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Volumn 36, Issue 1, 2000, Pages 114-122

Sequence and expression of a halobacterial β-galactosidase gene

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BETA GALACTOSIDASE;

EID: 0034128505     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2000.01832.x     Document Type: Article
Times cited : (79)

References (36)
  • 1
  • 2
    • 0031736121 scopus 로고    scopus 로고
    • Evidence for massive gene exchange between archaeal and bacterial hyperthermophiles
    • Aravind, L., Tatusov, R.L., Wolf, Y.I., Walker, D.R., and Koonin, E.V. (1998) Evidence for massive gene exchange between archaeal and bacterial hyperthermophiles. Trends Genet 14: 442-444.
    • (1998) Trends Genet , vol.14 , pp. 442-444
    • Aravind, L.1    Tatusov, R.L.2    Wolf, Y.I.3    Walker, D.R.4    Koonin, E.V.5
  • 3
    • 0026506592 scopus 로고
    • A rapid and simple chemiluminescent assay for Escherichia coli β-galactosidase
    • Beale, E.G., Deeb, E.A., Handley, R.S., Akhaven-Tafti, H., and Schaap, A.P. (1992) A rapid and simple chemiluminescent assay for Escherichia coli β-galactosidase. Biotechniques 12: 320-324.
    • (1992) Biotechniques , vol.12 , pp. 320-324
    • Beale, E.G.1    Deeb, E.A.2    Handley, R.S.3    Akhaven-Tafti, H.4    Schaap, A.P.5
  • 4
    • 0027276935 scopus 로고
    • Fibronectin type III modules in the receptor phosphatase CD45 and tapeworm antigens
    • Bork, P., and Doolittle, R.F. (1993) Fibronectin type III modules in the receptor phosphatase CD45 and tapeworm antigens. Protein Sci 2: 1185-1187.
    • (1993) Protein Sci , vol.2 , pp. 1185-1187
    • Bork, P.1    Doolittle, R.F.2
  • 6
    • 0024604672 scopus 로고
    • Central metabolism of the archaebacteria: An overview
    • Danson, M.J. (1989) Central metabolism of the archaebacteria: an overview. Can J Microbiol 35: 58-64.
    • (1989) Can J Microbiol , vol.35 , pp. 58-64
    • Danson, M.J.1
  • 8
    • 0027155201 scopus 로고
    • Analysis of gas vesicle gene expression in Haloferax mediterranei reveals that GvpA and GvpC are both gas vesicle structural proteins
    • Englert, C., and Pfeifer, F. (1993) Analysis of gas vesicle gene expression in Haloferax mediterranei reveals that GvpA and GvpC are both gas vesicle structural proteins. J Biol Chem 268: 9329-9336.
    • (1993) J Biol Chem , vol.268 , pp. 9329-9336
    • Englert, C.1    Pfeifer, F.2
  • 9
    • 0028913174 scopus 로고
    • Analysis of a novel gene and beta-galactosidase isozyme from a psychrotrophic Arthrobacter isolate
    • Gutshall, K.R., Trimbur, D.E., Kasmir, J.J., and Brenchley, J.E. (1995) Analysis of a novel gene and beta-galactosidase isozyme from a psychrotrophic Arthrobacter isolate. J Bacteriol 177: 1981-1988.
    • (1995) J Bacteriol , vol.177 , pp. 1981-1988
    • Gutshall, K.R.1    Trimbur, D.E.2    Kasmir, J.J.3    Brenchley, J.E.4
  • 10
    • 0030064025 scopus 로고    scopus 로고
    • The glucose effect and regulation of alpha-amylase synthesis in the hyperthermophilic archaeon Sulfolobus solfataricus
    • Haseltine, C., Rolfsmeier, M., and Blum, P. (1996) The glucose effect and regulation of alpha-amylase synthesis in the hyperthermophilic archaeon Sulfolobus solfataricus. J Bacteriol 178: 945-950.
    • (1996) J Bacteriol , vol.178 , pp. 945-950
    • Haseltine, C.1    Rolfsmeier, M.2    Blum, P.3
  • 11
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B., and Bairoch, A. (1993) New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 293: 781-788.
