메뉴 건너뛰기




Volumn 142, Issue 5, 1996, Pages 1289-1296

Regulation of bacterial methane oxidation: Transcription of the soluble methane mono-oxygenase operon of Methylococcus capsulatus (Bath) is repressed by copper ions

Author keywords

Copper ions; Methanotrophs; Methylococcus capsulatus (Bath); mRNA; smmo genes

Indexed keywords

COPPER ION; METHANE; METHANOL; PRIMER DNA; UNSPECIFIC MONOOXYGENASE;

EID: 0029884241     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/13500872-142-5-1289     Document Type: Article
Times cited : (74)

References (42)
  • 1
    • 0022541528 scopus 로고
    • Bacterial oxidation of methane and methanol
    • Anthony, C. (1986). Bacterial oxidation of methane and methanol. Adv Microb Physiol 27, 113-210.
    • (1986) Adv Microb Physiol , vol.27 , pp. 113-210
    • Anthony, C.1
  • 3
    • 0025528777 scopus 로고
    • Optimization of trichloroethylene oxidation by methanotrophs and the use of a colorimetric assay to detect soluble methane monooxygenase activity
    • Brusseau, G. A., Tsien, H.-C., Hanson, R. S. & Wackett, L. P. (1990). Optimization of trichloroethylene oxidation by methanotrophs and the use of a colorimetric assay to detect soluble methane monooxygenase activity. Biodegradation 1, 19-29.
    • (1990) Biodegradation , vol.1 , pp. 19-29
    • Brusseau, G.A.1    Tsien, H.-C.2    Hanson, R.S.3    Wackett, L.P.4
  • 4
    • 0025976406 scopus 로고
    • Molecular analysis of the methane monooxygenase (MMO) gene cluster of Methylosinus trichosporium OB3b
    • Cardy, D. L. N., Laidler, V., Salmond, G. P. C. & Murrell, J. C. (1991a). Molecular analysis of the methane monooxygenase (MMO) gene cluster of Methylosinus trichosporium OB3b. Mol Microbiol 5, 335-342.
    • (1991) Mol Microbiol , vol.5 , pp. 335-342
    • Cardy, D.L.N.1    Laidler, V.2    Salmond, G.P.C.3    Murrell, J.C.4
  • 5
    • 0026044876 scopus 로고
    • The methane monooxygenase gene cluster of Methylosinus trichosporium: Cloning and sequencing of the mmoC gene
    • Cardy, D. L. N., Laidler, V., Salmond, G. P. C. & Murrell, J. C. (1991b). The methane monooxygenase gene cluster of Methylosinus trichosporium: cloning and sequencing of the mmoC gene. Arch Microbiol 156, 477-483.
    • (1991) Arch Microbiol , vol.156 , pp. 477-483
    • Cardy, D.L.N.1    Laidler, V.2    Salmond, G.P.C.3    Murrell, J.C.4
  • 6
    • 0002471698 scopus 로고
    • Biochemical and biophysical studies towards characterization of the membrane-associated methane monooxygenase
    • Edited by J. C. Murrell & D. P. Kelly. Andover: Intercept Press
    • 1 Compounds, pp. 93-107. Edited by J. C. Murrell & D. P. Kelly. Andover: Intercept Press.
    • (1993) 1 Compounds , pp. 93-107
    • Chan, S.I.1    Nguyen, H.-H.T.2    Shiemke, A.K.3    Lidstrom, M.E.4
  • 7
    • 0017847369 scopus 로고
    • Resolution of the methane monooxygenase of Methylococcus capsulatus (Bath) into three components
    • Colby, J. & Dalton, H. (1978). Resolution of the methane monooxygenase of Methylococcus capsulatus (Bath) into three components. Biochem J 171, 461-468.
    • (1978) Biochem J , vol.171 , pp. 461-468
    • Colby, J.1    Dalton, H.2
  • 8
    • 9344243460 scopus 로고
    • Characterization of the second prosthetic group of the flavoenzyme NADH-acceptor reductase (component C) of the methane monooxygenase from Methylococcus capsulatus (Bath)
    • Colby, J. & Dalton, H. (1979). Characterization of the second prosthetic group of the flavoenzyme NADH-acceptor reductase (component C) of the methane monooxygenase from Methylococcus capsulatus (Bath). Biochem J 157, 495-497.
