메뉴 건너뛰기




Volumn 33, Issue 6, 1999, Pages 1221-1231

Glycerol-3-phosphate-mediated repression of malT in Escherichia coli does not require metabolism, depends on enzyme IIA(Glc) and is mediated by cAMP levels

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLATE CYCLASE; BACTERIAL ENZYME; CYCLIC AMP; DIHYDROXYACETONE PHOSPHATE; GLYCEROL; GLYCEROPHOSPHATE; MALTOSE; PHOSPHOTRANSFERASE; RECEPTOR PROTEIN; XYLOSE;

EID: 0032884020     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1999.01570.x     Document Type: Article
Times cited : (35)

References (62)
  • 1
    • 0032421104 scopus 로고    scopus 로고
    • Analysis of the effect exerted by extracellular pH on the maltose reguion in Escherichia coli K-12
    • Alongzo S., Hevde, M., Laloi, P., and Portalier, R. (1998) Analysis of the effect exerted by extracellular pH on the maltose reguion in Escherichia coli K-12. Microbiology 144: 3317-3325.
    • (1998) Microbiology , vol.144 , pp. 3317-3325
    • Alonzo, S.1    Hevde, M.2    Laloi, P.3    Portalier, R.4
  • 2
    • 0025651896 scopus 로고
    • Mutations that alter the ability of the Escherichia coli cyclic AMP receptor protein to activate transcription
    • Bell, A., Gaston, K., Williams, R., Chapman, K., Kolb, A., Buc, H., et al. (1990) Mutations that alter the ability of the Escherichia coli cyclic AMP receptor protein to activate transcription. Nucleic Acids Res 18: 7243-7250.
    • (1990) Nucleic Acids Res , vol.18 , pp. 7243-7250
    • Bell, A.1    Gaston, K.2    Williams, R.3    Chapman, K.4    Kolb, A.5    Buc, H.6
  • 3
    • 0021951798 scopus 로고
    • Temperature-sensitive catabolite activator protein in Escherichia coli BUG6
    • Benner, D., Müller, N., and Boos, W. (1985) Temperature-sensitive catabolite activator protein in Escherichia coli BUG6. J Bacteriol 161: 347-352.
    • (1985) J Bacteriol , vol.161 , pp. 347-352
    • Benner, D.1    Müller, N.2    Boos, W.3
  • 4
    • 0031887807 scopus 로고    scopus 로고
    • The maltose/maltodextrin system of Escherichia coli; transport, metabolism and regulation
    • Boos, W., and Shuman, H.A. (1998) The maltose/maltodextrin system of Escherichia coli; transport, metabolism and regulation. Microbiol Mol Biol Rev 62: 204-229.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 204-229
    • Boos, W.1    Shuman, H.A.2
  • 6
    • 0021866359 scopus 로고
    • Transposable λplac Mu bacteriophages for creating lacZ operon fusions and kanamycin resistance insertions in Escherichia coli
    • Bremer, E., Silhavy, T.J., and Weinstock, J.M. (1985) Transposable λplac Mu bacteriophages for creating lacZ operon fusions and kanamycin resistance insertions in Escherichia coli. J Bacteriol 162: 1092-1099.
    • (1985) J Bacteriol , vol.162 , pp. 1092-1099
    • Bremer, E.1    Silhavy, T.J.2    Weinstock, J.M.3
  • 7
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu
    • Casadaban, M.J. (1976) Transposition and fusion of the lac genes to selected promoters in 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
  • 8
    • 0020338594 scopus 로고
    • Expression of malT, the regulator gene of the maltose region in Escherichia coli, is limited both at transcription and translation
    • Chapon, C. (1982) Expression of malT, the regulator gene of the maltose region in Escherichia coli, is limited both at transcription and translation. EMBO J 1: 369-374.
    • (1982) EMBO J , vol.1 , pp. 369-374
    • Chapon, C.1
  • 9
    • 0021055023 scopus 로고
    • Action of CAP on the malT promoter in vitro
    • Chapon, C., and Kolb, A. (1983) Action of CAP on the malT promoter in vitro. J Bacteriol 156: 1135-1143.
