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Volumn 70, Issue 8, 2004, Pages 4491-4498

Differential protein expression during growth of Acidithiobacillus ferooxidans on ferrous iron, sulfur compounds, or metal sulfides

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; GENES; POLYSACCHARIDES; PROTEINS; SULFUR COMPOUNDS;

EID: 4143137531     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.70.8.4491-4498.2004     Document Type: Article
Times cited : (124)

References (45)
  • 3
    • 0027978204 scopus 로고
    • The partial removal of lipopolysaccharide from Thiobacillus ferrooxidans affects its attachment to solids
    • Arredondo, R., A. García, and C. A. Jerez. 1994. The partial removal of lipopolysaccharide from Thiobacillus ferrooxidans affects its attachment to solids. Appl. Environ. Microbiol. 60:2846-2851.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 2846-2851
    • Arredondo, R.1    García, A.2    Jerez, C.A.3
  • 4
    • 0021955321 scopus 로고
    • Long-chain fatty acid transport in Escherichia coli. Cloning, mapping, and expression of the fadL gene
    • Black, P. N., S. F. Kianian, C. C. DiRusso, and D. N. William. 1985. Long-chain fatty acid transport in Escherichia coli. Cloning, mapping, and expression of the fadL gene. J. Biol. Chem. 260:1780-1789.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1780-1789
    • Black, P.N.1    Kianian, S.F.2    DiRusso, C.C.3    William, D.N.4
  • 5
    • 0028108228 scopus 로고
    • Respiratory enzymes of Thiobacillus ferrooxidans: Kinetic properties of an acid-stable iron:rusticyanin oxidoreductase
    • Blake, R. C., II, and E. A. Shute. 1994. Respiratory enzymes of Thiobacillus ferrooxidans: kinetic properties of an acid-stable iron:rusticyanin oxidoreductase. Biochemistry 33:9220-9228.
    • (1994) Biochemistry , vol.33 , pp. 9220-9228
    • Blake II, R.C.1    Shute, E.A.2
  • 7
    • 0033010836 scopus 로고    scopus 로고
    • A novel gene encoding a sulfur-regulated outer membrane protein in Thiobacillus ferrooxidans
    • Buonfiglio, V., M. Polidoro, F. Soyer, P. Valenti, and J. Shively. 1999. A novel gene encoding a sulfur-regulated outer membrane protein in Thiobacillus ferrooxidans. J. Biotechnol. 72:85-93.
    • (1999) J. Biotechnol. , vol.72 , pp. 85-93
    • Buonfiglio, V.1    Polidoro, M.2    Soyer, F.3    Valenti, P.4    Shively, J.5
  • 8
    • 0001165287 scopus 로고
    • The role of rusticyanin, a blue copper protein, in the electron transport chain of Thiobacillus ferrooxidans grown on iron or thiosulfate
    • Cox, J. C., and D. H. Boxer. 1986. The role of rusticyanin, a blue copper protein, in the electron transport chain of Thiobacillus ferrooxidans grown on iron or thiosulfate. Biotechnol. Appl. Biochem. 8:269-275.
    • (1986) Biotechnol. Appl. Biochem. , vol.8 , pp. 269-275
    • Cox, J.C.1    Boxer, D.H.2
  • 9
    • 0031059057 scopus 로고    scopus 로고
    • Polythionate degradation by tetrathionate hydrolase of Thiobacillus ferrooxidans
    • De Jong, G. A. H., W. Hazeu, P. Bos, and G. Kuenen. 1997. Polythionate degradation by tetrathionate hydrolase of Thiobacillus ferrooxidans. Microbiology 143:499-504.
    • (1997) Microbiology , vol.143 , pp. 499-504
    • De Jong, G.A.H.1    Hazeu, W.2    Bos, P.3    Kuenen, G.4
  • 10
    • 0021328935 scopus 로고
    • Specific indication of hemoproteins in polyacrylamide gels using a double-staining process
    • Francis, R. T., and R. R. Becker. 1984. Specific indication of hemoproteins in polyacrylamide gels using a double-staining process. Anal. Biochem. 136:509-514.