    • (1979) Biochem J , vol.157 , pp. 495-497
    • Colby, J.1    Dalton, H.2
  • 9
    • 0017198961 scopus 로고
    • The acetylene reduction technique as an assay for the nitrogenase activity in the methane-oxidizing bacterium Methylococcus capsulatus strain Bath
    • Dalton, H. & Whittenbury, R. (1976). The acetylene reduction technique as an assay for the nitrogenase activity in the methane-oxidizing bacterium Methylococcus capsulatus strain Bath. Arch Microbiol 109, 147-151.
    • (1976) Arch Microbiol , vol.109 , pp. 147-151
    • Dalton, H.1    Whittenbury, R.2
  • 11
    • 0002936936 scopus 로고
    • Structure and mechanism of action of the hydroxylase of soluble methane monooxygenase
    • Edited by J. C. Murrell & D. P. Kelly. Andover: Intercept Press
    • 1 Compounds, pp. 65-80. Edited by J. C. Murrell & D. P. Kelly. Andover: Intercept Press.
    • (1993) 1 Compounds , pp. 65-80
    • Dalton, H.1    Wilkins, P.2    Jiang, Y.3
  • 12
    • 0023186377 scopus 로고
    • Alginate biosynthesis: A model system for gene regulation and function in Pseudomonas
    • Deretic, V., Gill, J. F. & Chakrabarty, A. M. (1987). Alginate biosynthesis: a model system for gene regulation and function in Pseudomonas. Biotechnology 5, 469-477.
    • (1987) Biotechnology , vol.5 , pp. 469-477
    • Deretic, V.1    Gill, J.F.2    Chakrabarty, A.M.3
  • 13
    • 0022558422 scopus 로고
    • The xylABC promoter from the Pseudomonas putida TOL plasmid is activated by nitrogen regulatory genes in Escherichia coli
    • Dixon, R. (1986). The xylABC promoter from the Pseudomonas putida TOL plasmid is activated by nitrogen regulatory genes in Escherichia coli. Mol Gen Genet 203, 129-136.
    • (1986) Mol Gen Genet , vol.203 , pp. 129-136
    • Dixon, R.1
  • 14
    • 0024970671 scopus 로고
    • Methane monooxygenase from Methylosinus trichosporium OB3b. Purification and properties of a three-component system with high specific activity from a type II methanotroph
    • Fox, B. G., Froland, W. A., Dege, J. E. & Lipscomb, J. D. (1989). Methane monooxygenase from Methylosinus trichosporium OB3b. Purification and properties of a three-component system with high specific activity from a type II methanotroph. J Biol Chem 264, 10023-10033.
    • (1989) J Biol Chem , vol.264 , pp. 10023-10033
    • Fox, B.G.1    Froland, W.A.2    Dege, J.E.3    Lipscomb, J.D.4
  • 15
    • 0025036376 scopus 로고
    • Methane monooxygenase from Methylosinus trichosporium OB3b
    • Fox, B. G., Froland, W. A., Jollie, D. R. & Lipscomb, J. D. (1990). Methane monooxygenase from Methylosinus trichosporium OB3b. Methods Enzymol 188, 191-202.
    • (1990) Methods Enzymol , vol.188 , pp. 191-202
    • Fox, B.G.1    Froland, W.A.2    Jollie, D.R.3    Lipscomb, J.D.4
  • 16
    • 0026088028 scopus 로고
    • Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b, identification of sites of component interaction
    • Fox, B. G., Lin, Y., Dege, J. E. & Lipscomb, J. D. (1991). Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b, identification of sites of component interaction. J Biol Chem 266, 540-550.
