.1    WHITE, R.H.2    CASH, V.L.3    JACK, R.F.4    DEAN, D.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.