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Volumn 185, Issue 1, 2003, Pages 98-106

Lack of the ApbC or ApbE protein results in a defect in Fe-S cluster metabolism in Salmonella enterica serovar typhimurium

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; IRON SULFUR PROTEIN; PROTEIN APBC; PROTEIN APBE; UNCLASSIFIED DRUG;

EID: 0037216551     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.1.98-106.2003     Document Type: Article
Times cited : (65)

References (63)
  • 1
    • 0031929614 scopus 로고    scopus 로고
    • The apbE gene encodes a lipoprotein involved in thiamine synthesis in Salmonella typhimurium
    • Beck, B. J., and D. M. Downs. 1998. The apbE gene encodes a lipoprotein involved in thiamine synthesis in Salmonella typhimurium, J. Bacteriol. 180:885-891.
    • (1998) J. Bacteriol. , vol.180 , pp. 885-891
    • Beck, B.J.1    Downs, D.M.2
  • 2
    • 0032720313 scopus 로고    scopus 로고
    • A periplasmic location is essential for the role of the ApbE lipoprotein in thiamine synthesis in Salmonella typhimurium
    • Beck, B. J., and D. M. Downs. 1999. A periplasmic location is essential for the role of the ApbE lipoprotein in thiamine synthesis in Salmonella typhimurium. J. Bacteriol. 181:7285-7290.
    • (1999) J. Bacteriol. , vol.181 , pp. 7285-7290
    • Beck, B.J.1    Downs, D.M.2
  • 3
    • 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
  • 4
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert, H., R. H. Holm, and E. Munck. 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
  • 5
    • 0032562758 scopus 로고    scopus 로고
    • Growth in iron-enriched medium partially compensates Escherichia coli for the lack of manganese and iron superoxide dismutase
    • Benov, L., and I. Fridovich. 1998. Growth in iron-enriched medium partially compensates Escherichia coli for the lack of manganese and iron superoxide dismutase. J. Biol. Chem. 273:10313-10316.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10313-10316
    • Benov, L.1    Fridovich, I.2
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 77956998704 scopus 로고
    • L-Threonine deaminase biosynthetic (Salmonella typhimurium)
    • Burns, R. O. 1971. L-Threonine deaminase biosynthetic (Salmonella typhimurium). Methods Enzymol. 17:555-560.
    • (1971) Methods Enzymol. , vol.17 , pp. 555-560
    • Burns, R.O.1
  • 9
    • 0042908615 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa hscA gene encodes Hsc66, a DnaK homologue
    • Campos-Garcia, J., G. O. L, and G. Soberon-Chavez. 2000. The Pseudomonas aeruginosa hscA gene encodes Hsc66, a DnaK homologue. Microbiology 146:1429-1435.
    • (2000) Microbiology , vol.146 , pp. 1429-1435
    • Campos-Garcia, J.G.O.L.1    Soberon-Chavez, G.2
  • 10
    • 0021324642 scopus 로고
    • Plasmid insertion mutagenesis and lac gene fusion with mini Mu bacteriophage transposons
    • Castilho, B, A., P. Olfson, and M. J. Casadaban. 1984, Plasmid insertion mutagenesis and lac gene fusion with mini Mu bacteriophage transposons. J. Bacteriol. 158:488-495.
    • (1984) J. Bacteriol. , vol.158 , pp. 488-495
    • Castilho, B.A.1    Olfson, P.2    Casadaban, M.J.3
  • 11
    • 0030846054 scopus 로고    scopus 로고
    • A new nos gene downstream from nosDFY is essential for dissimilatory reduction of nitrous oxide by Rhizobium (Sinorhizobium) meliloti
    • Chan, Y. K., W. A. McCormick, and R. J. Watson. 1997. A new nos gene downstream from nosDFY is essential for dissimilatory reduction of nitrous oxide by Rhizobium (Sinorhizobium) meliloti. Microbiology 143:2817-2824.
    • (1997) Microbiology , vol.143 , pp. 2817-2824
    • Chan, Y.K.1    McCormick, W.A.2    Watson, R.J.3
  • 12
    • 0025140554 scopus 로고
    • Transcription and regulation of expression of the Escherichia coli methionyl-tRNA synthetase gene
    • Dardel, F., M. Panvert, and G. Fayat. 1990. Transcription and regulation of expression of the Escherichia coli methionyl-tRNA synthetase gene. Mol. Gen. Genet. 223:121-133.
