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Volumn 178, Issue 7, 1996, Pages 2051-2059

glc Locus of Escherichia coli: Characterization of genes encoding the subunits of glycolate oxidase and the glc regulator protein

Author keywords

[No Author keywords available]

Indexed keywords

CHLORAMPHENICOL ACETYLTRANSFERASE; FLAVOPROTEIN; GLYCOLIC ACID; HYDROXY ACID OXIDASE A; IRON SULFUR PROTEIN; MALATE SYNTHASE; REGULATOR PROTEIN; RNA;

EID: 0029670395     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.7.2051-2059.1996     Document Type: Article
Times cited : (104)

References (39)
  • 1
    • 27844566896 scopus 로고
    • Identification of the rhaA, rhaD and rhaD gene products from Escherichia coli K12
    • Badía, J., L. Baldomà, J. Aguilar, and A. Boronat. 1989. Identification of the rhaA, rhaD and rhaD gene products from Escherichia coli K12. FEMS Microbiol Lett. 65:253-258.
    • (1989) FEMS Microbiol Lett. , vol.65 , pp. 253-258
    • Badía, J.1    Baldomà, L.2    Aguilar, J.3    Boronat, A.4
  • 2
    • 0021978242 scopus 로고
    • Differential expression of photosynthesis genes in R. capsulata results from segmental differences in stability within the polycistronic rxc4 transcript
    • Belasco, J. G., T. Beatty, C. W. Adams, A. von Gabain, and S. N. Cohen. 1985. Differential expression of photosynthesis genes in R. capsulata results from segmental differences in stability within the polycistronic rxc4 transcript Cell 40:171-181
    • (1985) Cell , vol.40 , pp. 171-181
    • Belasco, J.G.1    Beatty, T.2    Adams, C.W.3    Von Gabain, A.4    Cohen, S.N.5
  • 3
    • 0018566823 scopus 로고
    • Rhamnose-induced propanediol oxidoreductase in Escherichia coli: Purification, properties, and comparison with the fucose-induced enzyme
    • Boronat, A., and J. Aguilar. 1979 Rhamnose-induced propanediol oxidoreductase in Escherichia coli: purification, properties, and comparison with the fucose-induced enzyme. J Bacteriol. 140:320-326.
    • (1979) J Bacteriol. , vol.140 , pp. 320-326
    • Boronat, A.1    Aguilar, J.2
  • 4
    • 0019720790 scopus 로고
    • Metabolism of of L-fucose and L-rhamnose tn Escherichia coli: Differences in induction of propanediol oxidoreductase
    • Boronat, A., and J. Aguilar. 1981. Metabolism of of L-fucose and L-rhamnose tn Escherichia coli: differences in induction of propanediol oxidoreductase. J. Bacteriol. 147:181-185.
    • (1981) J. Bacteriol. , vol.147 , pp. 181-185
    • Boronat, A.1    Aguilar, J.2
  • 6
    • 0017129243 scopus 로고
    • Transposition and fusion of the Iac genes to selected promoters m Escherichia coli using bacteriophage lambda and Mu
    • Casadaban, M. J. 1976. Transposition and fusion of the Iac genes to selected promoters m Escherichia coli using bacteriophage lambda and Mu J. Mol. Biol. 104:541-555.
    • (1976) J. Mol. Biol. , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 7
    • 0027417393 scopus 로고
    • Molecular cloning, DNA sequencing, and biochemical analyses of Escherichia coli glyoxylate carboligase
    • Chang, Y. Y., A. Y. Wang, and J. E. Cronan, Jr. 1993. Molecular cloning, DNA sequencing, and biochemical analyses of Escherichia coli glyoxylate carboligase. J. Biol. Chem. 268:3911-3919.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3911-3919
    • Chang, Y.Y.1    Wang, A.Y.2    Cronan Jr., J.E.3
  • 8
    • 0020032929 scopus 로고
    • Nucleotide sequence coding for the flavoprotein subunit of the fumarate reductase of Escherichia coli
    • Cole, S. T. 1982. Nucleotide sequence coding for the flavoprotein subunit of the fumarate reductase of Escherichia coli. Eur J. Biochem 122:479-484.
    • (1982) Eur J. Biochem , vol.122 , pp. 479-484
    • Cole, S.T.1
  • 9
    • 0024025050 scopus 로고
    • Nucleotide sequence and gene-polypeptide relationship of the glpABC operon encoding the anaerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli K.-12