    • (1991) J Biol Chem , vol.266 , pp. 540-550
    • Fox, B.G.1    Lin, Y.2    Dege, J.E.3    Lipscomb, J.D.4
  • 17
    • 0022346556 scopus 로고
    • Protein B of the soluble methane monooxygenase from Methylococcus capsulatus (Bath): A novel regulatory protein of enzyme activity
    • Green, J. & Dalton, H. (1985). Protein B of the soluble methane monooxygenase from Methylococcus capsulatus (Bath): a novel regulatory protein of enzyme activity. J Biol Chem 260, 15795-15801.
    • (1985) J Biol Chem , vol.260 , pp. 15795-15801
    • Green, J.1    Dalton, H.2
  • 18
    • 0022377080 scopus 로고
    • Copper ions as inhibitors of protein C of soluble methane monooxygenase Methylococcus capsulatus (Bath)
    • Green, J., Prior, S. D. & Dalton, H. (1985). Copper ions as inhibitors of protein C of soluble methane monooxygenase Methylococcus capsulatus (Bath). Eur J Biochem 153, 137-144.
    • (1985) Eur J Biochem , vol.153 , pp. 137-144
    • Green, J.1    Prior, S.D.2    Dalton, H.3
  • 19
    • 0027450659 scopus 로고
    • Soluble methane monooxygenase production and trichlorethylene degradation by a type 1 methanotroph, Methylomonas methanica 68-1
    • Koh, S.-C., Bowman, J. P. & Sayler, G. S. (1993). Soluble methane monooxygenase production and trichlorethylene degradation by a type 1 methanotroph, Methylomonas methanica 68-1. Appl Environ Microbiol 59, 960-967.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 960-967
    • Koh, S.-C.1    Bowman, J.P.2    Sayler, G.S.3
  • 20
    • 0028090067 scopus 로고
    • Biochemistry of the soluble methane monooxygenase
    • Lipscomb, J. D. (1994). Biochemistry of the soluble methane monooxygenase. Annu Rev Microbiol 48, 371-399.
    • (1994) Annu Rev Microbiol , vol.48 , pp. 371-399
    • Lipscomb, J.D.1
  • 21
    • 0025766709 scopus 로고
    • Redox properties of the hydroxylase component of methane monooxygenase from Methylococcus capsulatus (Bath): Effects of protein B, reductase and substrate
    • Liu, K. E. & Lippard, S. J. (1991). Redox properties of the hydroxylase component of methane monooxygenase from Methylococcus capsulatus (Bath): effects of protein B, reductase and substrate. J Biol Chem 266, 12836-12839.
    • (1991) J Biol Chem , vol.266 , pp. 12836-12839
    • Liu, K.E.1    Lippard, S.J.2
  • 22
    • 0023258960 scopus 로고
    • Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor
    • de Lorenzo, V., Wee, S., Herrero, M. & Nielands, J. B. (1987). Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor. J Bacteriol 169, 2624-2630.
    • (1987) J Bacteriol , vol.169 , pp. 2624-2630
    • Lorenzo, V.1    Wee, S.2    Herrero, M.3    Nielands, J.B.4
  • 23
    • 0022033590 scopus 로고
    • 2 redox centres of component C, the NADH:acceptor reductase of the soluble methane monooxygenase of Methylococcus capsulatus (Bath)
    • 2 redox centres of component C, the NADH:acceptor reductase of the soluble methane monooxygenase of Methylococcus capsulatus (Bath). Eur J Biochem 147, 291-296.
    • (1985) Eur J Biochem , vol.147 , pp. 291-296
    • Lund, J.1    Dalton, H.2
  • 24
    • 0022039701 scopus 로고
    • Electron transfer reactions in the soluble methane monooxygenase of Methylococcus capsulatus (Bath)
    • Lund, J., Woodland, M. P. & Dalton, H. (1985). Electron transfer reactions in the soluble methane monooxygenase of Methylococcus capsulatus (Bath). Eur J Biochem 147, 297-305.
    • (1985) Eur J Biochem , vol.147 , pp. 297-305
    • Lund, J.1    Woodland, M.P.2    Dalton, H.3
  • 26
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory
    • Miller, J. (1972). Experiments in Molecular Genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.1
  • 27
    • 0026876403 scopus 로고
    • Genetics and molecular biology of methanotrophs
    • Murrell, J. C. (1992). Genetics and molecular biology of methanotrophs. FEMS Microbiol Rev 88, 233-248.