    • (1983) J Bacteriol , vol.156 , pp. 1135-1143
    • Chapon, C.1    Kolb, A.2
  • 10
    • 0000544768 scopus 로고
    • The formation and catabolism of methylglyoxal during glycolysis in E. coli
    • Cooper, R.A., and Anderson, A. (1970) The formation and catabolism of methylglyoxal during glycolysis in E. coli. FEBS Lett 11: 273-276.
    • (1970) FEBS Lett , vol.11 , pp. 273-276
    • Cooper, R.A.1    Anderson, A.2
  • 11
    • 0027200708 scopus 로고
    • Maltose and maltotriose can be formed endogenously in Escherichia coli from glucose and glucose-1-phosphate independently of enzymes of the maltose system
    • Decker, K., Peist, R., Reidl, J., Kossmann, M., Brand, B., and Boos, W. (1993) Maltose and maltotriose can be formed endogenously in Escherichia coli from glucose and glucose-1-phosphate independently of enzymes of the maltose system. J Bacteriol 175: 5655-5665.
    • (1993) J Bacteriol , vol.175 , pp. 5655-5665
    • Decker, K.1    Peist, R.2    Reidl, J.3    Kossmann, M.4    Brand, B.5    Boos, W.6
  • 12
    • 0031983641 scopus 로고    scopus 로고
    • Negative transcriptional regulation of a positive regulator: The expression of malT, encoding the transcriptional activator of the maltose regulon of Escherichia coli, is negatively controlled by Mlc
    • Decker, K., Plumbridge, J., and Boos, W. (1998) Negative transcriptional regulation of a positive regulator: the expression of malT, encoding the transcriptional activator of the maltose regulon of Escherichia coli, is negatively controlled by Mlc. Mol Microbiol 27: 381-390.
    • (1998) Mol Microbiol , vol.27 , pp. 381-390
    • Decker, K.1    Plumbridge, J.2    Boos, W.3
  • 13
    • 0033047695 scopus 로고    scopus 로고
    • The role of the trehalose system in regulating the maltose regulon of Escherichia coli
    • Decker, K., Gerhardt, F., and Boos, W. (1999) The role of the trehalose system in regulating the maltose regulon of Escherichia coli. Mol Microbiol 32: 777-788.
    • (1999) Mol Microbiol , vol.32 , pp. 777-788
    • Decker, K.1    Gerhardt, F.2    Boos, W.3
  • 14
    • 0018097321 scopus 로고
    • Pole cap formation in Escherichia coli following induction of the maltose-binding protein
    • Dietzel, I., Kolb, V., and Boos, W. (1978) Pole cap formation in Escherichia coli following induction of the maltose-binding protein. Arch Microbiol 118: 207-218.
    • (1978) Arch Microbiol , vol.118 , pp. 207-218
    • Dietzel, I.1    Kolb, V.2    Boos, W.3
  • 15
    • 0019332779 scopus 로고
    • Mutations affecting localization of an Escherichia coli outer membrane protein, the bacteriophage lambda receptor
    • Emr, S.D., and Silhavy, T.J. (1980) Mutations affecting localization of an Escherichia coli outer membrane protein, the bacteriophage lambda receptor. J Mol Biol 141: 63-90.
    • (1980) J Mol Biol , vol.141 , pp. 63-90
    • Emr, S.D.1    Silhavy, T.J.2
  • 16
    • 0000819850 scopus 로고
    • Adenosine 3′:5′-cyclic monophosphate as mediator of catabolite repression in Escherichia coli
    • Epstein, W., Rothman-Denes, L.B., and Hesse, J. (1975) Adenosine 3′:5′-cyclic monophosphate as mediator of catabolite repression in Escherichia coli. Proc Nat Acad Sci USA 72: 2300-2304.
    • (1975) Proc Nat Acad Sci USA , vol.72 , pp. 2300-2304
    • Epstein, W.1    Rothman-Denes, L.B.2    Hesse, J.3
  • 17
    • 0023906938 scopus 로고
    • Facilitated diffusion of p-nitrophenyl-α-D-maltohexaoside through the outer membrane of Escherichia coli
    • Freundlieb, S., Ehmann, U., and Boos, W. (1988) Facilitated diffusion of p-nitrophenyl-α-D-maltohexaoside through the outer membrane of Escherichia coli. J Biol Chem 263: 314-320.