    • Cole, S. T., K. Eiglmeir, S. Ahmed, N. Honore, L. Elmes, W. F. Anderson, and J. H. Weiner. 1988. Nucleotide sequence and gene-polypeptide relationship of the glpABC operon encoding the anaerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli K.-12. J. Bacteriol 170:2448-2456.
    • (1988) J. Bacteriol , vol.170 , pp. 2448-2456
    • Cole, S.T.1    Eiglmeir, K.2    Ahmed, S.3    Honore, N.4    Elmes, L.5    Anderson, W.F.6    Weiner, J.H.7
  • 10
    • 0020436637 scopus 로고
    • Location and nucleotide sequence of frdB, the gene encoding for the iron-sulphur protein subunit of the fumarate reductase of Escherichia coli
    • Cole, S. T., T. Grundtrom, B. Jaurin, J. J. Robinson, and J. H. Weiner. 1982. Location and nucleotide sequence of frdB, the gene encoding for the iron-sulphur protein subunit of the fumarate reductase of Escherichia coli. Eur J Biochem 126:211-216.
    • (1982) Eur J Biochem , vol.126 , pp. 211-216
    • Cole, S.T.1    Grundtrom, T.2    Jaurin, B.3    Robinson, J.J.4    Weiner, J.H.5
  • 11
    • 0029083167 scopus 로고
    • Biochemical and molecular characterization of the oxidative branch of glycerol utilization by Citrobacter freundii
    • Daniel, R., K. Stuertz, and G. Gottschalk. 1995. Biochemical and molecular characterization of the oxidative branch of glycerol utilization by Citrobacter freundii. J. Bacteriol. 177:4392-4401.
    • (1995) J. Bacteriol. , vol.177 , pp. 4392-4401
    • Daniel, R.1    Stuertz, K.2    Gottschalk, G.3
  • 12
    • 0021764402 scopus 로고
    • Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase of Escherichia coli
    • Darlison, M. G., and J. R. Guest. 1984. Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase of Escherichia coli Biochem. J. 223:507-517.
    • (1984) Biochem. J. , vol.223 , pp. 507-517
    • Darlison, M.G.1    Guest, J.R.2
  • 13
    • 0027358810 scopus 로고
    • Three overlapping lct genes involved in L-lactate utilization by Escherichia coli
    • Dong, J. M., J. S. Taylor, D. J. Latour, S. Iuchi, and E. C. C. Lin. 1993. Three overlapping lct genes involved in L-lactate utilization by Escherichia coli J. Bacteriol. 175:6671-6678.
    • (1993) J. Bacteriol. , vol.175 , pp. 6671-6678
    • Dong, J.M.1    Taylor, J.S.2    Latour, D.J.3    Iuchi, S.4    Lin, E.C.C.5
  • 14
    • 0026572721 scopus 로고
    • An improved chloramphenicol resistance gene cassette for site-directed marker replacement mutagenesis
    • Fuqua, W. C. 1992. An improved chloramphenicol resistance gene cassette for site-directed marker replacement mutagenesis BioTechniques 12:223-225.
    • (1992) BioTechniques , vol.12 , pp. 223-225
    • Fuqua, W.C.1
  • 15
    • 0001301980 scopus 로고
    • Glycolate metabolism in Escherichia coli
    • Hansen, R. W., and J. A. Hayashi. 1962. Glycolate metabolism in Escherichia coli. J. Bacteriol. 83:679-687.
    • (1962) J. Bacteriol. , vol.83 , pp. 679-687
    • Hansen, R.W.1    Hayashi, J.A.2
  • 16
    • 0027433865 scopus 로고
    • A mutation causing constitutive synthesis of the pyruvate dehydrogenase complex in Escherichia coli is located within the pdhR gene
    • Haydon, D. J., M. A. Quail, and J. R. Guest. 1993. A mutation causing constitutive synthesis of the pyruvate dehydrogenase complex in Escherichia coli is located within the pdhR gene. FEBS Lett. 336:43-47.
    • (1993) FEBS Lett. , vol.336 , pp. 43-47
    • Haydon, D.J.1    Quail, M.A.2    Guest, J.R.3
  • 17
    • 0019862344 scopus 로고
    • A rapid boiling method for the preparation of bacterial plasmids
    • Holmes, D. S., and M. Quigley. 1981. A rapid boiling method for the preparation of bacterial plasmids. Anal. Biochem. 114:193-197.
    • (1981) Anal. Biochem. , vol.114 , pp. 193-197
    • Holmes, D.S.1    Quigley, M.2
  • 18
    • 0001366577 scopus 로고
