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Volumn 143, Issue 6, 1997, Pages 1827-1835

Organization of methylamine utilization genes (mau) in 'Methylobacillus flagellatum' KT and analysis of mau mutants

Author keywords

'Methylobacillus flagellatum'; Mau mutants; Methylamine dehydrogenase; Tryptophan tryptophylquinone

Indexed keywords

AMINE DEHYDROGENASE; BACTERIAL PROTEIN; METHYLAMINE;

EID: 0030791125     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-143-6-1827     Document Type: Article
Times cited : (12)

References (44)
  • 1
    • 1842313893 scopus 로고
    • Energy metabolism of aerobic, methylotrophic bacteria
    • Edited by H. W. Van Verseveld & J. A. Duine. Groningen: University of Groningen
    • 1 Compounds, pp. 195-202. Edited by H. W. Van Verseveld & J. A. Duine. Groningen: University of Groningen.
    • (1987) 1 Compounds , pp. 195-202
    • Anthony, C.1    Jones, C.W.2
  • 2
    • 0013540305 scopus 로고
    • The role of cytochromes and blue copper proteins in growth of an obligate methylotroph on methanol and methylamine
    • Auton, K. A. & Anthony, C. (1989). The role of cytochromes and blue copper proteins in growth of an obligate methylotroph on methanol and methylamine. J Gen Microbiol 135, 1923-1931.
    • (1989) J Gen Microbiol , vol.135 , pp. 1923-1931
    • Auton, K.A.1    Anthony, C.2
  • 3
    • 0020566137 scopus 로고
    • The oxidation of methylated amines by methylotrophic bacterium Methylophilus methylotrophus
    • Burton, S. M., Byrom, D., Carver, M., Jones, G. D. D. & Jones, C. W. (1983). The oxidation of methylated amines by methylotrophic bacterium Methylophilus methylotrophus. FEMS Microbiol Lett 17, 185-190.
    • (1983) FEMS Microbiol Lett , vol.17 , pp. 185-190
    • Burton, S.M.1    Byrom, D.2    Carver, M.3    Jones, G.D.D.4    Jones, C.W.5
  • 5
    • 0025087101 scopus 로고
    • Cloning and sequencing of the structural gene for the small subunit of methylamine dehydrogenase from Methylobacterium extorquens AM1: Evidence for two tryptophan residues involved in the active center
    • Chistoserdov, A. Y., Tsygankov, Y. D. & Lidstrom, M. E. (1990). Cloning and sequencing of the structural gene for the small subunit of methylamine dehydrogenase from Methylobacterium extorquens AM1: evidence for two tryptophan residues involved in the active center. Biochem Biophys Res Comm 172, 211-216.
    • (1990) Biochem Biophys Res Comm , vol.172 , pp. 211-216
    • Chistoserdov, A.Y.1    Tsygankov, Y.D.2    Lidstrom, M.E.3
  • 6
    • 0026720414 scopus 로고
    • The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans
    • Chistoserdov, A. Y., Boyd, J., Mathews, F. S. & Lidstrom, M. E. (1992). The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans. Biochem Biophys Res Commun 184, 1226-1234.
    • (1992) Biochem Biophys Res Commun , vol.184 , pp. 1226-1234
    • Chistoserdov, A.Y.1    Boyd, J.2    Mathews, F.S.3    Lidstrom, M.E.4
  • 7
    • 0028216615 scopus 로고
    • The genetic organization of the mau gene cluster in Methylobacterium extorquens AMI: Complete nucleotide sequence and generation and characteristics of mau mutants
    • Chistoserdov, A. Y., Chistoserdova, L. V., McIntire, W. S. & Lidstrom, M. E. (1994a). The genetic organization of the mau gene cluster in Methylobacterium extorquens AMI: complete nucleotide sequence and generation and characteristics of mau mutants. J Bacteriol 176, 4052-4065.