    • (1988) J Biol Chem , vol.263 , pp. 314-320
    • Freundlieb, S.1    Ehmann, U.2    Boos, W.3
  • 18
    • 0023785204 scopus 로고
    • Scanning calorimetric study of the thermal unfolding of catabolite activator protein from Escherichia coli in the absence and presence of cyclic mononucleotides
    • Ghosaini, L.R., Brown, A.M., and Sturtevant, J.M. (1988) Scanning calorimetric study of the thermal unfolding of catabolite activator protein from Escherichia coli in the absence and presence of cyclic mononucleotides. Biochemistry 27: 5257-5261.
    • (1988) Biochemistry , vol.27 , pp. 5257-5261
    • Ghosaini, L.R.1    Brown, A.M.2    Sturtevant, J.M.3
  • 19
    • 0025773408 scopus 로고
    • Molecular mechanism of negative autoregulation of Escherichia coli crp gene
    • Hanamura, A., and Aiba, H. (1991) Molecular mechanism of negative autoregulation of Escherichia coli crp gene. Nucleic Acids Res 19: 4413-4419.
    • (1991) Nucleic Acids Res , vol.19 , pp. 4413-4419
    • Hanamura, A.1    Aiba, H.2
  • 20
    • 0027209454 scopus 로고
    • Mutations in phoB, the positive gene activator of the pho regulon in Escherichia coli, affect the carbohydrate phenotype on MacConkey indicator plates
    • Hartmann, A., and Boos, W. (1993) Mutations in phoB, the positive gene activator of the pho regulon in Escherichia coli, affect the carbohydrate phenotype on MacConkey indicator plates. Res Microbiol 144: 285-293.
    • (1993) Res Microbiol , vol.144 , pp. 285-293
    • Hartmann, A.1    Boos, W.2
  • 21
    • 0001385085 scopus 로고
    • Active transport of L-alpha-glycerophosphate in Escherichia coli
    • Hayashi, S., Koch, J.P., and Lin, E.C.C. (1964) Active transport of L-alpha-glycerophosphate in Escherichia coli. J Biol Chem 239: 3098-3105.
    • (1964) J Biol Chem , vol.239 , pp. 3098-3105
    • Hayashi, S.1    Koch, J.P.2    Lin, E.C.C.3
  • 22
    • 0025945286 scopus 로고
    • Identification of Escherichia coli genes whose expression increases as a function of external pH
    • Heyde, M., Coll, J.L., and Portalier, R. (1991) Identification of Escherichia coli genes whose expression increases as a function of external pH. Mol Gen Genet 229: 197-205.
    • (1991) Mol Gen Genet , vol.229 , pp. 197-205
    • Heyde, M.1    Coll, J.L.2    Portalier, R.3
  • 23
    • 0024462882 scopus 로고
    • Escherichia coli cAMP receptor protein: Evidence for three protein conformational states with different promoter binding affinities
    • Heyduk, T., and Lee, J.C. (1989) Escherichia coli cAMP receptor protein: evidence for three protein conformational states with different promoter binding affinities. Biochemistry 28: 6914-6924.
    • (1989) Biochemistry , vol.28 , pp. 6914-6924
    • Heyduk, T.1    Lee, J.C.2
  • 25
    • 0030905517 scopus 로고    scopus 로고
    • Catabolite repression by glucose 6-phosphate, gluconate and lactose in Escherichia coli
    • Hogema, B.M., Arents, J.C., Inada, T., Aiba, H., van Dam, K., and Postma, P.W. (1997) Catabolite repression by glucose 6-phosphate, gluconate and lactose in Escherichia coli. Mol Microbiol 24: 857-867.
    • (1997) Mol Microbiol , vol.24 , pp. 857-867
    • Hogema, B.M.1    Arents, J.C.2    Inada, T.3    Aiba, H.4    Van Dam, K.5    Postma, P.W.6
  • 28
    • 0001515246 scopus 로고
    • The regulation of E. coli methylglyoxal synthase. A new control site in glycolysis
    • Hopper, D.J., and Cooper, R.A. (1971) The regulation of E. coli methylglyoxal synthase. A new control site in glycolysis. FEBS Lett 13: 213-216.