    • 2 compounds in microorganisms. 8. A dicarboxylic acid cycle as a route for the oxidation of glycollate by Escherichia coli
    • 2 compounds in microorganisms. 8. A dicarboxylic acid cycle as a route for the oxidation of glycollate by Escherichia coli. Biochem. J. 81:503-513.
    • (1961) Biochem. J. , vol.81 , pp. 503-513
    • Kornberg, H.L.1    Sadler, J.R.2
  • 19
    • 0027210771 scopus 로고
    • Isolation of the DLD gene of Saccharomyces cerevisiae encoding the mitochondrial enzyme D-lactate ferricytochrome c oxidoreductase
    • Lodi, T., and I. Ferrero. 1993. Isolation of the DLD gene of Saccharomyces cerevisiae encoding the mitochondrial enzyme D-lactate ferricytochrome c oxidoreductase. Mol. Gen. Genet. 238:315-324.
    • (1993) Mol. Gen. Genet. , vol.238 , pp. 315-324
    • Lodi, T.1    Ferrero, I.2
  • 20
    • 0027942216 scopus 로고
    • Carbon catabolite repression in Kluyveromyces lactis: Isolation and characterization of the KIDLD gene encoding the mitochondrial enzyme D-lactate ferricytochrome c oxidoreductase
    • Lodi, T., D. O'Connor, P. Goffrini, and I. Ferrero. 1994. Carbon catabolite repression in Kluyveromyces lactis: isolation and characterization of the KIDLD gene encoding the mitochondrial enzyme D-lactate ferricytochrome c oxidoreductase Mol. Gen. Genet. 244:622-629.
    • (1994) Mol. Gen. Genet. , vol.244 , pp. 622-629
    • Lodi, T.1    O'Connor, D.2    Goffrini, P.3    Ferrero, I.4
  • 21
    • 0015523117 scopus 로고
    • Glycolate oxidoreductase in Escherichia coli
    • Lord, J. M. 1972. Glycolate oxidoreductase in Escherichia coli. Biochim. Biophys. Acta 267:227-237.
    • (1972) Biochim. Biophys. Acta , vol.267 , pp. 227-237
    • Lord, J.M.1
  • 23
    • 0020755762 scopus 로고
    • Structure of the extracellular ferredoxin from Rhodospirillum rubrum. close similarity to clostridial ferredoxins
    • Matsubara, H., K. Inove, T. Hase, H. Hiura, T. Kakuno, and J. Yamashita. 1983. Structure of the extracellular ferredoxin from Rhodospirillum rubrum. close similarity to clostridial ferredoxins. J. Biochem. 93:1385-1390
    • (1983) J. Biochem. , vol.93 , pp. 1385-1390
    • Matsubara, H.1    Inove, K.2    Hase, T.3    Hiura, H.4    Kakuno, T.5    Yamashita, J.6
  • 24
    • 0003842951 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N Y.
    • Miller, J. H. 1992. A short course in bacterial genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N Y.
    • (1992) A Short Course in Bacterial Genetics
    • Miller, J.H.1
  • 25
    • 0027991986 scopus 로고
    • Molecular characterization of Escherichia coli malate synthase G. Differentiation with the malate synthase A isoenzyme
    • Molina, I., M. T. Pellicer, J. Badiá, J. Aguilar, and L. Baldomà. 1994. Molecular characterization of Escherichia coli malate synthase G. Differentiation with the malate synthase A isoenzyme. Eur. J. Biochem. 224:541-548
    • (1994) Eur. J. Biochem. , vol.224 , pp. 541-548
    • Molina, I.1    Pellicer, M.T.2    Badiá, J.3    Aguilar, J.4    Baldomà, L.5
  • 26
    • 0027254760 scopus 로고
    • Sequencing and characterization of a gene cluster encoding the enzymes for L-rhamnose metabolism in Escherichia coli
    • Moralejo, P., S. M. Egan, E. Hidalgo, and J. Aguilar. 1993. Sequencing and characterization of a gene cluster encoding the enzymes for L-rhamnose metabolism in Escherichia coli. J. Bacteriol 175:5585-5594.
    • (1993) J. Bacteriol , vol.175 , pp. 5585-5594
    • Moralejo, P.1    Egan, S.M.2    Hidalgo, E.3    Aguilar, J.4
  • 27
    • 0014529445 scopus 로고
    • Regulation of glyoxylate metabolism in Escherichia coli K-12
    • Ornston, L. N., and M. K. Ornston. 1969. Regulation of glyoxylate metabolism in Escherichia coli K-12. J. Bacteriol. 98:1098-1108.
    • (1969) J. Bacteriol. , vol.98 , pp. 1098-1108
    • Ornston, L.N.1    Ornston, M.K.2