    • (1990) Mol. Gen. Genet. , vol.223 , pp. 121-133
    • Dardel, F.1    Panvert, M.2    Fayat, G.3
  • 13
    • 0001531847 scopus 로고    scopus 로고
    • Iron-sulfur proteins with nonredox functions
    • Flint, D. H., and R. M. Allen. 1996. Iron-sulfur proteins with nonredox functions. Chem. Rev. 96:2315-2334.
    • (1996) Chem. Rev. , vol.96 , pp. 2315-2334
    • Flint, D.H.1    Allen, R.M.2
  • 14
    • 0030993117 scopus 로고    scopus 로고
    • Superoxide-driven aconitase FE-S center cycling
    • Gardner, P. R. 1997. Superoxide-driven aconitase FE-S center cycling. Biosci. Rep. 17:33-42.
    • (1997) Biosci. Rep. , vol.17 , pp. 33-42
    • Gardner, P.R.1
  • 15
    • 0027274755 scopus 로고
    • Effect of glutathione on aconitase in Escherichia coli
    • Gardner, P. R., and I. Fridovich. 1993. Effect of glutathione on aconitase in Escherichia coli. Arch. Biochem. Biophys. 301:98-102.
    • (1993) Arch. Biochem. Biophys. , vol.301 , pp. 98-102
    • Gardner, P.R.1    Fridovich, I.2
  • 16
    • 0034940979 scopus 로고    scopus 로고
    • Protection from superoxide damage associated with an increased level of the YggX protein in Salmonella enterica
    • Gralnick, J., and D. Downs. 2001. Protection from superoxide damage associated with an increased level of the YggX protein in Salmonella enterica. Proc. Natl. Acad. Sci. USA 98:8030-8035.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8030-8035
    • Gralnick, J.1    Downs, D.2
  • 17
    • 0033821173 scopus 로고    scopus 로고
    • Lesions in gshA (encoding gamma-L-glutamyl-L-cysteine synthetase) prevent aerobic synthesis of thiamine in Salmonella enterica serovar typhimurium LT2
    • Gralnick, J., E. Webb, B. Beck, and D. Downs. 2000. Lesions in gshA (encoding gamma-L-glutamyl-L-cysteine synthetase) prevent aerobic synthesis of thiamine in Salmonella enterica serovar typhimurium LT2. J. Bacteriol. 182:5180-5187.
    • (2000) J. Bacteriol. , vol.182 , pp. 5180-5187
    • Gralnick, J.1    Webb, E.2    Beck, B.3    Downs, D.4
  • 18
    • 0036196173 scopus 로고    scopus 로고
    • Members of the Fur protein family regulate iron and zinc transport in E. coli and characteristics of the Fur-regulated fhuF protein
    • Hantke, K. 2002. Members of the Fur protein family regulate iron and zinc transport in E. coli and characteristics of the Fur-regulated fhuF protein. J. Mol. Microbiol. Biotechnol. 4:217-222.
    • (2002) J. Mol. Microbiol. Biotechnol. , vol.4 , pp. 217-222
    • Hantke, K.1
  • 19
    • 0035901493 scopus 로고    scopus 로고
    • Structural and functional studies of MinD ATPase: Implications for the molecular recognition of the bacterial cell division apparatus
    • Hayashi, I., T. Oyama, and K. Morikawa. 2001. Structural and functional studies of MinD ATPase: Implications for the molecular recognition of the bacterial cell division apparatus. EMBO J. 20:1819-1828.
    • (2001) EMBO J. , vol.20 , pp. 1819-1828
    • Hayashi, I.1    Oyama, T.2    Morikawa, K.3
  • 20
    • 0032541496 scopus 로고    scopus 로고
    • Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E. coli
    • Hesterkamp, T., and B. Bukau. 1998. Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E. coli. EMBO J. 17:4818-4828.
    • (1998) EMBO J. , vol.17 , pp. 4818-4828
    • Hesterkamp, T.1    Bukau, B.2
  • 21
    • 0030589485 scopus 로고    scopus 로고
    • The identification a novel gene required for lipopolysaccharide biosynthesis by Haemophilus influenzae RM7004, with transposon Tn916 mutagenesis
    • High, N. J., M. E. Deadman, D. W. Hood, and E. R. Moxon. 1996. The identification a novel gene required for lipopolysaccharide biosynthesis by Haemophilus influenzae RM7004, with transposon Tn916 mutagenesis. FEMS Microbiol. Lett. 145:325-331.