    • (1993) Biochem J , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 12
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat, B., and Bairoch, A. (1996) Updating the sequence-based classification of glycosyl hydrolases. Biochem J 316: 695-696.
    • (1996) Biochem J , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 13
    • 0029166485 scopus 로고
    • Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases
    • Henrissat, B., Callebaut, I., Fabrega, S., Lehn, P., Mornon, J.P., and Davies, G. (1995) Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc Natl Acad Sci USA 92: 7090-7094.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7090-7094
    • Henrissat, B.1    Callebaut, I.2    Fabrega, S.3    Lehn, P.4    Mornon, J.P.5    Davies, G.6
  • 14
    • 0025099311 scopus 로고
    • A plasmid vector with a selectable marker for halophilic archaebacteria
    • Holmes, M.L., and Dyall-Smith, M.L. (1990) A plasmid vector with a selectable marker for halophilic archaebacteria. J Bacteriol 172: 756-761.
    • (1990) J Bacteriol , vol.172 , pp. 756-761
    • Holmes, M.L.1    Dyall-Smith, M.L.2
  • 15
    • 0025962676 scopus 로고
    • Mutations in DNA gyrase result in novobiocin resistance in halophilic archaebacteria
    • Holmes, M.L., and Dyall-Smith, M.L. (1991) Mutations in DNA gyrase result in novobiocin resistance in halophilic archaebacteria. J Bacteriol 173: 642-648.
    • (1991) J Bacteriol , vol.173 , pp. 642-648
    • Holmes, M.L.1    Dyall-Smith, M.L.2
  • 16
    • 0025738011 scopus 로고
    • Construction and use of halobacterial shuttle vectors and further studies on Haloferax DNA gyrase
    • Holmes, M.L., Nuttall, S.D., and Dyall-Smith, M.L. (1991) Construction and use of halobacterial shuttle vectors and further studies on Haloferax DNA gyrase. J Bacteriol 173: 3807-3813.
    • (1991) J Bacteriol , vol.173 , pp. 3807-3813
    • Holmes, M.L.1    Nuttall, S.D.2    Dyall-Smith, M.L.3
  • 17
    • 0027968264 scopus 로고
    • Improved shuttle vectors for Haloferax volcanii including a dual-resistance plasmid
    • Holmes, M., Pfeifer, F., and Dyall-Smith, M.L. (1994) Improved shuttle vectors for Haloferax volcanii including a dual-resistance plasmid. Gene 146: 117-121.
    • (1994) Gene , vol.146 , pp. 117-121
    • Holmes, M.1    Pfeifer, F.2    Dyall-Smith, M.L.3
  • 18
    • 0031036727 scopus 로고    scopus 로고
    • Purification and analysis of an extremely halophilic β-galactosidase from Haloferax alicantei
    • Holmes, M.L., Scopes, R.K., Moritz, R.L., Simpson, R.J., Englert, C., Pfeifer, F., et al. (1997) Purification and analysis of an extremely halophilic β-galactosidase from Haloferax alicantei. Biochim Biophys Acta 1337: 276-286.
    • (1997) Biochim Biophys Acta , vol.1337 , pp. 276-286
    • Holmes, M.L.1    Scopes, R.K.2    Moritz, R.L.3    Simpson, R.J.4    Englert, C.5    Pfeifer, F.6
  • 19
    • 0029903278 scopus 로고    scopus 로고
    • Dihydrolipoamide dehydrogenase from the halophilic archaeon Haloferax volcanii: Homologous overexpression of the cloned gene
    • Jolley, K.A., Rapaport, E., Hough, D.W., Danson, M.J., Woods, W.G., and Dyall-Smith, M.L. (1996) Dihydrolipoamide dehydrogenase from the halophilic archaeon Haloferax volcanii: homologous overexpression of the cloned gene. J Bacteriol 178: 3044-3048.