    • (1994) J Bacteriol , vol.176 , pp. 4052-4065
    • Chistoserdov, A.Y.1    Chistoserdova, L.V.2    McIntire, W.S.3    Lidstrom, M.E.4
  • 8
    • 0028222405 scopus 로고
    • Organization of the methylamine utilization (mau) gene's in Methylophilus methylotrophus W3A1-NS
    • Chistoserdov, A. Y., McIntire, W. S., Mathews, F. S. & Lidstrom, M. E. (1994b). Organization of the methylamine utilization (mau) gene's in Methylophilus methylotrophus W3A1-NS. J Bacteriol 176, 4073-4080.
    • (1994) J Bacteriol , vol.176 , pp. 4073-4080
    • Chistoserdov, A.Y.1    McIntire, W.S.2    Mathews, F.S.3    Lidstrom, M.E.4
  • 9
    • 0024829501 scopus 로고
    • Cupredoxins of obligate methylotroph
    • Dinarieva, T. & Netrusov, A. (1989). Cupredoxins of obligate methylotroph. FEBS Lett 259, 47-49.
    • (1989) FEBS Lett , vol.259 , pp. 47-49
    • Dinarieva, T.1    Netrusov, A.2
  • 10
    • 0022000283 scopus 로고
    • Plasmids related to the broad host range vector, pRK290, useful for gene cloning and for monitoring gene expression
    • Ditt, G., Schmidhauser, T., Yakobson, E., Lu, P., Liang, X. W., Finlay, D. R., Guiney, D. & Helinski, D. R. (1985). Plasmids related to the broad host range vector, pRK290, useful for gene cloning and for monitoring gene expression. Plasmid 13, 149-153.
    • (1985) Plasmid , vol.13 , pp. 149-153
    • Ditt, G.1    Schmidhauser, T.2    Yakobson, E.3    Lu, P.4    Liang, X.W.5    Finlay, D.R.6    Guiney, D.7    Helinski, D.R.8
  • 11
    • 0014231042 scopus 로고
    • Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine
    • Eady, R. R. & Large, P. J. (1968). Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine. Biochem J 106, 245-255.
    • (1968) Biochem J , vol.106 , pp. 245-255
    • Eady, R.R.1    Large, P.J.2
  • 12
    • 0021689823 scopus 로고
    • Molecular cloning of a malyl coenzyme A lyase gene from Pseudomonas sp. strain AM1, a facultative methylotroph
    • Fulton, G. L., Nunn, D. N. & Lidstrom, M. E. (1984). Molecular cloning of a malyl coenzyme A lyase gene from Pseudomonas sp. strain AM1, a facultative methylotroph. J Bacteriol 160, 718-723.
    • (1984) J Bacteriol , vol.160 , pp. 718-723
    • Fulton, G.L.1    Nunn, D.N.2    Lidstrom, M.E.3
  • 13
    • 0029154216 scopus 로고
    • Cloning, sequencing, and mutation of a gene for azurin in 'Methylobacillus flagellatum' KT
    • Gak, E. R., Chistoserdov, A. Y. & Lidstrom, M. E. (1995). Cloning, sequencing, and mutation of a gene for azurin in 'Methylobacillus flagellatum' KT. J Bacteriol 177, 4575-4578.
    • (1995) J Bacteriol , vol.177 , pp. 4575-4578
    • Gak, E.R.1    Chistoserdov, A.Y.2    Lidstrom, M.E.3
  • 15
    • 0020376712 scopus 로고
    • Properties and subunit structure of methylamine dehydrogenase from Thiobacillus A2 and Methylophilus methylotrophus
    • Haywood, G. W., Janschke, N. S., Large, P. J. & Wallis, J. M. (1982). Properties and subunit structure of methylamine dehydrogenase from Thiobacillus A2 and Methylophilus methylotrophus. FEMS Microbiol Lett 15, 79-82.
    • (1982) FEMS Microbiol Lett , vol.15 , pp. 79-82
    • Haywood, G.W.1    Janschke, N.S.2    Large, P.J.3    Wallis, J.M.4
  • 16
    • 0027439274 scopus 로고
    • Cloning and sequencing of the gene coding for the large subunit of methylamine dehydrogenase from Thiobacillus versutus
    • Huitema, F., Van Beeumen, J., Van Driessche, G., Duine, J. A. & Canters, G. W. (1993). Cloning and sequencing of the gene coding for the large subunit of methylamine dehydrogenase from Thiobacillus versutus. J Bacteriol 175, 6254-6259.