    • (1984) Anal. Biochem. , vol.136 , pp. 509-514
    • Francis, R.T.1    Becker, R.R.2
  • 11
    • 0032466668 scopus 로고    scopus 로고
    • Physiology and genetics of sulfur-oxidizing bacteria
    • Friedrich, C. G. 1998. Physiology and genetics of sulfur-oxidizing bacteria. Adv. Microb. Physiol. 39:235-289.
    • (1998) Adv. Microb. Physiol. , vol.39 , pp. 235-289
    • Friedrich, C.G.1
  • 13
    • 0031866420 scopus 로고    scopus 로고
    • Importance of extracellular polymeric substances from Thiobacillus ferrooxidans for bioleaching
    • Gehrke, T., J. Telegdi, D. Thierry, and W. Sand. 1998. Importance of extracellular polymeric substances from Thiobacillus ferrooxidans for bioleaching. Appl. Environ. Microbiol. 64:2743-2747.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2743-2747
    • Gehrke, T.1    Telegdi, J.2    Thierry, D.3    Sand, W.4
  • 14
    • 0034045260 scopus 로고    scopus 로고
    • Molecular cloning, sequencing, and expression of omp-40, the gene coding for the major outer membrane protein from the acidophilic bacterium Thiobacillus ferrooxidans
    • Guiliani, N., and C. A. Jerez. 2000. Molecular cloning, sequencing, and expression of omp-40, the gene coding for the major outer membrane protein from the acidophilic bacterium Thiobacillus ferrooxidans. Appl. Environ. Microbiol. 66:2318-2324.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2318-2324
    • Guiliani, N.1    Jerez, C.A.2
  • 15
    • 0030790617 scopus 로고    scopus 로고
    • Alanyl-tRNA synthetase gene of the extreme acidophilic chemolithoautotrophic Thiobacillus ferrooxidans is highly homologous to alas genes from all living kingdoms but cannot be transcribed from its promoter in Escherichia coli
    • Guiliani, N., A. Bengrine, F. Borne, M. Chippaux, and V. Bonnefoy. 1997. Alanyl-tRNA synthetase gene of the extreme acidophilic chemolithoautotrophic Thiobacillus ferrooxidans is highly homologous to alas genes from all living kingdoms but cannot be transcribed from its promoter in Escherichia coli. Microbiology 143:2179-2187.
    • (1997) Microbiology , vol.143 , pp. 2179-2187
    • Guiliani, N.1    Bengrine, A.2    Borne, F.3    Chippaux, M.4    Bonnefoy, V.5
  • 16
    • 0021227370 scopus 로고
    • The acidophilic thiobacilli and others acidophilic bacteria that share their habitat
    • Harrison, A. P., Jr. 1984. The acidophilic thiobacilli and others acidophilic bacteria that share their habitat. Annu. Rev. Microbiol. 38:265-292.
    • (1984) Annu. Rev. Microbiol. , vol.38 , pp. 265-292
    • Harrison Jr., A.P.1
  • 17
    • 0036298196 scopus 로고    scopus 로고
    • ATP binding and hydrolysis and autophosphorylation of CbbQ encoded by the gene located downstream of RubisCO genes
    • Hayashi, N. R., and Y. Igarashi. 2002. ATP binding and hydrolysis and autophosphorylation of CbbQ encoded by the gene located downstream of RubisCO genes. Biochem. Biophys. Res. Commun. 290:1434-1440.
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 1434-1440
    • Hayashi, N.R.1    Igarashi, Y.2
  • 18
    • 0031577711 scopus 로고    scopus 로고
    • The novel genes, cbbQ and cbbO, located downstream from the RubisCO genes of Pseudomonas hydrogenothermophila, affect the conformational states and activity of RubisCO
    • Hayashi, N. R., H. Arai, T. Kodama, and Y. Igarashi. 1997. The novel genes, cbbQ and cbbO, located downstream from the RubisCO genes of Pseudomonas hydrogenothermophila, affect the conformational states and activity of RubisCO. Biochem. Biophys. Res. Commun. 241:565-569.