    • (1971) FEBS Lett , vol.13 , pp. 213-216
    • Hopper, D.J.1    Cooper, R.A.2
  • 29
    • 0029906892 scopus 로고    scopus 로고
    • Down regulation of cAMP production by cAMP receptor protein in Escherichia coli: An assessment of the contributions of transcriptional and posttranscriptional control of adenylate cyclase
    • Inada, T., Takahashi, H., Mizuno, T., and Aiba, H. (1996) Down regulation of cAMP production by cAMP receptor protein in Escherichia coli: an assessment of the contributions of transcriptional and posttranscriptional control of adenylate cyclase. Mol Gen Genet 253: 198-204.
    • (1996) Mol Gen Genet , vol.253 , pp. 198-204
    • Inada, T.1    Takahashi, H.2    Mizuno, T.3    Aiba, H.4
  • 30
    • 0027376662 scopus 로고
    • A lowered concentration of cAMP receptor protein caused by glucose is an important determinant for catabolite repression in Escherichia coli
    • Ishizuka, H., Hanamura, A., Kunimura, T., and Aiba, H. (1993) A lowered concentration of cAMP receptor protein caused by glucose is an important determinant for catabolite repression in Escherichia coli. Mol Microbiol 10: 341-350.
    • (1993) Mol Microbiol , vol.10 , pp. 341-350
    • Ishizuka, H.1    Hanamura, A.2    Kunimura, T.3    Aiba, H.4
  • 31
    • 0028298782 scopus 로고
    • Mechanism of the down-regulation of cAMP receptor protein by glucose in Escherichia coli: Role of autoregulation of the crp gene
    • Ishizuka, H., Hanamura, A., Inada, T., and Aiba, H. (1994) Mechanism of the down-regulation of cAMP receptor protein by glucose in Escherichia coli: Role of autoregulation of the crp gene. EMBO J 13: 3077-3082.
    • (1994) EMBO J , vol.13 , pp. 3077-3082
    • Ishizuka, H.1    Hanamura, A.2    Inada, T.3    Aiba, H.4
  • 32
    • 0030698856 scopus 로고    scopus 로고
    • cAMP receptor protein-cAMP plays a crucial role in glucose-lactose diauxie by activating the major glucose transporter gene in Escherichia coli
    • Kimata, K., Takahashi, H., Inada, T., Postma, P., and Aiba, H. (1997) cAMP receptor protein-cAMP plays a crucial role in glucose-lactose diauxie by activating the major glucose transporter gene in Escherichia coli. Proc Natl Acad Sci USA 94: 12914-12919.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12914-12919
    • Kimata, K.1    Takahashi, H.2    Inada, T.3    Postma, P.4    Aiba, H.5
  • 33
    • 0031697458 scopus 로고    scopus 로고
    • A global repressor (Mlc) is involved in glucose induction of the ptsG gene encoding major glucose transporter in Escherichia coli
    • Kimata, K., Inada, T., Tagami, H., and Aiba, H. (1998) A global repressor (Mlc) is involved in glucose induction of the ptsG gene encoding major glucose transporter in Escherichia coli. Mol Microbiol 29:1509-1519.
    • (1998) Mol Microbiol , vol.29 , pp. 1509-1519
    • Kimata, K.1    Inada, T.2    Tagami, H.3    Aiba, H.4
  • 34
    • 0029013340 scopus 로고
    • Molecular analysis of treB encoding the Escherichia coli enzyme II specific for trehalose
    • Klein, W., Horlacher, R., and Boos, W. (1995) Molecular analysis of treB encoding the Escherichia coli enzyme II specific for trehalose. J Bacteriol 177; 4043-4052.
    • (1995) J Bacteriol , vol.177 , pp. 4043-4052
    • Klein, W.1    Horlacher, R.2    Boos, W.3
  • 35
    • 0027236999 scopus 로고
    • Transcriptional regulation by cAMP and its receptor protein
    • Kolb, A., Busby, S., Buc, H., Garges, S., and Adhya, S. (1993) Transcriptional regulation by cAMP and its receptor protein. Annu Rev Biochem 62: 749-795.