    • (1993) J Bacteriol , vol.175 , pp. 6254-6259
    • Huitema, F.1    Van Beeumen, J.2    Van Driessche, G.3    Duine, J.A.4    Canters, G.W.5
  • 17
    • 0022400803 scopus 로고
    • An inducible periplasmic blue copper protein from Paracoccus denitrificans: Purification, properties, and physiological role
    • Husain, M. & Davidson, V. L. (1985). An inducible periplasmic blue copper protein from Paracoccus denitrificans: purification, properties, and physiological role. J Biol Chem 260, 14626-14629.
    • (1985) J Biol Chem , vol.260 , pp. 14626-14629
    • Husain, M.1    Davidson, V.L.2
  • 18
    • 0023217278 scopus 로고
    • Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans
    • Husain, M. & Davidson, V. L. (1987). Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans. J Bacteriol 169, 1712-1717.
    • (1987) J Bacteriol , vol.169 , pp. 1712-1717
    • Husain, M.1    Davidson, V.L.2
  • 19
    • 0021957665 scopus 로고
    • Methylophaga marina gen. nov., sp. nov. and Methylophaga thalassica sp. nov., marine methylotrophs
    • Janvier, M., Frehel, C., Grimont, F. & Gasser, F. (1985). Methylophaga marina gen. nov., sp. nov. and Methylophaga thalassica sp. nov., marine methylotrophs. Int J Syst Bacteriol 35, 131-139.
    • (1985) Int J Syst Bacteriol , vol.35 , pp. 131-139
    • Janvier, M.1    Frehel, C.2    Grimont, F.3    Gasser, F.4
  • 20
    • 0021093469 scopus 로고
    • Characterization of methylamine dehydrogenase from bacterium W3A1: Interaction with reductant and amino-containmg compounds
    • Kenny, W. C. & McIntire, W. (1983). Characterization of methylamine dehydrogenase from bacterium W3A1: interaction with reductant and amino-containmg compounds. Biochemistry 22, 3858-3868.
    • (1983) Biochemistry , vol.22 , pp. 3858-3868
    • Kenny, W.C.1    McIntire, W.2
  • 21
    • 0025008199 scopus 로고
    • Methylamine dehydrogenase from 'Methylobacillus flagellatum'
    • Kiriukhin, M. Y., Chistoserdov, A. Y. & Tsygankov, Y. D. (1990). Methylamine dehydrogenase from 'Methylobacillus flagellatum'. Methods Enzymol 188, 247-256.
    • (1990) Methods Enzymol , vol.188 , pp. 247-256
    • Kiriukhin, M.Y.1    Chistoserdov, A.Y.2    Tsygankov, Y.D.3
  • 22
    • 0042830095 scopus 로고
    • Mutants of obligate methylotroph 'Methylobacillus flagellatum' KT defective in genes of the ribulose monophosphate cycle of formaldehyde fixation
    • Kletsova, L. V., Chibisova, E. S. & Tsygankov, Y. D. (1988). Mutants of obligate methylotroph 'Methylobacillus flagellatum' KT defective in genes of the ribulose monophosphate cycle of formaldehyde fixation. Arch Microbiol 149, 441-449.
    • (1988) Arch Microbiol , vol.149 , pp. 441-449
    • Kletsova, L.V.1    Chibisova, E.S.2    Tsygankov, Y.D.3
  • 23
    • 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
  • 24
    • 0021813671 scopus 로고
    • The role of copper proteins in the oxidation of methylamine by an obligate methylotroph
    • Lawton, S. A. & Anthony, C. (1985). The role of copper proteins in the oxidation of methylamine by an obligate methylotroph. Biochem J 228, 719-725.
    • (1985) Biochem J , vol.228 , pp. 719-725
    • Lawton, S.A.1    Anthony, C.2
  • 25
    • 0004110203 scopus 로고
    • Molecular biology and genetics of methylamine dehydrogenase
    • Edited by J. C. Murrell & D. P. Kelly. Andover: Intercept
    • 1 Compounds, pp. 381-400. Edited by J. C. Murrell & D. P. Kelly. Andover: Intercept.