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 565-569
    • Hayashi, N.R.1    Arai, H.2    Kodama, T.3    Igarashi, Y.4
  • 20
    • 2642709245 scopus 로고    scopus 로고
    • Regulation of the sulfate starvation response in Pseudomonas aeruginosa: Role of cysteine biosynthetic intermediates
    • Hummerjohann, J., E. Küttel, M. Quadroni, J. Ragaller, T. Leisinger, and M. A. Kertesz. 1998. Regulation of the sulfate starvation response in Pseudomonas aeruginosa: role of cysteine biosynthetic intermediates. Microbiology 144:1375-1386.
    • (1998) Microbiology , vol.144 , pp. 1375-1386
    • Hummerjohann, J.1    Küttel, E.2    Quadroni, M.3    Ragaller, J.4    Leisinger, T.5    Kertesz, M.A.6
  • 21
    • 0020372284 scopus 로고
    • Thiobacillus ferrooxidans. The bioenergetics of an acidophilic chemolitotroph
    • Ingledew, W. J. 1982. Thiobacillus ferrooxidans. The bioenergetics of an acidophilic chemolitotroph. Biochim. Biophys. Acta 683:89-117.
    • (1982) Biochim. Biophys. Acta , vol.683 , pp. 89-117
    • Ingledew, W.J.1
  • 22
    • 0031032795 scopus 로고    scopus 로고
    • Oxidative metabolism of inorganic sulfur compounds by bacteria
    • Kelly, D. P., J. K. Shergill, W.-P. Lu, and A. P. Wood. 1997. Oxidative metabolism of inorganic sulfur compounds by bacteria. Antonie Leewenhoek 71:95-107.
    • (1997) Antonie Leewenhoek , vol.71 , pp. 95-107
    • Kelly, D.P.1    Shergill, J.K.2    Lu, W.-P.3    Wood, A.P.4
  • 23
    • 0027399386 scopus 로고
    • Specific binding of Thiobacillus ferrooxidans RbcR to the intergenic sequence between the rbc operon and the rbcR gene
    • Kusano, T., and K. Sugawara. 1993. Specific binding of Thiobacillus ferrooxidans RbcR to the intergenic sequence between the rbc operon and the rbcR gene. J. Bacteriol. 175:1019-1025.
    • (1993) J. Bacteriol. , vol.175 , pp. 1019-1025
    • Kusano, T.1    Sugawara, K.2
  • 24
    • 0025720491 scopus 로고
    • Evidence for two sets of structural genes coding for ribulose bisphosphate carboxylase in Thiobacillus ferrooxidans
    • Kusano, T., T. Takeshima, C. Inoue, and K. Sugawara. 1991. Evidence for two sets of structural genes coding for ribulose bisphosphate carboxylase in Thiobacillus ferrooxidans. J. Bacteriol. 173:7313-7323.
    • (1991) J. Bacteriol. , vol.173 , pp. 7313-7323
    • Kusano, T.1    Takeshima, T.2    Inoue, C.3    Sugawara, K.4
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0019291535 scopus 로고
    • Ore leaching by bacteria
    • Lundgren, D. G. 1980. Ore leaching by bacteria. Annu. Rev. Microbiol. 34:263-283.
    • (1980) Annu. Rev. Microbiol. , vol.34 , pp. 263-283
    • Lundgren, D.G.1
  • 28
    • 0017696571 scopus 로고
    • High resolution two-dimensional electrophoresis of basic as well as acidic proteins
    • O'Farrel, P. Z., H. M. Goodman, and P. H. O'Farrel. 1977. High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell 12:1133-1142.
