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Volumn 64, Issue 6, 1998, Pages 2013-2019

The gal genes for the leloir pathway of Lactobacillus casei 64H

Author keywords

[No Author keywords available]

Indexed keywords

DNA FRAGMENT; EPIMERASE; GALACTOKINASE; GALACTOSE 1 PHOSPHATE URIDYLYLTRANSFERASE; GENE PRODUCT; REPRESSOR PROTEIN; RNA; URIDINE DIPHOSPHATE GLUCOSE 4 EPIMERASE;

EID: 0031776947     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.64.6.2013-2019.1998     Document Type: Article
Times cited : (38)

References (53)
  • 1
    • 0031058131 scopus 로고    scopus 로고
    • The lac operon of Lactobacillus casei contains lacT, a gene coding for a protein of the BglG family of transcriptional antiterminators
    • Alpert, C.-A., and U. Siebers. 1997. The lac operon of Lactobacillus casei contains lacT, a gene coding for a protein of the BglG family of transcriptional antiterminators. J. Bacteriol. 179:1555-1562.
    • (1997) J. Bacteriol. , vol.179 , pp. 1555-1562
    • Alpert, C.-A.1    Siebers, U.2
  • 3
    • 0025778670 scopus 로고
    • Construction and properties of a family of pACYC184-derived cloning vectors compatible with pBR322 and its derivatives
    • Bartolome, B., Y. Jubete, E. Martinez, and F. de la Cruz. 1991. Construction and properties of a family of pACYC184-derived cloning vectors compatible with pBR322 and its derivatives. Gene 102:75-78.
    • (1991) Gene , vol.102 , pp. 75-78
    • Bartolome, B.1    Jubete, Y.2    Martinez, E.3    De La Cruz, F.4
  • 5
    • 0027948942 scopus 로고
    • Dependence of lactose metabolism upon mutarotase encoded in the gal operon in Escherichia coli
    • Bouffard, G., K. Rudd, and S. L. Adhya. 1994. Dependence of lactose metabolism upon mutarotase encoded in the gal operon in Escherichia coli. J. Mol. Biol. 244:269-278.
    • (1994) J. Mol. Biol. , vol.244 , pp. 269-278
    • Bouffard, G.1    Rudd, K.2    Adhya, S.L.3
  • 6
    • 0014674485 scopus 로고
    • A complementation analysis of the restriction and modification of DNA in Escherichia coli
    • Boyer, H. W., and D. Roulland-Dussoix. 1969. A complementation analysis of the restriction and modification of DNA in Escherichia coli. J. Mol. Biol. 41:459-472.
    • (1969) J. Mol. Biol. , vol.41 , pp. 459-472
    • Boyer, H.W.1    Roulland-Dussoix, D.2
  • 7
    • 0010523226 scopus 로고
    • Mechanismes regulateur dans la biosynthese des enzymes du metabolisme du galactose chez Escherichia coli K-12 II. Le determinisme genetique de la regulation
    • Buttin, G. 1963. Mechanismes regulateur dans la biosynthese des enzymes du metabolisme du galactose chez Escherichia coli K-12 II. Le determinisme genetique de la regulation. J. Mol. Biol. 7:183-205.
    • (1963) J. Mol. Biol. , vol.7 , pp. 183-205
    • Buttin, G.1
  • 8
    • 0024312842 scopus 로고
    • Molecular characterization of the plasmid-encoded lactose-PTS of Lactobacillus casei
    • Chassy, B. M., and C.-A. Alpert. 1989. Molecular characterization of the plasmid-encoded lactose-PTS of Lactobacillus casei. FEMS Microbiol. Rev. 63:157-166.
    • (1989) FEMS Microbiol. Rev. , vol.63 , pp. 157-166
    • Chassy, B.M.1    Alpert, C.-A.2
  • 9
    • 0018231809 scopus 로고
    • Evidence for plasmid-associated lactose metabolism in Lactobacillus casei subsp. casei
    • Chassy, B. M., E. M. Gibson, and A. Giuffrida. 1978. Evidence for plasmid-associated lactose metabolism in Lactobacillus casei subsp. casei. Curr. Microbiol. 1:141-144.
    • (1978) Curr. Microbiol. , vol.1 , pp. 141-144
    • Chassy, B.M.1    Gibson, E.M.2    Giuffrida, A.3
  • 11
    • 0020522266 scopus 로고
    • Regulation and characterization of the galactose-phosphoenolpyruvate-dependent phosphotransferase system in Lactobacillus casei
    • Chassy, B. M., and J. Thompson. 1983. Regulation and characterization of the galactose-phosphoenolpyruvate-dependent phosphotransferase system in Lactobacillus casei. J. Bacteriol. 154:1204-1214.