    • (1996) J Bacteriol , vol.178 , pp. 3044-3048
    • Jolley, K.A.1    Rapaport, E.2    Hough, D.W.3    Danson, M.J.4    Woods, W.G.5    Dyall-Smith, M.L.6
  • 20
    • 0026519194 scopus 로고
    • Cloning, sequence analysis, and expression of the structural gene encoding glucose-fructose oxidoreductase from Zymomonas mobilis
    • Kanagasundaram, V., and Scopes, R.K. (1992) Cloning, sequence analysis, and expression of the structural gene encoding glucose-fructose oxidoreductase from Zymomonas mobilis. J Bacteriol 174: 1439-1447.
    • (1992) J Bacteriol , vol.174 , pp. 1439-1447
    • Kanagasundaram, V.1    Scopes, R.K.2
  • 21
    • 0029036154 scopus 로고
    • Archaea: Narrowing the gap between prokaryotes and eukaryotes
    • Keeling, P.J., and Doolittle, W.F. (1995) Archaea: narrowing the gap between prokaryotes and eukaryotes. Proc Natl Acad Sci USA 92: 5761-5764.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5761-5764
    • Keeling, P.J.1    Doolittle, W.F.2
  • 22
    • 0021678370 scopus 로고
    • A proposed pathway for sorbitol production in Zymomonas mobilis
    • Leigh, D., Scopes, R.K., and Rogers, P.L. (1984) A proposed pathway for sorbitol production in Zymomonas mobilis. Appl Microbiol Biotechnol 20: 413-415.
    • (1984) Appl Microbiol Biotechnol , vol.20 , pp. 413-415
    • Leigh, D.1    Scopes, R.K.2    Rogers, P.L.3
  • 23
    • 0027943212 scopus 로고
    • Tracing the spread of fibronectin type III domains in bacterial glycohydrolases
    • Little, E., Bork, P., and Doolittle, R.F. (1994) Tracing the spread of fibronectin type III domains in bacterial glycohydrolases. J Mol Evol 39: 631-643.
    • (1994) J Mol Evol , vol.39 , pp. 631-643
    • Little, E.1    Bork, P.2    Doolittle, R.F.3
  • 24
    • 0028033756 scopus 로고
    • Sorbitol promotes growth of Zymomonas mobilis in environments with high concentrations of sugar: Evidence for a physiological function of glucose-fructose oxidoreductase in osmoprotection
    • Loos, H., Kramer, R., Sahm, H., and Sprenger, G.A. (1994) Sorbitol promotes growth of Zymomonas mobilis in environments with high concentrations of sugar: evidence for a physiological function of glucose-fructose oxidoreductase in osmoprotection. J Bacteriol 176: 7688-7693.
    • (1994) J Bacteriol , vol.176 , pp. 7688-7693
    • Loos, H.1    Kramer, R.2    Sahm, H.3    Sprenger, G.A.4
  • 26
    • 0015893286 scopus 로고
    • + and Cl of a moderately halophilic bacterium
    • + and Cl of a moderately halophilic bacterium. Can J Microbiol 19: 1181-1186.
    • (1973) Can J Microbiol , vol.19 , pp. 1181-1186
    • Masui, M.1    Wada, S.2
  • 27
    • 0022003836 scopus 로고
    • Genetic transfer in Halobacterium volcanii
    • Mevarech, M., and Werczberger, R. (1985) Genetic transfer in Halobacterium volcanii. J Bacteriol 162: 461-462.
    • (1985) J Bacteriol , vol.162 , pp. 461-462
    • Mevarech, M.1    Werczberger, R.2
  • 28
    • 0028960638 scopus 로고
    • Complementation studies with the gas vesicle-encoding, p-vac region of Halobacterium salinarium pHH1 reveal a regulatory role for the, p-gvpDE genes
    • Offner, S., and Pfeifer, F. (1995) Complementation studies with the gas vesicle-encoding, p-vac region of Halobacterium salinarium pHH1 reveal a regulatory role for the, p-gvpDE genes. Mol Microbiol 16: 9-19.
