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Volumn 1804, Issue 7, 2010, Pages 1476-1482

SufS protein from Haloferax volcanii involved in Fe-S cluster assembly in haloarchaea

Author keywords

Archaea; Cysteine desulphurases; Fe S cluster; Haloarchaea

Indexed keywords

ALANINE; BACTERIAL PROTEIN; CYSTATHIONINE GAMMA LYASE; CYSTEINE; FERREDOXIN; IRON; PROTEIN SUFS; SULFUR; UNCLASSIFIED DRUG;

EID: 77952421991     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.03.001     Document Type: Article
Times cited : (15)

References (38)
  • 2
    • 0035219736 scopus 로고    scopus 로고
    • Biosynthesis of biotin and lipoic acid
    • Marquet A., Bui B.T., and Florentin D. Biosynthesis of biotin and lipoic acid. Vitam. Horm. 61 (2001) 51-101
    • (2001) Vitam. Horm. , vol.61 , pp. 51-101
    • Marquet, A.1    Bui, B.T.2    Florentin, D.3
  • 3
    • 33750083296 scopus 로고    scopus 로고
    • Enzymatic activation of sulfur for incorporation into biomolecules in prokaryotes
    • Kessler D. Enzymatic activation of sulfur for incorporation into biomolecules in prokaryotes. FEMS Microbiol. Rev. 30 (2006) 825-840
    • (2006) FEMS Microbiol. Rev. , vol.30 , pp. 825-840
    • Kessler, D.1
  • 4
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis
    • Zheng L., White R.H., Cash V.L., Jack R.F., and Dean D.R. Cysteine desulfurase activity 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    White, R.H.2    Cash, V.L.3    Jack, R.F.4    Dean, D.R.5
  • 5
    • 0028339794 scopus 로고
    • Catalytic Formation of a Nitrogenase Iron-Sulfur Cluster
    • Zheng L., and Dean D.R. Catalytic Formation of a Nitrogenase Iron-Sulfur Cluster. J. Biol. Chem. 269 (1994) 18723-18726
    • (1994) J. Biol. Chem. , vol.269 , pp. 18723-18726
    • Zheng, L.1    Dean, D.R.2
  • 6
    • 0037209757 scopus 로고    scopus 로고
    • Bacterial cysteine desulfurases: their function and mechanisms
    • Mihara H., and Esaki N. Bacterial cysteine desulfurases: their function and mechanisms. Appl. Microbiol. Biotechnol. 60 (2002) 12-23
    • (2002) Appl. Microbiol. Biotechnol. , vol.60 , pp. 12-23
    • Mihara, H.1    Esaki, N.2
  • 7
    • 20744446399 scopus 로고    scopus 로고
    • Structure, Function, and Formation of Biological Iron-Sulfur Clusters
    • Johnson D.C., Dean D.R., Smith A.D., and Johnson M.K. 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
  • 10
    • 0034719118 scopus 로고    scopus 로고
    • Characterization of the NifU and NifS Fe-S cluster formation proteins essential for viability in Helicobacter pylori
    • Olson J.W., Agar J.N., Johnson M.K., and Maier R.J. Characterization of the NifU and NifS Fe-S cluster formation proteins essential for viability in Helicobacter pylori. Biochemistry 39 (2000) 16213-16219
    • (2000) Biochemistry , vol.39 , pp. 16213-16219
    • Olson, J.W.1    Agar, J.N.2    Johnson, M.K.3    Maier, R.J.4
  • 11
    • 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
    • Ali V., Shigeta Y., Tokumoto U., Takahashi Y., and Nozaki T. 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    Shigeta, Y.2    Tokumoto, U.3    Takahashi, Y.4    Nozaki, T.5
  • 12
    • 0032557666 scopus 로고    scopus 로고
    • Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii
    • Zheng L., Cash V.L., Flint D.H., and Dean D.R. 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
  • 13
    • 0034911990 scopus 로고    scopus 로고
    • Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins
    • Tokumoto U., and Takahashi Y. Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins. J. Biochem. 130 (2001) 63-71
    • (2001) J. Biochem. , vol.130 , pp. 63-71
    • Tokumoto, U.1    Takahashi, Y.2
  • 14
    • 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. Cysteine sulfinate desulfinase, a NifS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. J. Biol. Chem. 272 (1997) 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
  • 15
    • 0033591390 scopus 로고    scopus 로고
    • A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase
    • Mihara H., Maeda M., Fujii T., Kurihara T., Hata Y., and Esaki N. A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase. J. Biol. Chem. 274 (1999) 14768-14772
    • (1999) J. Biol. Chem. , vol.274 , pp. 14768-14772
    • Mihara, H.1    Maeda, M.2    Fujii, T.3    Kurihara, T.4    Hata, Y.5    Esaki, N.6
  • 16