    • (1983) J. Bacteriol. , vol.154 , pp. 1204-1214
    • Chassy, B.M.1    Thompson, J.2
  • 12
    • 0020570242 scopus 로고
    • Regulation of lactose-phosphoenolypruvate-dependent phosphotransferase system and β-D-phosphogalactoside galactohydrolase activities in Lactobacillus casei
    • Chassy, B. M., and J. Thompson. 1983. Regulation of lactose-phosphoenolypruvate-dependent phosphotransferase system and β-D-phosphogalactoside galactohydrolase activities in Lactobacillus casei. J. Bacteriol. 154: 1195-1203.
    • (1983) J. Bacteriol. , vol.154 , pp. 1195-1203
    • Chassy, B.M.1    Thompson, J.2
  • 13
    • 0001765472 scopus 로고
    • An antigenic analysis of Lactobacillus acidophilus
    • Efthymiou, C., and P. A. Hansen. 1962. An antigenic analysis of Lactobacillus acidophilus. J. Infect. Dis. 110:258-267.
    • (1962) J. Infect. Dis. , vol.110 , pp. 258-267
    • Efthymiou, C.1    Hansen, P.A.2
  • 14
    • 0029920614 scopus 로고    scopus 로고
    • The Leloir pathway: A mechanistic imperative for three enzymes to change the stereochemical configuration of a single carbon in galactose
    • Frey, P. A. 1996. The Leloir pathway: a mechanistic imperative for three enzymes to change the stereochemical configuration of a single carbon in galactose. FASEB J. 10:461-470.
    • (1996) FASEB J. , vol.10 , pp. 461-470
    • Frey, P.A.1
  • 15
    • 0014335675 scopus 로고
    • Deoxyribonucleic acid base composition of the genus Lactobacillus
    • Gasser, F., and M. Mandel. 1968. Deoxyribonucleic acid base composition of the genus Lactobacillus. J. Bacteriol. 96:580-588.
    • (1968) J. Bacteriol. , vol.96 , pp. 580-588
    • Gasser, F.1    Mandel, M.2
  • 16
    • 0031105265 scopus 로고    scopus 로고
    • Establishing a model to study regulation of the lactose operon in Lactobacillus casei
    • Gosalbes, M. J., V. Monedero, C.-A. Alpert, and G. Pérez-Martinez. 1997. Establishing a model to study regulation of the lactose operon in Lactobacillus casei. FEMS Microbiol. Lett. 148:83-89.
    • (1997) FEMS Microbiol. Lett. , vol.148 , pp. 83-89
    • Gosalbes, M.J.1    Monedero, V.2    Alpert, C.-A.3    Pérez-Martinez, G.4
  • 17
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 18
    • 0017350368 scopus 로고
    • Transport of galactose, glucose and their analogues by Escherichia coli K12
    • Henderson, P. J. F., R. A. Giddens, and M. C. Jones-Mortimer. 1977. Transport of galactose, glucose and their analogues by Escherichia coli K12. Biochem. J. 162:309-320.
    • (1977) Biochem. J. , vol.162 , pp. 309-320
    • Henderson, P.J.F.1    Giddens, R.A.2    Jones-Mortimer, M.C.3
  • 19
    • 0023484188 scopus 로고
    • Unidirectional digestion with exonucleaseIII in DNA sequence analysis
    • Henikoff, S. 1987. Unidirectional digestion with exonucleaseIII in DNA sequence analysis. Methods Enzymol. 155:156-165.
    • (1987) Methods Enzymol. , vol.155 , pp. 156-165
    • Henikoff, S.1
  • 20
    • 0030884564 scopus 로고    scopus 로고
    • Substrate recognition domains as revealed by active hybrids between the D-arabinitol and ribitol transporters from Klebsiella pneumoniae
    • Heuel, H., S. Turgut, K. Schmid, and J. W. Lengeler. 1997. Substrate recognition domains as revealed by active hybrids between the D-arabinitol and ribitol transporters from Klebsiella pneumoniae. J. Bacteriol. 179:6014-6019.