  • 28
    • 0024352951 scopus 로고
    • The intracellular localization of glycolate oxidoreductase in Escherichia coli
    • Sallal, A.-K. J., and N. A. Nimer. 1989 The intracellular localization of glycolate oxidoreductase in Escherichia coli. FEBS Lett. 258:277-280.
    • (1989) FEBS Lett. , vol.258 , pp. 277-280
    • Sallal, A.-K.J.1    Nimer, N.A.2
  • 31
    • 0025127054 scopus 로고
    • Nucleotide sequence of the gene encoding the repressor for the histidine utilization genes of Klebsiella aerogenes
    • Schwacha, A., and R. A. Bender. 1990. Nucleotide sequence of the gene encoding the repressor for the histidine utilization genes of Klebsiella aerogenes. J. Bacteriol. 172:5477-5451
    • (1990) J. Bacteriol. , vol.172 , pp. 5477-15451
    • Schwacha, A.1    Bender, R.A.2
  • 33
    • 0021094214 scopus 로고
    • Nucleotide sequence of the lipoamide dehydrogenase gene of Escherichia coli K-12
    • Stephens, P. E., H. M. Lewis, M. G. Darlison, and J. R. Guest. 1983. Nucleotide sequence of the lipoamide dehydrogenase gene of Escherichia coli K-12. Eur. J. Biochem. 135:519-527.
    • (1983) Eur. J. Biochem. , vol.135 , pp. 519-527
    • Stephens, P.E.1    Lewis, H.M.2    Darlison, M.G.3    Guest, J.R.4
  • 34
    • 0011214362 scopus 로고
    • "In vivo" gene expression systems in prokaryotes
    • B. D. Hames and S. H. Higgins (ed.), IRL Press Ltd., Oxford
    • Stoker, N. G., J. M. Pratt, and H. B. Holland. 1984 "In vivo" gene expression systems in prokaryotes, p. 154-172. In B. D. Hames and S. H. Higgins (ed.), Transcription and translation: a practical approach. IRL Press Ltd., Oxford.
    • (1984) Transcription and Translation: A Practical Approach , pp. 154-172
    • Stoker, N.G.1    Pratt, J.M.2    Holland, H.B.3
  • 35
    • 0015807494 scopus 로고
    • The primary structure of the Clostridium thermosaccharolyticum ferredoxin, a heat stable ferredoxin
    • Tanaka, M., M. Haniu, K. T. Yasunobu, H. H. Himes, and J. M. Akagi. 1973. The primary structure of the Clostridium thermosaccharolyticum ferredoxin, a heat stable ferredoxin. J. Biol. Chem. 248:2215-2217.
    • (1973) J. Biol. Chem. , vol.248 , pp. 2215-2217
    • Tanaka, M.1    Haniu, M.2    Yasunobu, K.T.3    Himes, H.H.4    Akagi, J.M.5
  • 36
    • 0014300025 scopus 로고
    • Physiologie et génétique de l'isocitritase et des malate synthases chez Escherichia coli
    • Vanderwinkel, E., and M. De Vlieghere. 1968. Physiologie et génétique de l'isocitritase et des malate synthases chez Escherichia coli. Eur. J. Biochem. 5:81-90.
    • (1968) Eur. J. Biochem. , vol.5 , pp. 81-90
    • Vanderwinkel, E.1    De Vlieghere, M.2
  • 37
    • 0015928150 scopus 로고
    • Genetic transformation in E. coli: The inhibitory role of the recBC DNase
    • Wackernagel, W. 1973. Genetic transformation in E. coli: the inhibitory role of the recBC DNase. Biochem. Biophys. Res. Commun. 51:306-311.
    • (1973) Biochem. Biophys. Res. Commun. , vol.51 , pp. 306-311
    • Wackernagel, W.1
  • 38
    • 0021992336 scopus 로고
    • Site-directed insertion and deletion mutagenesis with cloned fragments in Escherichia coli
    • Winans, S. C., S. J. Elledge, J. H. Krueger, and G. C. Walker. 1985. Site-directed insertion and deletion mutagenesis with cloned fragments in Escherichia coli. J. Bacteriol. 161:1219-1221.
    • (1985) J. Bacteriol. , vol.161 , pp. 1219-1221
    • Winans, S.C.1    Elledge, S.J.2    Krueger, J.H.3    Walker, G.C.4
  • 39
    • 0021487096 scopus 로고
    • Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli
    • Woods, D., M. G. Darlison, R. J. Wilde, and J. R. Guest. 1984 Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli. Biochem. J. 222:519-534.
    • (1984) Biochem. J. , vol.222 , pp. 519-534
    • Woods, D.1    Darlison, M.G.2    Wilde, R.J.3    Guest, J.R.4


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