    • 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. 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    Ollagnier-de-Choudens, S.2    Nachin, L.3    Fontecave, M.4    Barras, F.5
  • 17
    • 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., Wood M.J., Muñoz F.M., and Storz G. 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 (2003) 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
  • 18
    • 0032933919 scopus 로고    scopus 로고
    • SufS is a NifS-Like protein, and SufD is necessary for stability of the [2Fe-2S] FhuF protein in Escherichia coli
    • Patzer S.I., and Hantke K. SufS is a NifS-Like protein, and SufD is necessary for stability of the [2Fe-2S] FhuF protein in Escherichia coli. J. Bacteriol. 181 (1999) 3307-3309
    • (1999) J. Bacteriol. , vol.181 , pp. 3307-3309
    • Patzer, S.I.1    Hantke, K.2
  • 19
    • 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. SoxR-dependent response to oxidative stress and virulence of Erwinia chrysanthemi: the key role of SufC, an orphan ABC ATPase. Mol. Microbiol. 39 (2001) 960-972
    • (2001) Mol. Microbiol. , vol.39 , pp. 960-972
    • Nachin, L.1    El Hassouni, M.2    Loiseau, L.3    Expert, D.4    Barras, F.5
  • 20
    • 33947540909 scopus 로고    scopus 로고
    • The SUF iron-sulfur cluster biosynthetic machinery: Sulfur transfer from the SUFS-SUFE complex to SUFA
    • Sendra M., Ollagnier de Choudens S., Lascouxb D., Sanakis Y., and Fontecave M. The SUF iron-sulfur cluster biosynthetic machinery: Sulfur transfer from the SUFS-SUFE complex to SUFA. FEBS Lett. 581 (2007) 1362-1368
    • (2007) FEBS Lett. , vol.581 , pp. 1362-1368
    • Sendra, M.1    Ollagnier de Choudens, S.2    Lascouxb, D.3    Sanakis, Y.4    Fontecave, M.5
  • 21
    • 0029042171 scopus 로고
    • Acidic residues important for substrate binding and cofactor reactivity in eukaryotic ornithine decarboxylase identified by alanine scanning mutagenesis
    • Osterman A.L., Kinch N., L.N., Grishin N.V., and Phillips M.A. Acidic residues important for substrate binding and cofactor reactivity in eukaryotic ornithine decarboxylase identified by alanine scanning mutagenesis. J. Biol. Chem. 270 (1995) 11797-11802
    • (1995) J. Biol. Chem. , vol.270 , pp. 11797-11802
    • Osterman, A.L.1    Kinch, N.2    Grishin, N.V.3    Phillips, M.A.4
  • 22
    • 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. A novel L-Cysteine/Cystine C-S-Lyase directing [2Fe-2S] cluster formation of Synechocystis ferredoxin. J. Biol. Chem. 272 (1997) 10442-10447
    • (1997) J. Biol. Chem. , vol.272 , pp. 10442-10447
    • Leibrecht, I.1    Kessler, D.2
  • 23
    • 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. Evidence for cysteine persulfide as reaction product of L-Cyst(e)ine C-S-Lyase (C-DES) from Synechocystis. J. Biol. Chem. 274 (1999) 189-195
    • (1999) J. Biol. Chem. , vol.274 , pp. 189-195
    • Lang, T.1    Kessler, D.2
  • 25
    • 0033526898 scopus 로고    scopus 로고
    • Expression, reactivation, and purification of enzymes from Haloferax volcanii in Escherichia coli
    • Connaris H., Chaudhuri J.B., Danson M.J., and Hough D.W. Expression, reactivation, and purification of enzymes from Haloferax volcanii in Escherichia coli. Biotechnol. Bioeng. 64 (1999) 38-45
    • (1999) Biotechnol. Bioeng. , vol.64 , pp. 38-45
    • Connaris, H.1    Chaudhuri, J.B.2    Danson, M.J.3    Hough, D.W.4
  • 26
    • 0000904065 scopus 로고
    • A direct microdetermination for sulfide
    • Siegel L.M. A direct microdetermination for sulfide. Anal. Biochem. 11 (1965) 126-132
    • (1965) Anal. Biochem. , vol.11 , pp. 126-132
    • Siegel, L.M.1
  • 28
    • 35748982883 scopus 로고    scopus 로고
    • Spectopotentiometric properties and salt-dependent thermotolerance of a [2Fe-2S] ferredoxin-involved nitrate assimilation in Haloferax mediterranei
    • Martínez-Espinosa R.M., Richardson D.J., Butt J.N., and Bonete M.J. Spectopotentiometric properties and salt-dependent thermotolerance of a [2Fe-2S] ferredoxin-involved nitrate assimilation in Haloferax mediterranei. FEMS Microbiol. Lett. 277 (2007) 50-55
    • (2007) FEMS Microbiol. Lett. , vol.277 , pp. 50-55
    • Martínez-Espinosa, R.M.1    Richardson, D.J.2    Butt, J.N.3    Bonete, M.J.4
  • 29
    • 0034725582 scopus 로고    scopus 로고
    • Transfer of iron-sulfur cluster from NifU to apoferredoxin
    • Nishio K., and Nakai M. 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
  • 30
    • 0022313128 scopus 로고