    • (1977) Cell , vol.12 , pp. 1133-1142
    • O'Farrel, P.Z.1    Goodman, H.M.2    O'Farrel, P.H.3
  • 29
    • 0036211118 scopus 로고    scopus 로고
    • An exported rhodanese-like protein is induced during growth of Acidithiobacillus ferrooxidans in metal sulfides and different sulfur compounds
    • Ramírez, P., H. Toledo, N. Guiliani, and C. A. Jerez. 2002. An exported rhodanese-like protein is induced during growth of Acidithiobacillus ferrooxidans in metal sulfides and different sulfur compounds. Appl. Environ. Microbiol. 68:1837-1845.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 1837-1845
    • Ramírez, P.1    Toledo, H.2    Guiliani, N.3    Jerez, C.A.4
  • 30
    • 0036405454 scopus 로고    scopus 로고
    • Heavy metal mining using microbes
    • Rawlings, D. E. 2002. Heavy metal mining using microbes. Annu. Rev. Microbiol. 56:65-91.
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 65-91
    • Rawlings, D.E.1
  • 31
    • 0037810930 scopus 로고    scopus 로고
    • The sulfane sulfur of persulfides is the actual substrate of the sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphilium spp.
    • Rohwerder, T., and W. Sand. 2003. The sulfane sulfur of persulfides is the actual substrate of the sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphilium spp. Microbiology 149:1699-1709.
    • (2003) Microbiology , vol.149 , pp. 1699-1709
    • Rohwerder, T.1    Sand, W.2
  • 32
    • 0035253889 scopus 로고    scopus 로고
    • (Bio)chemistry of bacterial leaching-direct vs. indirect bioleaching
    • Sand, W., T. Gehrke, P. G. Jozsa, and A. Schippers. 2001. (Bio)chemistry of bacterial leaching-direct vs. indirect bioleaching. Hydrometallurgy 59:159-175.
    • (2001) Hydrometallurgy , vol.59 , pp. 159-175
    • Sand, W.1    Gehrke, T.2    Jozsa, P.G.3    Schippers, A.4
  • 33
    • 0028864512 scopus 로고
    • Sulfur chemistry, biofilm, and the (in)direct attack mechanism - A critical evaluation of bacterial leaching
    • Sand, W., T. Gehrke, R. Hallmann, and A. Schippers. 1995. Sulfur chemistry, biofilm, and the (in)direct attack mechanism - a critical evaluation of bacterial leaching. Appl. Microbiol. Biotechnol. 43:961-966.
    • (1995) Appl. Microbiol. Biotechnol. , vol.43 , pp. 961-966
    • Sand, W.1    Gehrke, T.2    Hallmann, R.3    Schippers, A.4
  • 34
    • 0032906223 scopus 로고    scopus 로고
    • Bacterial leaching of metal sulfides proceeds by two indirect mechanisms via thiosulfate or via polysulfides and sulfur
    • Schippers, A., and W. Sand. 1999. Bacterial leaching of metal sulfides proceeds by two indirect mechanisms via thiosulfate or via polysulfides and sulfur. Appl. Environ. Microbiol. 65:319-321.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 319-321
    • Schippers, A.1    Sand, W.2
  • 35
    • 0031752797 scopus 로고    scopus 로고
    • Something from almost nothing: Carbon dioxide fixation in chemoautotrophs
    • Shively, J. M., G. van Keulen, and W. G. Meijer. 1998. Something from almost nothing: carbon dioxide fixation in chemoautotrophs. Annu. Rev. Microbiol. 52:191-230.
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 191-230
    • Shively, J.M.1    Van Keulen, G.2    Meijer, W.G.3
  • 36
    • 0014345097 scopus 로고
    • The thiosulfate-oxidizing enzyme of Ferrobacillus ferrooxidans (Thiobacillus ferrooxidons)
    • Silver, M., and D. G. Lundgren. 1968. The thiosulfate-oxidizing enzyme of Ferrobacillus ferrooxidans (Thiobacillus ferrooxidons). Can. J. Biochem. 46:1215-1220.
    • (1968) Can. J. Biochem. , vol.46 , pp. 1215-1220
    • Silver, M.1    Lundgren, D.G.2
  • 37
    • 0014284337 scopus 로고
    • Sulfur-oxidizing enzyme of Ferrobacillus ferrooxidans (Thiobacillus ferrooxidans)
    • Silver, M., and D. G. Lundgren. 1968. Sulfur-oxidizing enzyme of Ferrobacillus ferrooxidans (Thiobacillus ferrooxidans). Can. J. Biochem. 46:457-461.