    • (1993) 1 Compounds , pp. 381-400
    • Lidstrom, M.E.1    Chistoserdov, A.Y.2
  • 27
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxyribonucleic acid from microorganisms
    • Marmur, J. (1961). A procedure for the isolation of deoxyribonucleic acid from microorganisms. J Mol Biol 3, 208-218.
    • (1961) J Mol Biol , vol.3 , pp. 208-218
    • Marmur, J.1
  • 28
    • 0019179987 scopus 로고
    • Methylamine dehydrogenase of Methylomonas J and Pseudomonas AM1. Hybridization of light and heavy subunits and some properties of an isolated hybrid enzymes
    • Matsumoto, T., Shirai, S., Ishii, Y. & Tobari, J. (1980). Methylamine dehydrogenase of Methylomonas J and Pseudomonas AM1. Hybridization of light and heavy subunits and some properties of an isolated hybrid enzymes. J Biochem 88, 1097-1102.
    • (1980) J Biochem , vol.88 , pp. 1097-1102
    • Matsumoto, T.1    Shirai, S.2    Ishii, Y.3    Tobari, J.4
  • 29
    • 0025785660 scopus 로고
    • A new cofactor in a prokaryotic enzyme : Tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase
    • McIntire, W. S., Wemmer, D. E., Chistoserdov, A. Y. & Lidstrom, M. E. (1991). A new cofactor in a prokaryotic enzyme : tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase. Science 252, 817-824.
    • (1991) Science , vol.252 , pp. 817-824
    • McIntire, W.S.1    Wemmer, D.E.2    Chistoserdov, A.Y.3    Lidstrom, M.E.4
  • 30
    • 0018612053 scopus 로고
    • Dimethylamine dehydrogenase from Hyphomicrobium X: Purification and some properties of a new enzyme that oxidizes secondary amines
    • Meiberg, J. B. & Harder, W. (1979). Dimethylamine dehydrogenase from Hyphomicrobium X: purification and some properties of a new enzyme that oxidizes secondary amines. J Gen Microbiol 115, 49-58.
    • (1979) J Gen Microbiol , vol.115 , pp. 49-58
    • Meiberg, J.B.1    Harder, W.2
  • 31
    • 0021431375 scopus 로고
    • Hybridization of nucleic acids immobilized on a solid support
    • Meinkoth, J. & Wahl, G. (1984). Hybridization of nucleic acids immobilized on a solid support. Anal Biochem 138, 267-284.
    • (1984) Anal Biochem , vol.138 , pp. 267-284
    • Meinkoth, J.1    Wahl, G.2
  • 32
  • 33
    • 0027133569 scopus 로고
    • Mutants of Methylobacterium extorquens and Paracoccus denitrificans deficient in c-type cytochrome biogenesis synthesize the methylamine-dehydrogenase polypeptides but cannot assemble the tryptophan-tryptophanylquinone group
    • Page, M. D. & Ferguson, S. J. (1993). Mutants of Methylobacterium extorquens and Paracoccus denitrificans deficient in c-type cytochrome biogenesis synthesize the methylamine-dehydrogenase polypeptides but cannot assemble the tryptophan-tryptophanylquinone group. Eur J Biochem 218, 711-718.
    • (1993) Eur J Biochem , vol.218 , pp. 711-718
    • Page, M.D.1    Ferguson, S.J.2
  • 34
    • 0025967971 scopus 로고
    • Specific detection of quinoproteins by redox-cycling staining
    • Paz, M. A., Fluckiger, R., Boak, A., Kagan, H. M. & Gallop, P. M. (1991). Specific detection of quinoproteins by redox-cycling staining. J Biol Chem 266, 689-692.
    • (1991) J Biol Chem , vol.266 , pp. 689-692
    • Paz, M.A.1    Fluckiger, R.2    Boak, A.3    Kagan, H.M.4    Gallop, P.M.5
  • 35
    • 0019365279 scopus 로고
    • A general method for site-directed mutagenesis in prokaryotes
    • Ruvkun, G. B. & Ausubel, J. R. (1981). A general method for site-directed mutagenesis in prokaryotes. Nature 289, 85-88.