    • (1996) FEMS Microbiol. Lett. , vol.145 , pp. 325-331
    • High, N.J.1    Deadman, M.E.2    Hood, D.W.3    Moxon, E.R.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
    • Hoff, K. G., J. J. Silberg, and L. E. Vickery. 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. USA , vol.97 , pp. 7790-7795
    • Hoff, K.G.1    Silberg, J.J.2    Vickery, L.E.3
  • 23
    • 0036135646 scopus 로고    scopus 로고
    • Transcription factor FnrP from Paracoccus denitrificans contains an iron-sulfur cluster and is activated by anoxia: Identification of essential cysteine residues
    • Hutchings, M. I., J. C. Crack, N. Shearer, B. J. Thompson, A. J. Thomson, and S. Spiro. 2002. Transcription factor FnrP from Paracoccus denitrificans contains an iron-sulfur cluster and is activated by anoxia: Identification of essential cysteine residues. J. Bacteriol. 184:503-508.
    • (2002) J. Bacteriol. , vol.184 , pp. 503-508
    • Hutchings, M.I.1    Crack, J.C.2    Shearer, N.3    Thompson, B.J.4    Thomson, A.J.5    Spiro, S.6
  • 24
    • 0034107324 scopus 로고    scopus 로고
    • Role of Saccharomyces cerevisiae ISA1 and ISA2 in iron homeostasis
    • Jensen, L. T., and V. C. Culotta. 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
  • 25
    • 0035914323 scopus 로고    scopus 로고
    • Purification and characterization of membrane-associated CooC protein and its functional role in the insertion of nickel into carbon monoxide
    • Jeon, W., J. Cheng, and P. Ludden. 2001. Purification and characterization of membrane-associated CooC protein and its functional role in the insertion of nickel into carbon monoxide. J. Biol. Chem. 276:38602-38609.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38602-38609
    • Jeon, W.1    Cheng, J.2    Ludden, P.3
  • 26
    • 0032043449 scopus 로고    scopus 로고
    • Iron-sulfur proteins: New roles for old clusters
    • Johnson, M. K. 1998. Iron-sulfur proteins: New roles for old clusters. Curr. Opin. Chem. Biol. 2:173-181.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 173-181
    • Johnson, M.K.1
  • 27
    • 0034646676 scopus 로고    scopus 로고
    • Evidence for the transfer of sulfane sulfur from IscS to Thil during the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA
    • Kambampati, R., and C. T. Lauhon. 2000. Evidence for the transfer of sulfane sulfur from IscS to Thil during the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA J. Biol. Chem. 275:10727-10730.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10727-10730
    • Kambampati, R.1    Lauhon, C.T.2
  • 28
    • 0033554855 scopus 로고    scopus 로고
    • IscS is a sulfurtransferase for the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA
    • Kambampati, R., and C. T. Lauhon. 1999. IscS is a sulfurtransferase for the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA. Biochemistry 38:16561-16568.
    • (1999) Biochemistry , vol.38 , pp. 16561-16568
    • Kambampati, R.1    Lauhon, C.T.2
  • 29
    • 0034097778 scopus 로고    scopus 로고
    • Contribution of cysteine desulfurase (NifS protein) to the biotin synthase reaction of Escherichia coli
    • Kiyasu, T., A. Asakura, Y. Nagahashi, and T. Hoshino. 2000. Contribution of cysteine desulfurase (NifS protein) to the biotin synthase reaction of Escherichia coli. J. Bacteriol. 182:2879-2885.
    • (2000) J. Bacteriol. , vol.182 , pp. 2879-2885
    • Kiyasu, T.1    Asakura, A.2    Nagahashi, Y.3    Hoshino, T.4
  • 31
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., J. D. Roberts, and R. A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 32
    • 0033953353 scopus 로고    scopus 로고
    • A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins
    • Lange, H., A. Kaut, G. Kispal, and R. Lill. 2000. A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins. Proc. Natl. Acad. Sci. USA 97:1050-1055.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1050-1055
    • Lange, H.1    Kaut, A.2    Kispal, G.3    Lill, R.4
  • 33
    • 0023267311 scopus 로고
    • Toxic accumulation of α-ketobutyrate caused by inhibition of the branched-chain amino acid biosynthetic enzyme acetolactate synthase in Salmonella typhimurium
    • LaRossa, R. A., T. K. Van Dyk, and D. R. Smulski. 1987. Toxic accumulation of α-ketobutyrate caused by inhibition of the branched-chain amino acid biosynthetic enzyme acetolactate synthase in Salmonella typhimurium. J. Bacteriol. 169:1372-1378.
