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Volumn 248, Issue 1, 1997, Pages 72-79

Inactivation of the regulatory protein a of soluble methane monooxygenase from Methylococcus capsulatus (Bath) by proteolysis can be overcome by a Gly to Gln modification

Author keywords

Methane monooxygenase; N terminal processing; Post translational modification; Proteolytic cleavage; Site directed mutagenesis

Indexed keywords

HYBRID PROTEIN; PROTEINASE INHIBITOR; REGULATOR PROTEIN; UNSPECIFIC MONOOXYGENASE;

EID: 0030848173     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-1-00072.x     Document Type: Article
Times cited : (34)

References (36)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein using the principle of protein-binding dye
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein using the principle of protein-binding dye, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 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. (1991) 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
  • 3
    • 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
  • 4
    • 0002936936 scopus 로고
    • Structure and mechanism of action of the hydroxylase of soluble methane monooxygenase
    • (Murrell, J. C. & Kelly, D. P., eds) Andover, Intercept Press
    • 1 compounds (Murrell, J. C. & Kelly, D. P., eds) pp. 65-80, Andover, Intercept Press.
    • (1993) 1 Compounds , pp. 65-80
    • Dalton, H.1    Wilkins, P.2    Jiang, Y.3
  • 5
    • 0030904926 scopus 로고    scopus 로고
    • Radiolytic reduction of methane monooxygenase dinuclear iron cluster at 77 K
    • Davydov, A., Davydov, R., Graslund, A., Lipscomb, J. D. & Andersson, K. K. (1997) Radiolytic reduction of methane monooxygenase dinuclear iron cluster at 77 K, J. Biol. Chem. 272, 7022-7026.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7022-7026
    • Davydov, A.1    Davydov, R.2    Graslund, A.3    Lipscomb, J.D.4    Andersson, K.K.5
  • 7
    • 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
  • 8
    • 0026088028 scopus 로고
    • Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b
    • Fox, B. G., Liu, Y., Dege, J. E. & Lipscomb, J. D. (1991) Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b, J. Biol. Chem. 266, 540-550.
    • (1991) J. Biol. Chem. , vol.266 , pp. 540-550
    • Fox, B.G.1    Liu, Y.2    Dege, J.E.3    Lipscomb, J.D.4
  • 9
    • 0026630133 scopus 로고
    • Methane monooxygenase component B and reductase alter the regioselectivity of the hydroxylase component-catalysed reactions
    • Froland, W. A., Andersson, K. K., Lee, S.-K., Liu, Y. & Lipscomb, J. D. (1992) Methane monooxygenase component B and reductase alter the regioselectivity of the hydroxylase component-catalysed reactions, J. Biol. Chem. 267, 17588-17597.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17588-17597
    • Froland, W.A.1    Andersson, K.K.2    Lee, S.-K.3    Liu, Y.4    Lipscomb, J.D.5
  • 10
    • 0030569498 scopus 로고    scopus 로고
    • A computational investigation of the possible substrate binding sites in the hydroxylase of soluble methane monooxygenase
    • George, A. R., Wilkins, P. C. & Dalton, H. (1996) A computational investigation of the possible substrate binding sites in the hydroxylase of soluble methane monooxygenase, J. Mol. Catal. 2, 103-113.
    • (1996) J. Mol. Catal. , vol.2 , pp. 103-113
    • George, A.R.1    Wilkins, P.C.2    Dalton, H.3
  • 11
    • 0022346556 scopus 로고
    • Protein B of the soluble methane monoxygenase from Methylococcus capsulatus (Bath): A novel regulatory protein of enzyme activity
    • Green, J. & Dalton, H. (1985) Protein B of the soluble methane monoxygenase 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
  • 12
    • 0029858185 scopus 로고    scopus 로고
    • Direct electrochemsistry of the hydroxylase of soluble methane monooxygenase from Methylococcus capsulatus (Bath)