    • (1993) Annu Rev Biochem , vol.62 , pp. 749-795
    • Kolb, A.1    Busby, S.2    Buc, H.3    Garges, S.4    Adhya, S.5
  • 36
    • 0030856586 scopus 로고    scopus 로고
    • The global regulator CsrA of Escherichia coli is a specific mRNA-binding protein
    • Liu, M.Y., and Romeo, T. (1997) The global regulator CsrA of Escherichia coli is a specific mRNA-binding protein. J Bacteriol 179: 4639-4642.
    • (1997) J Bacteriol , vol.179 , pp. 4639-4642
    • Liu, M.Y.1    Romeo, T.2
  • 38
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Miller, J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 39
    • 0019877801 scopus 로고
    • Affinity purification of antibodies from diazotized paper blots of heterogeneous protein samples
    • Olmsted, J.B. (1981) Affinity purification of antibodies from diazotized paper blots of heterogeneous protein samples. J Biol Chem 256: 11955-11957.
    • (1981) J Biol Chem , vol.256 , pp. 11955-11957
    • Olmsted, J.B.1
  • 40
    • 0031768746 scopus 로고    scopus 로고
    • The ATP-binding cassette subunit of the maltose transporter MalK antagonizes MalT, the activator of the Escherichia coli mal regulon
    • Panagiotidis, C.H., Boos, W., and Shuman, H.A. (1998) The ATP-binding cassette subunit of the maltose transporter MalK antagonizes MalT, the activator of the Escherichia coli mal regulon. Mol Microbiol 30: 535-546.
    • (1998) Mol Microbiol , vol.30 , pp. 535-546
    • Panagiotidis, C.H.1    Boos, W.2    Shuman, H.A.3
  • 41
    • 0030781626 scopus 로고    scopus 로고
    • Characterization of the aes gene of Escherichia coli encoding an enzyme with esterase activity
    • Peist, R., Koch, A., Bolek, P., Sewitz, S., Kolbus, T., and Boos, W. (1997) Characterization of the aes gene of Escherichia coli encoding an enzyme with esterase activity. J Bacteriol 179: 7679-7686.
    • (1997) J Bacteriol , vol.179 , pp. 7679-7686
    • Peist, R.1    Koch, A.2    Bolek, P.3    Sewitz, S.4    Kolbus, T.5    Boos, W.6
  • 42
    • 0024327471 scopus 로고
    • Regulation of Escherichia coli adenylate cyclase activity by the phosphoenolpyruvate:sugar phosphotransferase system
    • Peterkofsky, A., Svenson, I., and Amin, N. (1989) Regulation of Escherichia coli adenylate cyclase activity by the phosphoenolpyruvate:sugar phosphotransferase system. FEMS Microbiol Rev 63: 103-108.
    • (1989) FEMS Microbiol Rev , vol.63 , pp. 103-108
    • Peterkofsky, A.1    Svenson, I.2    Amin, N.3
  • 43
    • 0029152980 scopus 로고
    • The Escherichia coli adenylyl cyclase complex: Requirement of PTS proteins for stimulation by nucleotides
    • Peterkofsky, A., Seok, Y.J., Amin, N., Thapar, R., Lee, S.Y., Klevit, R.E., et al. (1995) The Escherichia coli adenylyl cyclase complex: requirement of PTS proteins for stimulation by nucleotides. Biochemistry 34: 8950-8959.
    • (1995) Biochemistry , vol.34 , pp. 8950-8959
    • Peterkofsky, A.1    Seok, Y.J.2    Amin, N.3    Thapar, R.4    Lee, S.Y.5    Klevit, R.E.6
  • 44
    • 0031973888 scopus 로고    scopus 로고
    • Control of the expression of the man-XYZ operon in Escherichia coli: Mlc is a negative regulator of the mannose PTS
    • Plumbridge, J. (1997) Control of the expression of the man-XYZ operon in Escherichia coli: Mlc is a negative regulator of the mannose PTS. Mol Microbiol 27: 369-380.