    • (1981) Nature , vol.289 , pp. 85-88
    • Ruvkun, G.B.1    Ausubel, J.R.2
  • 36
    • 0021027842 scopus 로고
    • A broad-host-range mobilization system for in vivo genetic engineering: Transposon mutagenesis in Gram-negative bctena
    • Simon, R., Priefer, U. & Puhler, A. (1983). A broad-host-range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram-negative bctena. Bio/Technology 1, 784-791.
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 37
    • 0002883405 scopus 로고
    • Blue copper proteins in electron transport in methylotrophic bacteria
    • Edited by R. L. Crawford & R. S. Hanson. Washington, DC: American Society for Microbiology
    • 1 Compounds, pp. 106-112. Edited by R. L. Crawford & R. S. Hanson. Washington, DC: American Society for Microbiology.
    • (1984) 1 Compounds , pp. 106-112
    • Tobari, J.1
  • 38
    • 0019891342 scopus 로고
    • Amicyanin : An electron acceptor of methylamine dehydrogenase
    • Tobari, J. & Harada, Y. (1981). Amicyanin : an electron acceptor of methylamine dehydrogenase. Biochem Biophys Res Commun 101, 502-508.
    • (1981) Biochem Biophys Res Commun , vol.101 , pp. 502-508
    • Tobari, J.1    Harada, Y.2
  • 39
    • 0026342987 scopus 로고
    • Cloning, sequencing and expression studies of the genes encoding amicyanin and the β-subunit of methylamine dehydrogenase from Thiobacillus versutus
    • Ubbink, M., van Kleef, M. A. G., Kleinjan, D.-J., Hoitink, C. W. G., Huitema, F., Beintema, J. J., Duine, J. A. & Canters, G. W. (1991). Cloning, sequencing and expression studies of the genes encoding amicyanin and the β-subunit of methylamine dehydrogenase from Thiobacillus versutus. Eur J Biochem 202, 1003-1012.
    • (1991) Eur J Biochem , vol.202 , pp. 1003-1012
    • Ubbink, M.1    Van Kleef, M.A.G.2    Kleinjan, D.-J.3    Hoitink, C.W.G.4    Huitema, F.5    Beintema, J.J.6    Duine, J.A.7    Canters, G.W.8
  • 42
    • 0025149403 scopus 로고
    • Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation
    • Van Spanning, R. J. M., Wansell, C. W., Reijnders, W. N. M., Oltmann, L. F. & Stouthamer, A. H. (1990). Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation. FEBS Lett 275, 217-220.
    • (1990) FEBS Lett , vol.275 , pp. 217-220
    • Van Spanning, R.J.M.1    Wansell, C.W.2    Reijnders, W.N.M.3    Oltmann, L.F.4    Stouthamer, A.H.5
  • 43
    • 0027996934 scopus 로고
    • Expression of the man genes involved in methylamine metabolism in Paracoccus denitrificans is under control of a LysR-type transcriptional activator
    • Van Spanning, R. J. M., van der Palen, C. J. N. M., Slotbook, D.-J., Reijnders, W. N. M., Stouthamer, A. H. & Duine, J. A. (1995). Expression of the man genes involved in methylamine metabolism in Paracoccus denitrificans is under control of a LysR-type transcriptional activator. Eur J Biochem 226, 201-210.
    • (1995) Eur J Biochem , vol.226 , pp. 201-210
    • Van Spanning, R.J.M.1    Van Der Palen, C.J.N.M.2    Slotbook, D.-J.3    Reijnders, W.N.M.4    Stouthamer, A.H.5    Duine, J.A.6
  • 44
    • 0019293885 scopus 로고
    • An absolute method for protein determination based on difference in absorbance at 235 and 280 nm
    • Whitaker, J. R. & Granum, P. E. (1980). An absolute method for protein determination based on difference in absorbance at 235 and 280 nm. Anal Biochem 109, 156-159.
    • (1980) Anal Biochem , vol.109 , pp. 156-159
    • Whitaker, J.R.1    Granum, P.E.2


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