    • Kazlauskaite, H., Hill, A. O., Wilkins, P. C. & Dalton, H. (1996) Direct electrochemsistry of the hydroxylase of soluble methane monooxygenase from Methylococcus capsulatus (Bath). Eur. J. Biochem. 241, 552-556.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 552-556
    • Kazlauskaite, H.1    Hill, A.O.2    Wilkins, P.C.3    Dalton, H.4
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of the bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 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
  • 15
    • 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
  • 16
    • 0022033590 scopus 로고
    • 2 redox centers of component C, the NADH: Acceptor reductase of the soluble methane monooxygenase of Methylococcus capsulatus (Bath)
    • 2 redox centers 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
  • 17
    • 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
  • 19
    • 0030986084 scopus 로고    scopus 로고
    • The soluble methane monooxygenase gene cluster of the trichloroethylene degrading methanotroph Methylocystis sp. strain M
    • McDonald, I. R., Uchiyama, H., Kombe, S., Yagi, O. & Murrell, J. C. (1997) The soluble methane monooxygenase gene cluster of the trichloroethylene degrading methanotroph Methylocystis sp. strain M, Appl. Environ. Microbiol. 63, 1898-1904.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 1898-1904
    • McDonald, I.R.1    Uchiyama, H.2    Kombe, S.3    Yagi, O.4    Murrell, J.C.5
  • 20
    • 0018391876 scopus 로고
    • Genetic and physiological studies on the relationship between colicin B resistance and ferrienterochelin uptake in E. coli K12
    • McIntosh, M. A., Chenault, S. S. & Earhart, C. F. (1979) Genetic and physiological studies on the relationship between colicin B resistance and ferrienterochelin uptake in E. coli K12, J. Bact. 137, 653-657.
    • (1979) J. Bact. , vol.137 , pp. 653-657
    • McIntosh, M.A.1    Chenault, S.S.2    Earhart, C.F.3
  • 21
    • 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
  • 22
    • 84950843334 scopus 로고
    • Purification and properties of a soluble methane monooxygenase from Methylocystis sp. M
    • Nakajima, T., Uchiyama, H., Yagi, O. & Nakahara, Y. (1992) Purification and properties of a soluble methane monooxygenase from Methylocystis sp. M, Biosci. Biotech. Biochem. 56, 736-740.
    • (1992) Biosci. Biotech. Biochem. , vol.56 , pp. 736-740
    • Nakajima, T.1    Uchiyama, H.2    Yagi, O.3    Nakahara, Y.4
  • 23
    • 0028279274 scopus 로고
    • Purification of glutathione S-transferase fusion proteins as a non-degraded form by using a protease negative E. coli strain, AD202
    • Nakano, H., Yamazaki, T., Ikeda, M., Masai, H., Miyatake, S. & Saito, T. (1994) Purification of glutathione S-transferase fusion proteins as a non-degraded form by using a protease negative E. coli strain, AD202, Nucleic Acids Res. 22, 543-544.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 543-544
    • Nakano, H.1    Yamazaki, T.2    Ikeda, M.3    Masai, H.4    Miyatake, S.5    Saito, T.6
  • 24
    • 0029884241 scopus 로고    scopus 로고
    • Regulation of bacterial methane oxidation: Transcription of the soluble methane monooxygenase operon of Methylococcus capsulatus (Bath) is repressed by copper ions
    • Nielsen, A. K., Gerdes, K., Degn, H. & Murrell, J. C. (1996) Regulation of bacterial methane oxidation: transcription of the soluble methane monooxygenase operon of Methylococcus capsulatus (Bath) is repressed by copper ions. Microbiol. UK. 142, 1289-1296.
    • (1996) Microbiol. UK , vol.142 , pp. 1289-1296
    • Nielsen, A.K.1    Gerdes, K.2    Degn, H.3    Murrell, J.C.4
  • 25
    • 0028008778 scopus 로고
    • Oxidation-reduction potentials of the methane monooxygenase hydroxylase component from Methylosinus trichosporium OB3b
    • Paulsen, K. E., Liu, Y., Fox, B. G., Lipscomb, J. D., Munck, E. & Stankovich, M. T. (1994) Oxidation-reduction potentials of the methane monooxygenase hydroxylase component from Methylosinus trichosporium OB3b, Biochem. 33, 713-722.