    • (1997) Mol Microbiol , vol.27 , pp. 369-380
    • Plumbridge, J.1
  • 45
    • 0031866040 scopus 로고    scopus 로고
    • Expression of ptsG, the gene for the major glucose PTS transporter in Escherichia coli, is repressed by Mlc and induced by growth on glucose
    • Plumbridge, J. (1998) Expression of ptsG, the gene for the major glucose PTS transporter in Escherichia coli, is repressed by Mlc and induced by growth on glucose. Mol Microbiol 29: 1053-1063.
    • (1998) Mol Microbiol , vol.29 , pp. 1053-1063
    • Plumbridge, J.1
  • 46
    • 0001014412 scopus 로고    scopus 로고
    • Phosphoenolpyruvate: Carbohydrate phosphotransferase system
    • Escherichia coli and Salmonella typhimurium; Neidhardt, F.C., Curtiss, R., Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., et al. (eds). Washington, DC: American Society for Microbiology Press
    • Postma, P.W., Lengeler, J.W., and Jacobson, G.R. (1996) Phosphoenolpyruvate:carbohydrate phosphotransferase system. In Escherichia coli and Salmonella typhimurium; Cellular and Molecular Biology. Neidhardt, F.C., Curtiss, R., Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., et al. (eds). Washington, DC: American Society for Microbiology Press, pp. 1149-1174.
    • (1996) Cellular and Molecular Biology , pp. 1149-1174
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 47
    • 0020540489 scopus 로고
    • Use of deletions created in vitro to map transcriptional regulatory signals in the malA region of Escherichia coli
    • Raibaud, O., Débarbouillé, M., and Schwartz, M. (1983) Use of deletions created in vitro to map transcriptional regulatory signals in the malA region of Escherichia coli. J Mol Biol 163: 395-408.
    • (1983) J Mol Biol , vol.163 , pp. 395-408
    • Raibaud, O.1    Débarbouillé, M.2    Schwartz, M.3
  • 48
    • 0024095619 scopus 로고
    • Overproduction of MalK protein prevents expression of the Escherichia coli mal regulon
    • Reyes, M., and Shuman, H.A. (1988) Overproduction of MalK protein prevents expression of the Escherichia coli mal regulon. J Bacteriol 170: 4598-4602.
    • (1988) J Bacteriol , vol.170 , pp. 4598-4602
    • Reyes, M.1    Shuman, H.A.2
  • 49
    • 0030596146 scopus 로고    scopus 로고
    • On the role of the multiple regulatory elements involved in the activation of the Escherichia coli malEp promoter
    • Richet, E. (1996) On the role of the multiple regulatory elements involved in the activation of the Escherichia coli malEp promoter. J Mol Biol 264: 852-862.
    • (1996) J Mol Biol , vol.264 , pp. 852-862
    • Richet, E.1
  • 50
    • 0031854376 scopus 로고    scopus 로고
    • Limits to inducer exclusion: Inhibition of the bacterial phosphotransferase system by glycerol kinase
    • Rohwer, J.M., Bader, R., Westerhoff, H.V., and Postma, P.W. (1998) Limits to inducer exclusion: inhibition of the bacterial phosphotransferase system by glycerol kinase. Mol Microbiol 29: 641-652.
    • (1998) Mol Microbiol , vol.29 , pp. 641-652
    • Rohwer, J.M.1    Bader, R.2    Westerhoff, H.V.3    Postma, P.W.4
  • 51
    • 0029941168 scopus 로고    scopus 로고
    • The catabolite repressor activator (Cra) protein of enteric bacteria
    • Saier M.H. and Ramseier, T.M. (1996) The catabolite repressor activator (Cra) protein of enteric bacteria. J Bacteriol 178: 3411-3417.
    • (1996) J Bacteriol , vol.178 , pp. 3411-3417
    • Saier, M.H.1    Ramseier, T.M.2
  • 53
    • 0015623514 scopus 로고
    • Regulation of the β-methylgalactoside transport system and the galactose-binding protein by the cell cycle of Escherichia coli
    • Shen B.H.P., and Boos, W (1973) Regulation of the β-methylgalactoside transport system and the galactose-binding protein by the cell cycle of Escherichia coli. Proc Natl Acad Sci USA 70: 1481-1485.