    • (1987) J. Bacteriol. , vol.169 , pp. 1372-1378
    • LaRossa, R.A.1    Van Dyk, T.K.2    Smulski, D.R.3
  • 34
    • 0034255836 scopus 로고    scopus 로고
    • Maturation of cellular Fe-S proteins: An essential function of mitochondria
    • Lill, R., and G. Kispal 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
  • 35
    • 0037077310 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis. Thermatoga maritima IscU is a structured iron-sulfur cluster assembly protein
    • Mansy, S. S., G. Wu, K. K. Surerus, and J. A. Cowan. 2002. Iron-sulfur cluster biosynthesis. Thermatoga maritima IscU is a structured iron-sulfur cluster assembly protein. J. Biol. Chem. 277:21397-21404.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21397-21404
    • Mansy, S.S.1    Wu, G.2    Surerus, K.K.3    Cowan, J.A.4
  • 36
    • 0023787932 scopus 로고
    • pACYC184-derived cloning vectors containing the multiple cloning site and lacAa reporter gene of pUC8/9 and pUC18/19 plasmids
    • Martinez, E., B. Bartolome, and F. de la Cruz. 1988. pACYC184-derived cloning vectors containing the multiple cloning site and lacAa reporter gene of pUC8/9 and pUC18/19 plasmids. Gene 68:159-162.
    • (1988) Gene , vol.68 , pp. 159-162
    • Martinez, E.1    Bartolome, B.2    De la Cruz, F.3
  • 37
    • 0034093325 scopus 로고    scopus 로고
    • Kinetic and mutational studies of three NifS homologs from Escherichia coli: Mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions
    • Mihara, H., T. Kurihara, T. Yoshimura, and N. Esaki. 2000. Kinetic and mutational studies of three NifS homologs from Escherichia coli: Mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions. J. Biochem. (Tokyo) 127:559-567.
    • (2000) J. Biochem. (Tokyo) , vol.127 , pp. 559-567
    • Mihara, H.1    Kurihara, T.2    Yoshimura, T.3    Esaki, N.4
  • 38
    • 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 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
    • Muhlenhoff, U.1    Lill, R.2
  • 39
    • 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., M. El Hassouni, L. Loiseau, D. Expert, and F. Barras. 2001. SoxR-dependent response to oxidative stress and virulence of Erwinia chrysanthemi: The key role of SufC, an orphan ABC ATPase. Mol. Microbiol. 39:960-972.
    • (2001) Mol. Microbiol. , vol.39 , pp. 960-972
    • Nachin, L.1    El Hassouni, M.2    Loiseau, L.3    Expert, D.4    Barras, F.5
  • 40
    • 0035933791 scopus 로고    scopus 로고
    • Iron-sulfur cluster assembly: Characterization of IscA and evidence for a specific and functional complex with ferredoxin
    • Ollagnier-de-Choudens, S., T. Mattioli, Y. Takahashi, and M. Fontecave. 2001. Iron-sulfur cluster assembly: Characterization of IscA and evidence for a specific and functional complex with ferredoxin. J. Biol. Chem. 276:22604-22607.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22604-22607
    • Ollagnier-de-Choudens, S.1    Mattioli, T.2    Takahashi, Y.3    Fontecave, M.4
  • 41
    • 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 K. Hantke. 1999. SufS is a NifS-like protein, and SufD is necessary for stability of the [2Fe-2S] FhuF protein in Escherichia coli. J. Bacteriol. 181:3307-3309.
    • (1999) J. Bacteriol. , vol.181 , pp. 3307-3309
    • Patzer, S.I.1    Hantke, K.2
  • 42
    • 0029796311 scopus 로고    scopus 로고
    • Mutations in apbC (mrp) prevent function of the alternative pyrimidine biosynthetic pathway in Salmonella typhimurium
    • Petersen, L., and D. M. Downs. 1996. Mutations in apbC (mrp) prevent function of the alternative pyrimidine biosynthetic pathway in Salmonella typhimurium. J. Bacteriol. 178:5676-5682.