    • (1992) FEMS Microbiol Rev , vol.88 , pp. 233-248
    • Murrell, J.C.1
  • 28
    • 0028672043 scopus 로고
    • Molecular genetics of methane oxidation
    • Murrell, J. C. (1994). Molecular genetics of methane oxidation. Biodegradation 5, 145-159.
    • (1994) Biodegradation , vol.5 , pp. 145-159
    • Murrell, J.C.1
  • 29
    • 84950843334 scopus 로고
    • Purification and properties of a soluble methane monooxygenase from Methylocystis sp
    • Nakajima, T., Uchiyama, H., Yagi, O., Nakahara, T. (1992). Purification and properties of a soluble methane monooxygenase from Methylocystis sp. M. Biosci Biotech Biochem 56, 736-740.
    • (1992) M. Biosci Biotech Biochem , vol.56 , pp. 736-740
    • Nakajima, T.1    Uchiyama, H.2    Yagi, O.3    Nakahara, T.4
  • 30
    • 0028304991 scopus 로고
    • The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath)
    • Nguyen, H.-H. T., Shiemke, A. K., Jacobs, S. J., Hales, B. J., Lidstrom, M. E. & Chan, S. I. (1994). The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath). J Biol Chem 269, 14995-15005.
    • (1994) J Biol Chem , vol.269 , pp. 14995-15005
    • Nguyen, H.-H.T.1    Shiemke, A.K.2    Jacobs, S.J.3    Hales, B.J.4    Lidstrom, M.E.5    Chan, S.I.6
  • 31
    • 0026023610 scopus 로고
    • Purification and characterization of the soluble methane monooxygenase from Methylosinus sporium 5 demonstrates the highly conserved nature of this enzyme in mechanotrophs
    • Pilkington, S. J. & Dalton, H. (1991). Purification and characterization of the soluble methane monooxygenase from Methylosinus sporium 5 demonstrates the highly conserved nature of this enzyme in mechanotrophs. FEMS Microbiol Lett 78, 103-108.
    • (1991) FEMS Microbiol Lett , vol.78 , pp. 103-108
    • Pilkington, S.J.1    Dalton, H.2
  • 32
    • 0021911405 scopus 로고
    • The effect of copper ions on membrane content and methane monooxygenase activity in methanol-grown cells of Methylococcus capsulatus (Bath)
    • Prior, S. D. & Dalton, H. (1985). The effect of copper ions on membrane content and methane monooxygenase activity in methanol-grown cells of Methylococcus capsulatus (Bath). J Gen Microbiol 131, 155-163.
    • (1985) J Gen Microbiol , vol.131 , pp. 155-163
    • Prior, S.D.1    Dalton, H.2
  • 33
    • 0017681196 scopus 로고
    • DNA sequencing with chain terminating inhibitors
    • Sanger, F., Nicklen, S. & Coulsen, A. R. (1977). DNA sequencing with chain terminating inhibitors. Proc Natl Acad Sci USA 74, 5463-5467.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 5463-5467
    • Sanger, F.1    Nicklen, S.2    Coulsen, A.R.3
  • 34
    • 0019387176 scopus 로고
    • The effect of growth conditions on intracytoplasmic membranes and methane monooxygenase activities in Methylosinus trichosporium OB3b
    • Scott, D., Brannan, J. & Higgins, I. J. (1981a). The effect of growth conditions on intracytoplasmic membranes and methane monooxygenase activities in Methylosinus trichosporium OB3b. J Gen Microbiol 125, 63-72.
    • (1981) J Gen Microbiol , vol.125 , pp. 63-72
    • Scott, D.1    Brannan, J.2    Higgins, I.J.3
  • 35
    • 0040748173 scopus 로고
    • Intracytoplasmic membranes in oxygen-limited chemostat cultures of Methylosinus trichosporium OB3b: Biocatalystic implication of physiologically balanced growth
    • Scott, D., Best, D. J. & Higgins, I. J. (1981b). Intracytoplasmic membranes in oxygen-limited chemostat cultures of Methylosinus trichosporium OB3b: biocatalystic implication of physiologically balanced growth. Biotechnol Lett 3, 641-644.