    • (1995) Mol Microbiol , vol.16 , pp. 9-19
    • Offner, S.1    Pfeifer, F.2
  • 29
    • 0028908091 scopus 로고
    • In vivo definition of an archaeal promoter
    • Palmer, J.R., and Daniels, C.J. (1995) In vivo definition of an archaeal promoter. J Bacteriol 177: 1844-1849.
    • (1995) J Bacteriol , vol.177 , pp. 1844-1849
    • Palmer, J.R.1    Daniels, C.J.2
  • 30
    • 0034074062 scopus 로고    scopus 로고
    • The gene for a halophilic β-galactosidase (bgaH) of Haloferax alicantei as a reporter gene for promoter analyses in Halobacterium salinarum
    • Patenge, N., Haase, A., Bolhuis, H. and Oesterhelt, D. (2000) The gene for a halophilic β-galactosidase (bgaH) of Haloferax alicantei as a reporter gene for promoter analyses in Halobacterium salinarum. Mol Microbiol 36: 105-113.
    • (2000) Mol Microbiol , vol.36 , pp. 105-113
    • Patenge, N.1    Haase, A.2    Bolhuis, H.3    Oesterhelt, D.4
  • 31
    • 0024652141 scopus 로고
    • Characterization of the L11, L1, L10 and L12 equivalent ribosomal protein gene cluster of the halophilic archaebacterium Halobacterium cutirubrum
    • Shimmin, L.C., and Dennis, P.P. (1989) Characterization of the L11, L1, L10 and L12 equivalent ribosomal protein gene cluster of the halophilic archaebacterium Halobacterium cutirubrum. EMBO J 8: 1225-1235.
    • (1989) EMBO J , vol.8 , pp. 1225-1235
    • Shimmin, L.C.1    Dennis, P.P.2
  • 32
    • 0025836769 scopus 로고
    • Genetic fusions as experimental tools
    • Slauch, J.M., and Silhavy, T.J. (1991) Genetic fusions as experimental tools. Methods Enzymol 204: 213-248.
    • (1991) Methods Enzymol , vol.204 , pp. 213-248
    • Slauch, J.M.1    Silhavy, T.J.2
  • 33
    • 0028349908 scopus 로고
    • Compilation of halobacterial protein coding genes, the halobacterial codon usage table and its use
    • Soppa, J. (1994) Compilation of halobacterial protein coding genes, the halobacterial codon usage table and its use. Syst Appl Microbiol 16: 725-733.
    • (1994) Syst Appl Microbiol , vol.16 , pp. 725-733
    • Soppa, J.1
  • 34
    • 0003012234 scopus 로고
    • Classification of non-alkaliphilic halobacteria based on numerical taxonomy and polar lipid composition, and description of Haloarcula gen. nov. and Haloferax gen. nov.
    • Torreblanca, M., Rodriguez-Valera, F., Juez, G., Ventosa, A., Kamekura, M., and Kates, M. (1986) Classification of non-alkaliphilic halobacteria based on numerical taxonomy and polar lipid composition, and description of Haloarcula gen. nov. and Haloferax gen. nov. Syst Appl Microbiol 8: 89-99.
    • (1986) Syst Appl Microbiol , vol.8 , pp. 89-99
    • Torreblanca, M.1    Rodriguez-Valera, F.2    Juez, G.3    Ventosa, A.4    Kamekura, M.5    Kates, M.6
  • 35
    • 0021943518 scopus 로고
    • Improved M13 Phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, L., Vieira, J., and Messing, J. (1985) Improved M13 Phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33: 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, L.1    Vieira, J.2    Messing, J.3
  • 36
    • 0022497812 scopus 로고
    • Glucose-fructose oxidoreductase, a new enzyme isolated from Zymomonas mobilis that is responsible for sorbitol production
    • Zachariou, M., and Scopes, R.K. (1986) Glucose-fructose oxidoreductase, a new enzyme isolated from Zymomonas mobilis that is responsible for sorbitol production. J Bacteriol 167: 863-869.
    • (1986) J Bacteriol , vol.167 , pp. 863-869
    • Zachariou, M.1    Scopes, R.K.2


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