    • (1996) J. Bacteriol. , vol.178 , pp. 5676-5682
    • Petersen, L.1    Downs, D.M.2
  • 44
    • 0033538446 scopus 로고    scopus 로고
    • In vitro biosynthesis of iron-molybdenum cofactor and maturation of the nif-encoded apodinitrogenase. Effect of substitution for NifH with site-specifically altered forms of NifH
    • Rangaraj, P., M. J. Ryle, W. N. Lanzilotta, P. W. Ludden, and V. K. Shah. 1999. In vitro biosynthesis of iron-molybdenum cofactor and maturation of the nif-encoded apodinitrogenase. Effect of substitution for NifH with site-specifically altered forms of NifH J. Biol. Chem. 274:19778-19784.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19778-19784
    • Rangaraj, P.1    Ryle, M.J.2    Lanzilotta, W.N.3    Ludden, P.W.4    Shah, V.K.5
  • 45
    • 0030826663 scopus 로고    scopus 로고
    • ApoNifH functions in iron-molybdenum cofactor synthesis and apodinitrogenase maturation
    • Rangaraj, P., P. Shah, and P. Ludden. 1997. ApoNifH functions in iron-molybdenum cofactor synthesis and apodinitrogenase maturation. Proc. Natl. Acad. Sci. USA 94:11250-11255.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11250-11255
    • Rangaraj, P.1    Shah, P.2    Ludden, P.3
  • 46
    • 0029930904 scopus 로고    scopus 로고
    • Iron-sulfur clusters as biosensors of oxidants and iron
    • Rouault, T. A., and R. D. Klausner. 1996. Iron-sulfur clusters as biosensors of oxidants and iron. Trends Biochem. Sci. 21:174-177.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 174-177
    • Rouault, T.A.1    Klausner, R.D.2
  • 47
    • 0033811104 scopus 로고    scopus 로고
    • The NosX and NirX proteins of Paracoccus denitrificans are functional homologues: Their role in maturation of nitrous oxide reductase
    • Saunders, N. F. W., J. J. Hornberg, W. N. M. Reijnders, H. V. Westerhoff, S. D. E. Vries, and R. J. M. Van Spanning. 2000. The NosX and NirX proteins of Paracoccus denitrificans are functional homologues: Their role in maturation of nitrous oxide reductase. J. Bacteriol. 182:5211-5217.
    • (2000) J. Bacteriol. , vol.182 , pp. 5211-5217
    • Saunders, N.F.W.1    Hornberg, J.J.2    Reijnders, W.N.M.3    Westerhoff, H.V.4    Vries, S.D.E.5    Van Spanning, R.J.M.6
  • 48
    • 0027131592 scopus 로고
    • Identification of a new class of nitrogen fixation genes in Rhodobacter capsulatus: A putative membrane complex involved in electron transport to nitrogenase
    • Schmehl, M., A. Jahn, A. Meyer zu Vilsendorf, S. Hennecke, B. Masepohl, M. Schuppler, M. Marxer, J. Oelze, and W. Klipp 1993. Identification of a new class of nitrogen fixation genes in Rhodobacter capsulatus: A putative membrane complex involved in electron transport to nitrogenase. Mol. Gen. Genet. 241:602-615.