    • (1997) J. Bacteriol. , vol.179 , pp. 6014-6019
    • Heuel, H.1    Turgut, S.2    Schmid, K.3    Lengeler, J.W.4
  • 21
    • 0006323949 scopus 로고
    • Uridyl-Transferase
    • H. U. Bergmeyer (ed.), Verlag Chemie, Weinheim, Germany
    • Isselbacher, K. J. 1974. Uridyl-Transferase, p. 830-833. In H. U. Bergmeyer (ed.), Methoden der enzymatischen Analyse, 3rd ed. Verlag Chemie, Weinheim, Germany.
    • (1974) Methoden der Enzymatischen Analyse, 3rd Ed. , pp. 830-833
    • Isselbacher, K.J.1
  • 22
    • 0001065712 scopus 로고
    • Galactose-1-phosphate uridyl transferase, its purification and application
    • Kuruhashi, K., and E. P. Anderson. 1958. Galactose-1-phosphate uridyl transferase, its purification and application. Biochim. Biophys. Acta 29:498-502.
    • (1958) Biochim. Biophys. Acta , vol.29 , pp. 498-502
    • Kuruhashi, K.1    Anderson, E.P.2
  • 23
    • 0015245156 scopus 로고
    • The regulation of the β-methylgalactoside transport system and of the galactose binding protein of Escherichia coli K12
    • Lengeler, J., K. O. Herman, H. J. Unsöld, and W. Boos. 1971. The regulation of the β-methylgalactoside transport system and of the galactose binding protein of Escherichia coli K12. Eur. J. Biochem. 19:457-470.
    • (1971) Eur. J. Biochem. , vol.19 , pp. 457-470
    • Lengeler, J.1    Herman, K.O.2    Unsöld, H.J.3    Boos, W.4
  • 24
    • 0018973399 scopus 로고
    • Characterization of mutants of Escherichia coli K12, selected by resistance to streptozotocin
    • Lengeler, J. W. 1980. Characterization of mutants of Escherichia coli K12, selected by resistance to streptozotocin. Mol. Gen. Genet. 79:49-54.
    • (1980) Mol. Gen. Genet. , vol.79 , pp. 49-54
    • Lengeler, J.W.1
  • 25
    • 0019408121 scopus 로고
    • The phosphoenolpyruvate dependent carbohydrate phosphotransferase system enzymes II as chemoreceptors in chemotaxis of Escherichia coli K12
    • Lengeler, J. W., A. M. Auburger, R. Mayer, and A. Pecher. 1981. The phosphoenolpyruvate dependent carbohydrate phosphotransferase system enzymes II as chemoreceptors in chemotaxis of Escherichia coli K12. Mol. Gen. Genet. 183:163-170.
    • (1981) Mol. Gen. Genet. , vol.183 , pp. 163-170
    • Lengeler, J.W.1    Auburger, A.M.2    Mayer, R.3    Pecher, A.4
  • 26
    • 50449147866 scopus 로고
    • Transduction of linked genetic characters of the host by bacteriophage P1
    • Lennox, E. S. 1955. Transduction of linked genetic characters of the host by bacteriophage P1. Virology 1:190-206.
    • (1955) Virology , vol.1 , pp. 190-206
    • Lennox, E.S.1
  • 27
    • 84955554260 scopus 로고
    • Lactose fermenting bacteria in faeces
    • MacConkey, A. 1905. Lactose fermenting bacteria in faeces. J. Hyg. 8:333-379.
    • (1905) J. Hyg. , vol.8 , pp. 333-379
    • MacConkey, A.1
  • 28
    • 0021739440 scopus 로고
    • Demonstration of two operator elements in gal: In vitro repressor binding studies
    • Majumdar, A., and S. Adhya. 1984. Demonstration of two operator elements in gal: in vitro repressor binding studies. Proc. Natl. Acad. Sci. USA 81: 6100-6104.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 6100-6104
    • Majumdar, A.1    Adhya, S.2
  • 29
    • 0026730625 scopus 로고
    • Protein sequence from downstream of Escherichia coli galK is homologous with galM from other organisms
    • Letter
    • Maskell, D. 1992. Protein sequence from downstream of Escherichia coli galK is homologous with galM from other organisms. Mol. Microbiol. 6:2211. (Letter.)
    • (1992) Mol. Microbiol. , vol.6 , pp. 2211
    • Maskell, D.1
  • 30
    • 0026699188 scopus 로고
    • The gal locus from Haemophilus influenzae: Cloning, sequencing and the use of gal mutants to study lipopolysaccharide
    • Maskell, D. J., M. J. Szabo, M. E. Deadman, and E. R. Moxon. 1992. The gal locus from Haemophilus influenzae: cloning, sequencing and the use of gal mutants to study lipopolysaccharide. Mol. Microbiol. 6:3051-3063.