    • (1968) Can. J. Biochem. , vol.46 , pp. 457-461
    • Silver, M.1    Lundgren, D.G.2
  • 38
    • 0023449864 scopus 로고
    • Purification and some properties of sulfur:ferric ion oxidoreductase from Thiobacillus ferrooxidans
    • Sugio, T., W. Mizunashi, K. Inagaki, and T. Tano. 1987. Purification and some properties of sulfur:ferric ion oxidoreductase from Thiobacillus ferrooxidans. J. Bacteriol. 169:4916-4922.
    • (1987) J. Bacteriol. , vol.169 , pp. 4916-4922
    • Sugio, T.1    Mizunashi, W.2    Inagaki, K.3    Tano, T.4
  • 39
    • 0032786758 scopus 로고    scopus 로고
    • Oxidation of inorganic sulfur compounds: Chemical and enzymatic reactions
    • Suzuki, I. 1999. Oxidation of inorganic sulfur compounds: chemical and enzymatic reactions. Can. J. Microbiol. 45:97-105.
    • (1999) Can. J. Microbiol. , vol.45 , pp. 97-105
    • Suzuki, I.1
  • 40
    • 0014628095 scopus 로고
    • The rhodanese enzyme of Ferrobacillus ferrooxidans (Thiobacillus ferrooxidans)
    • Tabita, R., M. Silver, and D. G. Lundgren. 1969. The rhodanese enzyme of Ferrobacillus ferrooxidans (Thiobacillus ferrooxidans). Can. J. Biochem. 47:1141-1145.
    • (1969) Can. J. Biochem. , vol.47 , pp. 1141-1145
    • Tabita, R.1    Silver, M.2    Lundgren, D.G.3
  • 41
    • 0001774950 scopus 로고
    • Biological fundamentals of mineral leaching processes
    • H. L. Ehrlich and C. L. Brierley (ed.). McGraw-Hill Book Co., New York, N.Y.
    • Tuovinen, O. 1990. Biological fundamentals of mineral leaching processes, p. 55-77. In H. L. Ehrlich and C. L. Brierley (ed.), Microbial mineral recovery. McGraw-Hill Book Co., New York, N.Y.
    • (1990) Microbial Mineral Recovery , pp. 55-77
    • Tuovinen, O.1
  • 42
    • 0026490048 scopus 로고
    • Identification and characterization of GroEL and DnaK homologues in Thiobacillus ferrooxidans
    • Varela, P., and C. A. Jerez. 1992. Identification and characterization of GroEL and DnaK homologues in Thiobacillus ferrooxidans. FEMS Microbiol. Lett. 98:149-154.
    • (1992) FEMS Microbiol. Lett. , vol.98 , pp. 149-154
    • Varela, P.1    Jerez, C.A.2
  • 43
    • 0141903932 scopus 로고    scopus 로고
    • Proteomic and genomic analysis of the phosphate starvation response of Acidithiobacillus ferrooxidans
    • Vera, M., N. Guiliani, and C. A. Jerez. 2003. Proteomic and genomic analysis of the phosphate starvation response of Acidithiobacillus ferrooxidans. Hydrometallurgy 71:125-132.
    • (2003) Hydrometallurgy , vol.71 , pp. 125-132
    • Vera, M.1    Guiliani, N.2    Jerez, C.A.3
  • 45
    • 17944400111 scopus 로고    scopus 로고
    • Rusticyanin gene expression of Acidithiobacillus ferrooxidans ATCC 33020 in sulfur- and in ferrous iron media
    • Yarzábal, A., K. Duquesne, and V. Bonnefoy. 2003. Rusticyanin gene expression of Acidithiobacillus ferrooxidans ATCC 33020 in sulfur- and in ferrous iron media. Hydrometallurgy 71:107-114.
    • (2003) Hydrometallurgy , vol.71 , pp. 107-114
    • Yarzábal, A.1    Duquesne, K.2    Bonnefoy, V.3


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