    • Silver staining of proteins in polyacrylamide gels: Increased sensitivity through a combined Coomassie blue-silver stain procedure
    • De Moreno M.R., Smith J.F., and Smith R.V. Silver staining of proteins in polyacrylamide gels: Increased sensitivity through a combined Coomassie blue-silver stain procedure. Anal. Biochem. 151 (1985) 466-470
    • (1985) Anal. Biochem. , vol.151 , pp. 466-470
    • De Moreno, M.R.1    Smith, J.F.2    Smith, R.V.3
  • 31
    • 0031195026 scopus 로고    scopus 로고
    • The structural basis of protein halophilicity
    • Danson M.J., and Hough D.W. The structural basis of protein halophilicity. Comp. Biochem. Physiol. 117 (1997) 307-312
    • (1997) Comp. Biochem. Physiol. , vol.117 , pp. 307-312
    • Danson, M.J.1    Hough, D.W.2
  • 32
    • 4644275046 scopus 로고    scopus 로고
    • Kinetic and structural characterization of Slr0077/SufS, the essential cysteine desulfurase from Synechocystis sp. PCC 6803
    • Tirupati B., Vey J.L., Drennan C.L., and Bollinger J.M. Kinetic and structural characterization of Slr0077/SufS, the essential cysteine desulfurase from Synechocystis sp. PCC 6803. Biochemistry 43 (2004) 12210-12219
    • (2004) Biochemistry , vol.43 , pp. 12210-12219
    • Tirupati, B.1    Vey, J.L.2    Drennan, C.L.3    Bollinger, J.M.4
  • 33
    • 0029994972 scopus 로고    scopus 로고
    • Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: enzyme purification, characterisation and N-terminal sequence
    • Bonete M.J., Pire C., Llorca F.I., and Camacho M.L. Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: enzyme purification, characterisation and N-terminal sequence. FEBS Lett. 383 (1996) 227-229
    • (1996) FEBS Lett. , vol.383 , pp. 227-229
    • Bonete, M.J.1    Pire, C.2    Llorca, F.I.3    Camacho, M.L.4
  • 34
    • 0036562516 scopus 로고    scopus 로고
    • Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: Implications for its specificity toward selenocysteine
    • Mihara H., Fujii T., Kato S.-I., Kurihara T., Hata Y., and Esaki N. Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: Implications for its specificity toward selenocysteine. J. Biochem. 131 (2002) 679-685
    • (2002) J. Biochem. , vol.131 , pp. 679-685
    • Mihara, H.1    Fujii, T.2    Kato, S.-I.3    Kurihara, T.4    Hata, Y.5    Esaki, N.6
  • 35
    • 0031688651 scopus 로고    scopus 로고
    • Operation of glyoxylate cycle in halophilic archaea: presence of malate synthase and isocitrate lyase in Haloferax volcanii
    • Serrano J.A., Camacho M., and Bonete M.J. Operation of glyoxylate cycle in halophilic archaea: presence of malate synthase and isocitrate lyase in Haloferax volcanii. FEBS Lett. 434 (1998) 13-16
    • (1998) FEBS Lett. , vol.434 , pp. 13-16
    • Serrano, J.A.1    Camacho, M.2    Bonete, M.J.3
  • 36
    • 0035948221 scopus 로고    scopus 로고
    • Heterologous overexpression of glucose dehydrogenase from the halophilic archaeon Haloferax mediterranei, an enzyme of the medium chain dehydrogenase/reductase family
    • Pire C., Esclapez J., Ferrer J., and Bonete M.J. Heterologous overexpression of glucose dehydrogenase from the halophilic archaeon Haloferax mediterranei, an enzyme of the medium chain dehydrogenase/reductase family. FEMS Microbiol. Lett. 200 (2001) 221-227
    • (2001) FEMS Microbiol. Lett. , vol.200 , pp. 221-227
    • Pire, C.1    Esclapez, J.2    Ferrer, J.3    Bonete, M.J.4
  • 37
    • 0035868537 scopus 로고    scopus 로고
    • Purification and characterisation of a possible assimilatory nitrite reductase from the halophile archaeon Haloferax mediterranei
    • Martínez-Espinosa R.M., Marhuenda-Egea F.C., and Bonete M.J. Purification and characterisation of a possible assimilatory nitrite reductase from the halophile archaeon Haloferax mediterranei. FEMS Microbiol. Lett. 196 (2001) 113-118
    • (2001) FEMS Microbiol. Lett. , vol.196 , pp. 113-118
    • Martínez-Espinosa, R.M.1    Marhuenda-Egea, F.C.2    Bonete, M.J.3
  • 38
    • 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 S.E., and Bollinger J.M. Mechanism of cysteine desulfurase Slr0387 from Synechocystis sp. PCC 6803: Kinetic analysis of cleavage of the persulfide Intermediate by chemical reductants. Biochemistry 43 (2004) 12220-12226
    • (2004) Biochemistry , vol.43 , pp. 12220-12226
    • Behshad, E.1    Parkin, S.E.2    Bollinger, J.M.3


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