    • (1992) Mol. Microbiol. , vol.6 , pp. 3051-3063
    • Maskell, D.J.1    Szabo, M.J.2    Deadman, M.E.3    Moxon, E.R.4
  • 31
    • 0028101111 scopus 로고
    • Determination and comparison of Lactobacillus delbrueckii ssp. lactis DSM7290 promoter sequences
    • Matern H. T., J. R. Klein, B. Henrich, and R. Plapp. 1994. Determination and comparison of Lactobacillus delbrueckii ssp. lactis DSM7290 promoter sequences. FEMS Microbiol. Lett. 122:121-128.
    • (1994) FEMS Microbiol. Lett. , vol.122 , pp. 121-128
    • Matern, H.T.1    Klein, J.R.2    Henrich, B.3    Plapp, R.4
  • 32
    • 0025910489 scopus 로고
    • Galactose utilization in Lactobacillus helveticus: Isolation and characterization of the galactokinase (galK) and galactose-1-phosphate uridyl transferase (galT) genes
    • Mollet B., and N. Pilloud. 1991. Galactose utilization in Lactobacillus helveticus: isolation and characterization of the galactokinase (galK) and galactose-1-phosphate uridyl transferase (galT) genes. J. Bacteriol. 173:4464-4473.
    • (1991) J. Bacteriol. , vol.173 , pp. 4464-4473
    • Mollet, B.1    Pilloud, N.2
  • 33
    • 0026805942 scopus 로고
    • Rapid isolation of genomic DNA from gram negative bacteria
    • Neumann, B., A. Pospiech, and H. U. Schairer. 1992. Rapid isolation of genomic DNA from gram negative bacteria. Trends Genet. 8:332-333.
    • (1992) Trends Genet. , vol.8 , pp. 332-333
    • Neumann, B.1    Pospiech, A.2    Schairer, H.U.3
  • 34
    • 0027169357 scopus 로고
    • Northern hybridization: Rapid and simple electrophoretic conditions
    • Pellé, R., and N. B. Murphy. 1993. Northern hybridization: rapid and simple electrophoretic conditions. Nucleic Acids Res. 21:2783-2785.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 2783-2785
    • Pellé, R.1    Murphy, N.B.2
  • 35
    • 0025341372 scopus 로고
    • Carbohydrate utilization in Streptococcus thermophilus: Characterization of the genes for aldose 1-epimerase (mutarotase) and UDP-glucose 4-epimerase
    • Poolman, B., T. J. Royer, S. E. Mainzer, and B. F. Schmidt. 1990. Carbohydrate utilization in Streptococcus thermophilus: characterization of the genes for aldose 1-epimerase (mutarotase) and UDP-glucose 4-epimerase. J. Bacteriol. 172:4037-4047.
    • (1990) J. Bacteriol. , vol.172 , pp. 4037-4047
    • Poolman, B.1    Royer, T.J.2    Mainzer, S.E.3    Schmidt, B.F.4
  • 36
    • 0027323057 scopus 로고
    • Energy transduction in lactic acid bacteria
    • Poolman, B. 1993. Energy transduction in lactic acid bacteria. FEMS Microbiol. Rev. 12:125-148.
    • (1993) FEMS Microbiol. Rev. , vol.12 , pp. 125-148
    • Poolman, B.1
  • 37
    • 0014413977 scopus 로고
    • Transport systems for galactose and galactosides in Escherichia coli. II. Substrate and inducer specificities
    • Rotman, B., A. K. Ganesan, and R. Guzman. 1968. Transport systems for galactose and galactosides in Escherichia coli. II. Substrate and inducer specificities. J. Mol. Biol. 36:247-260.
    • (1968) J. Mol. Biol. , vol.36 , pp. 247-260
    • Rotman, B.1    Ganesan, A.K.2    Guzman, R.3
  • 39
    • 0022372670 scopus 로고
    • Enzymatic amplification of β-globin genomic sequences and restriction sites of sickle cell anemia
    • Saiki R., S. Scharf, F. Faloona, K. B. Mullis, G. T. Horn, H. A. Ehrlich, and M. Arnheim. 1985. Enzymatic amplification of β-globin genomic sequences and restriction sites of sickle cell anemia. Science 230:1350-1354.