    • (1993) Mol. Gen. Genet. , vol.241 , pp. 602-615
    • Schmehl, M.1    Jahn, A.2    Meyer zu Vilsendorf, A.3    Hennecke, S.4    Masepohl, B.5    Schuppler, M.6    Marxer, M.7    Oelze, J.8    Klipp, W.9
  • 49
    • 0034255455 scopus 로고    scopus 로고
    • The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli
    • Schwartz, C. J., O. Djaman, J. A. Imlay, and P. J. Kiley. 2000. The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli. Proc. Natl. Acad. Sci. USA 97:9009-9014.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9009-9014
    • Schwartz, C.J.1    Djaman, O.2    Imlay, J.A.3    Kiley, P.J.4
  • 50
    • 0035909963 scopus 로고    scopus 로고
    • IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins
    • Schwartz, C. J., J. L. Giel, T. Patschkowski, C. Luther, F. J. Ruzicka, H. Beinert, and P. J. Kiley. 2001. IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins. Proc. Natl. Acad. Sci. USA 98:14895-14900.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14895-14900
    • Schwartz, C.J.1    Giel, J.L.2    Patschkowski, T.3    Luther, C.4    Ruzicka, F.J.5    Beinert, H.6    Kiley, P.J.7
  • 51
    • 0034859174 scopus 로고    scopus 로고
    • Incorporation of iron-sulphur clusters in membrane-bound proteins
    • Seidler, A., K. Jaschkowitz, and M. Wollenberg. 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
  • 52
    • 0033942998 scopus 로고    scopus 로고
    • Metabolic defects caused by mutations in the isc gene cluster in Salmonella enterica serovar Typhimurium: Implications for thiamine synthesis
    • Skovran, E., and D. M. Downs. 2000. Metabolic defects caused by mutations in the isc gene cluster in Salmonella enterica serovar Typhimurium: Implications for thiamine synthesis. J. Bacteriol. 182:3896-3903.
    • (2000) J. Bacteriol. , vol.182 , pp. 3896-3903
    • Skovran, E.1    Downs, D.M.2
  • 54
    • 0035282866 scopus 로고    scopus 로고
    • Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization with new analysis and information visualization methods
    • Sofia, H. J., G. Chen, B. G. Hetzler, J. F. Reyes-Spindola, and N. E. Miller. 2001. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization with new analysis and information visualization methods. Nucleic Acids Res. 29:1097-1106.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3    Reyes-Spindola, J.F.4    Miller, N.E.5
  • 55
    • 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., L. B. Sanchez, and M. Muller. 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    Sanchez, L.B.2    Muller, M.3
  • 56
    • 0032725568 scopus 로고    scopus 로고
    • Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster involved in the assembly of Fe-S clusters in Escherichia coli
    • Takahashi, Y., and M. Nakamura. 1999. Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster involved in the assembly of Fe-S clusters in Escherichia coli. J. Biochem. (Tokyo) 126:917-926.
    • (1999) J. Biochem. (Tokyo) , vol.126 , pp. 917-926
    • Takahashi, Y.1    Nakamura, M.2
  • 57
    • 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 Y. Takahashi. 2001. Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins. J. Biochem. (Tokyo) 130:63-71.
    • (2001) J. Biochem. (Tokyo) , vol.130 , pp. 63-71
    • Tokumoto, U.1    Takahashi, Y.2
  • 58
    • 0012193852 scopus 로고    scopus 로고
    • Transfer of sulfur from IscS to IscU during Fe/S cluster assembly
    • Urbina, H. D., J. J. Silberg, K. G. Hoff, and L. E. Vickery. 2001. Transfer of sulfur from IscS to IscU during Fe/S cluster assembly. J. Biol. Chem. 27:445244526.
    • (2001) J. Biol. Chem. , vol.27 , pp. 445244526
    • Urbina, H.D.1    Silberg, J.J.2    Hoff, K.G.3    Vickery, L.E.4
  • 59
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., M. Saraste, M. J. Runswick, and N. J. Gay. 1982. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1:945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 60
    • 0021681568 scopus 로고
    • New Tn10 derivatives for transposon mutagenesis and for construction of lacZ operon fusions by transposition
    • Way, J. C., M. A. Davis, D. Morisato, D. E. Roberts, and N. Kleckner. 1984. New Tn10 derivatives for transposon mutagenesis and for construction of lacZ operon fusions by transposition. Gene 32:369-379.
    • (1984) Gene , vol.32 , pp. 369-379
    • Way, J.C.1    Davis, M.A.2    Morisato, D.3    Roberts, D.E.4    Kleckner, N.5
  • 62
    • 0032557666 scopus 로고    scopus 로고
    • Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii
    • Zheng, L., V. L. Cash, D. H. Flint, and D. R. Dean. 1998. Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii. J. Biol. Chem. 273:13264-13272.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13264-13272
    • Zheng, L.1    Cash, V.L.2    Flint, D.H.3    Dean, D.R.4
  • 63
    • 0034932337 scopus 로고    scopus 로고
    • DNA microarray transcriptional profiling of the Escherichia coli response to hydrogen peroxide
    • Zheng, M., X. Wang, L. J. Templeton, D. R. Smulski, R. A. LaRossa, and G. Storz. 2001. DNA microarray 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


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