    • (1973) Proc Natl Acad Sci USA , vol.70 , pp. 1481-1485
    • Shen, B.H.P.1    Boos, W.2
  • 55
    • 0028923213 scopus 로고
    • Role of CRP in transcription activation at Escherichia coli lac promoter: CRP is dispensable after the formation of open complex
    • Tagami, H., and Aiba, H. (1995) Role of CRP in transcription activation at Escherichia coli lac promoter: CRP is dispensable after the formation of open complex. Nucleic Acids Res 23: 599-605.
    • (1995) Nucleic Acids Res , vol.23 , pp. 599-605
    • Tagami, H.1    Aiba, H.2
  • 56
    • 0029142624 scopus 로고
    • Glucose lowers CRP levels resulting in repression of the lac optron in cells lacking cAMP
    • Tagami, H., Inada, T., Kunimura, T., and Aiba, H. (1995) Glucose lowers CRP levels resulting in repression of the lac optron in cells lacking cAMP. Mol Microbiol 17: 251-258.
    • (1995) Mol Microbiol , vol.17 , pp. 251-258
    • Tagami, H.1    Inada, T.2    Kunimura, T.3    Aiba, H.4
  • 57
    • 0031686015 scopus 로고    scopus 로고
    • Glc, the glucose-specific phosphotransferase protein in Escherichia coli
    • Glc, the glucose-specific phosphotransferase protein in Escherichia coli. Mol Gen Genet 259: 317-326.
    • (1998) Mol Gen Genet , vol.259 , pp. 317-326
    • Takahashi, H.1    Inada, T.2    Postma, P.3    Aiba, H.4
  • 58
    • 0025985499 scopus 로고
    • The malZ gene of Escherichia coli, a member of the maltose regulon, encodes a maltodextrin glucosidase
    • Tapio, S., Yeh, F., Shuman, H.A., and Boos, W. (1991) The malZ gene of Escherichia coli, a member of the maltose regulon, encodes a maltodextrin glucosidase. J Biol Chem 266: 19450-19458.
    • (1991) J Biol Chem , vol.266 , pp. 19450-19458
    • Tapio, S.1    Yeh, F.2    Shuman, H.A.3    Boos, W.4
  • 59
    • 0026698144 scopus 로고
    • Molecular analysis of the glpFKX regions of Escherichia coli and Shigella flexneri
    • Truniger, V., Boos, W., and Sweet, G. (1992) Molecular analysis of the glpFKX regions of Escherichia coli and Shigella flexneri. J Bacteriol 174: 6981-6991.
    • (1992) J Bacteriol , vol.174 , pp. 6981-6991
    • Truniger, V.1    Boos, W.2    Sweet, G.3
  • 60
    • 0031686598 scopus 로고    scopus 로고
    • Effect of slow growth on metabolism of Escherichia coli, as revealed by global metabolite pool ('metabolome') analysis
    • Tweeddale, H., Notley-McRobb, L., and Ferenci, T. (1998) Effect of slow growth on metabolism of Escherichia coli, as revealed by global metabolite pool ('metabolome') analysis, J Bacteriol 180: 5109-5116.
    • (1998) J Bacteriol , vol.180 , pp. 5109-5116
    • Tweeddale, H.1    Notley-McRobb, L.2    Ferenci, T.3
  • 61
    • 0020619694 scopus 로고
    • Purification and characterization of adenylate cyclase from E. coli
    • Yang, J.K., and Epstein, W. (1983) Purification and characterization of adenylate cyclase from E. coli. J Biol Chem 258: 3750-3758.
    • (1983) J Biol Chem , vol.258 , pp. 3750-3758
    • Yang, J.K.1    Epstein, W.2
  • 62
    • 0029127483 scopus 로고
    • MalY of Escherichia coli is an enzyme with the activity of a βC-S lyase (cystathionase)
    • Zdych, E., Peist, R., Reidl, J., and Boos, W. (1995) MalY of Escherichia coli is an enzyme with the activity of a βC-S lyase (cystathionase). J Bacteriol 177: 5035-5039.
    • (1995) J Bacteriol , vol.177 , pp. 5035-5039
    • Zdych, E.1    Peist, R.2    Reidl, J.3    Boos, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.