    • (1981) Biotechnol Lett , vol.3 , pp. 641-644
    • Scott, D.1    Best, D.J.2    Higgins, I.J.3
  • 36
    • 0026549141 scopus 로고
    • Gene regulation of plasmid-and chromosome-determined inorganic ion transport in bacteria
    • Silver, S. & Walderhaug, M. (1992). Gene regulation of plasmid-and chromosome-determined inorganic ion transport in bacteria. Microbiol Rev 56, 195-228.
    • (1992) Microbiol Rev , vol.56 , pp. 195-228
    • Silver, S.1    Walderhaug, M.2
  • 37
    • 0024368089 scopus 로고
    • Molecular analysis of methane monooxygenase from Methylococcus capsulatus (Bath)
    • Stainthorpe, A. C., Murrell, J. C., Salmond, G. P. C., Dalton, H. & Lees, V. (1989). Molecular analysis of methane monooxygenase from Methylococcus capsulatus (Bath). Arch Microbiol 152, 154-159.
    • (1989) Arch Microbiol , vol.152 , pp. 154-159
    • Stainthorpe, A.C.1    Murrell, J.C.2    Salmond, G.P.C.3    Dalton, H.4    Lees, V.5
  • 38
    • 0025006802 scopus 로고
    • The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath)
    • Stainthorpe, A. C., Lees, V., Salmond, G. P. C., Dalton, H. & Murrell, J. C. (1990). The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath). Gene 91, 27-34.
    • (1990) Gene , vol.91 , pp. 27-34
    • Stainthorpe, A.C.1    Lees, V.2    Salmond, G.P.C.3    Dalton, H.4    Murrell, J.C.5
  • 39
    • 0020559210 scopus 로고
    • Copper stress underlies the fundamental change in intracellular location of methane monooxygenase in methane-oxidizing organisms: Studies in batch and continuous cultures
    • Stanley, S. H., Prior, S. D., Leak, D. J. & Dalton, H. (1983). Copper stress underlies the fundamental change in intracellular location of methane monooxygenase in methane-oxidizing organisms: studies in batch and continuous cultures. Biotechnol Lett 5, 487-492.
    • (1983) Biotechnol Lett , vol.5 , pp. 487-492
    • Stanley, S.H.1    Prior, S.D.2    Leak, D.J.3    Dalton, H.4
  • 40
    • 0018362819 scopus 로고
    • Properties of the methane monooxygenase from extracts of Methylosinus trichosporium OB3b and evidence for its similarity to the enzyme from Methylococcus capsulatus (Bath)
    • Stirling, D. I. & Dalton, H. (1979). Properties of the methane monooxygenase from extracts of Methylosinus trichosporium OB3b and evidence for its similarity to the enzyme from Methylococcus capsulatus (Bath). Eur J Biochem 96, 205-212.
    • (1979) Eur J Biochem , vol.96 , pp. 205-212
    • Stirling, D.I.1    Dalton, H.2
  • 41
    • 0024377330 scopus 로고
    • Biodegradation of trichlorethylene by Methylosinus trichosporium OB3b
    • Tsien, H.-C., Brusseau, G. A., Hanson, R. S. & Wacket L. P. (1989). Biodegradation of trichlorethylene by Methylosinus trichosporium OB3b. Appl Environ Microbiol 55, 3155-3161.
    • (1989) Appl Environ Microbiol , vol.55 , pp. 3155-3161
    • Tsien, H.-C.1    Brusseau, G.A.2    Hanson, R.S.3    Wacket, L.P.4
  • 42
    • 0021759122 scopus 로고
    • Purification and characterization of Component A of the methane monooxygenase from Methylococcus capsulatus (Bath)
    • Woodland, M. P. & Dalton, H. (1989). Purification and characterization of Component A of the methane monooxygenase from Methylococcus capsulatus (Bath). J Biol Chem 259, 53-59.
    • (1989) J Biol Chem , vol.259 , pp. 53-59
    • Woodland, M.P.1    Dalton, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.