    • (1994) Biochem. , vol.33 , pp. 713-722
    • Paulsen, K.E.1    Liu, Y.2    Fox, B.G.3    Lipscomb, J.D.4    Munck, E.5    Stankovich, M.T.6
  • 26
    • 0025109631 scopus 로고
    • Soluble methane monooxygenase from Methylococcus capsulatus (Bath)
    • Pilkington, S. J. & Dalton, H. (1990) Soluble methane monooxygenase from Methylococcus capsulatus (Bath), Methods Enzymol. 188, 181-190.
    • (1990) Methods Enzymol. , vol.188 , pp. 181-190
    • Pilkington, S.J.1    Dalton, H.2
  • 27
    • 0025011069 scopus 로고
    • Identification of the gene encoding the regulatory protein B of soluble methane monooxygenase
    • Pilkington, S. J., Salmond, G. P. C., Murrell, J. C. & Dalton, H. (1990) Identification of the gene encoding the regulatory protein B of soluble methane monooxygenase, FEMS Microbiol. Lett. 72, 345-348.
    • (1990) FEMS Microbiol. Lett. , vol.72 , pp. 345-348
    • Pilkington, S.J.1    Salmond, G.P.C.2    Murrell, J.C.3    Dalton, H.4
  • 28
    • 0027913094 scopus 로고
    • Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane
    • Rosenzweig, A. C., Frederick, C. A., Lippard, S. J. & Nordlund, P. (1993) Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane, Nature 366, 537-543.
    • (1993) Nature , vol.366 , pp. 537-543
    • Rosenzweig, A.C.1    Frederick, C.A.2    Lippard, S.J.3    Nordlund, P.4
  • 29
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase
    • Smith, D. B. & Johnson, K. S. (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase, Gene (Amst.) 67, 31-40.
    • (1988) Gene (Amst.) , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 30
    • 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
  • 31
    • 0025006802 scopus 로고
    • The methane monooxygenase gene cluster from Methylococcus capsulatus (Bath)
    • Stainthorpe, A. C. Lees, V., Salmond, G. P. C., Dalton, H. & Murrell, J. C. (1990) The methane monooxygenase gene cluster from Methylococcus capsulatus (Bath), Gene (Amst.) 91, 27-34.
    • (1990) Gene (Amst.) , vol.91 , pp. 27-34
    • Stainthorpe, A.C.1    Lees, V.2    Salmond, G.P.C.3    Dalton, H.4    Murrell, J.C.5
  • 32
    • 0020559210 scopus 로고
    • Copper stress underlies the fundamental change in intracellular location of methane monooxygenase in methane-oxidising 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-oxidising organisms: studies in batch and continuous cultures, Biotechnol. Letts 5, 487-492.
    • (1983) Biotechnol. Letts , vol.5 , pp. 487-492
    • Stanley, S.H.1    Prior, S.D.2    Leak, D.J.3    Dalton, H.4
  • 33
    • 0021184998 scopus 로고
    • Lon transcriptional regulation of genes necessary for capsular polysaccharide synthesis in E. coli K12
    • Trisler, P. & Gottesman, S. (1984) Lon transcriptional regulation of genes necessary for capsular polysaccharide synthesis in E. coli K12, J. Bacteriol. 160, 184-191.
    • (1984) J. Bacteriol. , vol.160 , pp. 184-191
    • Trisler, P.1    Gottesman, S.2
  • 34
    • 0026779760 scopus 로고
    • Functional expression in Escherichia coli of proteins B and C from soluble methane monooxygnease of Methylococcus capsulatus (Bath)
    • West, C. A., Salmond, G. P. C., Dalton, H. & Murrell, J. C. (1992) Functional expression in Escherichia coli of proteins B and C from soluble methane monooxygnease of Methylococcus capsulatus (Bath), J. Gen. Microbiol. 138, 1301-1307.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1301-1307
    • West, C.A.1    Salmond, G.P.C.2    Dalton, H.3    Murrell, J.C.4
  • 35
    • 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
  • 36
    • 0030067648 scopus 로고    scopus 로고
    • Membrane associated methane monooxygenase from Methylococcus capsulatus (Bath)
    • Zahn, J. A. & DiSpirito, A. A. (1996) Membrane associated methane monooxygenase from Methylococcus capsulatus (Bath), J. Bact. 178, 1018-1029.
    • (1996) J. Bact. , vol.178 , pp. 1018-1029
    • Zahn, J.A.1    DiSpirito, A.A.2


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