    • (1985) Science , vol.230 , pp. 1350-1354
    • Saiki, R.1    Scharf, S.2    Faloona, F.3    Mullis, K.B.4    Horn, G.T.5    Ehrlich, H.A.6    Arnheim, M.7
  • 42
    • 0014521181 scopus 로고
    • The galactose operon of E. coli K-12. II. a deletion analysis of operon structure and polarity
    • Shapiro, J. A., and S. L. Adhya. 1969. The galactose operon of E. coli K-12. II. A deletion analysis of operon structure and polarity. Genetics 62:249-264.
    • (1969) Genetics , vol.62 , pp. 249-264
    • Shapiro, J.A.1    Adhya, S.L.2
  • 43
    • 0345111804 scopus 로고
    • Rapid enzyme assay technique utilizing radioactive substrate, ion-exchange paper and scintillation counting
    • Sherman, J. R. 1963. Rapid enzyme assay technique utilizing radioactive substrate, ion-exchange paper and scintillation counting. Anal. Biochem. 5: 548.
    • (1963) Anal. Biochem. , vol.5 , pp. 548
    • Sherman, J.R.1
  • 45
    • 0023042283 scopus 로고
    • Use of the bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F. W., and B. A. Moffat. 1986. Use of the bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffat, B.A.2
  • 46
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system of controlled exclusive expression of specific genes
    • Tabor, S., and C. C. Richardson. 1985. A bacteriophage T7 RNA polymerase/promoter system of controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. USA 82:1074-1078.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 47
    • 0014055981 scopus 로고
    • Replacement of a phosphoenolpyruvate-dependent phosphotransferase by a nicotinamide adenine dinucleotide-linked dehydrogenase for the utilization of mannitol
    • Tanaka S., S. A. Lerner, and E. C. C. Lin. 1967. Replacement of a phosphoenolpyruvate-dependent phosphotransferase by a nicotinamide adenine dinucleotide-linked dehydrogenase for the utilization of mannitol. J. Bacteriol. 93:642-648.
    • (1967) J. Bacteriol. , vol.93 , pp. 642-648
    • Tanaka, S.1    Lerner, S.A.2    Lin, E.C.C.3
  • 48
    • 0000192671 scopus 로고
    • Primer extension. Unit 4.8
    • F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), John Wiley and Sons, Inc., New York, N.Y.
    • Triezenberg, S. J. 1990. Primer extension. Unit 4.8 In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology. John Wiley and Sons, Inc., New York, N.Y.
    • (1990) Current Protocols in Molecular Biology
    • Triezenberg, S.J.1
  • 49
    • 0023787609 scopus 로고
    • A procedure for in vitro amplification of DNA segments that lie outside the boundaries of known sequences
    • Triglia, T., M. G. Peterson, and D. J. Kemp. 1988. A procedure for in vitro amplification of DNA segments that lie outside the boundaries of known sequences. Nucleic Acids Res. 19:8186.
    • (1988) Nucleic Acids Res. , vol.19 , pp. 8186
    • Triglia, T.1    Peterson, M.G.2    Kemp, D.J.3
  • 50
    • 0025052301 scopus 로고
    • Molecular cloning, transcriptional analysis and nucleotide sequence of lacR, a gene encoding the represser of the lactose phosphotransferase system of Lactococcus lactis
    • van Rooijen, R. J., and W. M. de Vos. 1990. Molecular cloning, transcriptional analysis and nucleotide sequence of lacR, a gene encoding the represser of the lactose phosphotransferase system of Lactococcus lactis. J. Biol. Chem. 265:18499-18503.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18499-18503
    • Van Rooijen, R.J.1    De Vos, W.M.2
  • 51
    • 0026682712 scopus 로고
    • Isorepressor of the gal regulon in Escherichia coli
    • Weickert, M. J., and S. Adhya. 1992. Isorepressor of the gal regulon in Escherichia coli. J. Mol. Biol. 226:69-83.
    • (1992) J. Mol. Biol. , vol.226 , pp. 69-83
    • Weickert, M.J.1    Adhya, S.2
  • 52
    • 0001622993 scopus 로고
    • Galactokinase and uridine diphosphogalactose 4-epimerase from Escherichia coli
    • Wilson, D. B., and D. S. Hogness. 1966. Galactokinase and uridine diphosphogalactose 4-epimerase from Escherichia coli. Methods Enzymol. VIII: 229-240.
    • (1966) Methods Enzymol. , vol.8 , pp. 229-240
    • Wilson, D.B.1    Hogness, D.S.2
  • 53
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


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