메뉴 건너뛰기




Volumn 85, Issue 12, 1998, Pages 583-592

Coupling physiology and gene regulation in bacteria: The phosphotransferase sugar uptake system delivers the signals

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP DERIVATIVE; DNA DIRECTED RNA POLYMERASE; PHOSPHOTRANSFERASE; SERINE;

EID: 0031774448     PISSN: 00281042     EISSN: None     Source Type: Journal    
DOI: 10.1007/s001140050555     Document Type: Review
Times cited : (63)

References (95)
  • 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 CA, Siebers U (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
  • 2
    • 0026739805 scopus 로고
    • Modulation of the dimerization of a transcriptional antiterminator protein by phosphorylation
    • Amster-Choder O, Wright A (1992) Modulation of the dimerization of a transcriptional antiterminator protein by phosphorylation. Science 257:1395-1398
    • (1992) Science , vol.257 , pp. 1395-1398
    • Amster-Choder, O.1    Wright, A.2
  • 3
    • 0030931685 scopus 로고    scopus 로고
    • BglG, the response regulator of the Escherichia coli bgl operon, is phosphorylated on a histidine residue
    • Amster-Choder O, Wright A (1997) BglG, the response regulator of the Escherichia coli bgl operon, is phosphorylated on a histidine residue. J Bacteriol 179:5621-5624
    • (1997) J Bacteriol , vol.179 , pp. 5621-5624
    • Amster-Choder, O.1    Wright, A.2
  • 4
    • 0024462409 scopus 로고
    • Protein phosphorylation regulates transcription of the β-glucoside utilization operon in E. coli
    • Amster-Choder O, Houman F, Wright A (1989) Protein phosphorylation regulates transcription of the β-glucoside utilization operon in E. coli. Cell 58:847-855
    • (1989) Cell , vol.58 , pp. 847-855
    • Amster-Choder, O.1    Houman, F.2    Wright, A.3
  • 5
    • 0026772662 scopus 로고
    • Regulation of the sacPA operon of Bacillus subtilis: Identification of phosphotransferase system components involved in SacT activity
    • Arnaud M, Vary P, Zagorec M, Klier A. Débarbouillé M, Postma P, Rapoport G (1992) Regulation of the sacPA operon of Bacillus subtilis: Identification of phosphotransferase system components involved in SacT activity. J Bacteriol 174:3161-3170
    • (1992) J Bacteriol , vol.174 , pp. 3161-3170
    • Arnaud, M.1    Vary, P.2    Zagorec, M.3    Klier, A.4    Débarbouillé, M.5    Postma, P.6    Rapoport, G.7
  • 6
    • 0029763998 scopus 로고    scopus 로고
    • In vitro reconstitution of transcriptional antitermination by the SacT and SacY proteins of Bacillus subtilis
    • Arnaud M, Débarbouillé M, Rapoport G, Saier MH, Reizer J (1996) In vitro reconstitution of transcriptional antitermination by the SacT and SacY proteins of Bacillus subtilis. J Biol Chem 271:18966-18972
    • (1996) J Biol Chem , vol.271 , pp. 18966-18972
    • Arnaud, M.1    Débarbouillé, M.2    Rapoport, G.3    Saier, M.H.4    Reizer, J.5
  • 7
    • 0031573040 scopus 로고    scopus 로고
    • Characterization of the presumptive phosphorylation sites of the Bacillus subtilis glucose permease by site-directed mutagenesis: Implication in glucose transport and catabolite repression
    • Bachem S, Faires N, Stülke J (1997) Characterization of the presumptive phosphorylation sites of the Bacillus subtilis glucose permease by site-directed mutagenesis: implication in glucose transport and catabolite repression. FEMS Microbiol Lett 156:233-238
    • (1997) FEMS Microbiol Lett , vol.156 , pp. 233-238
    • Bachem, S.1    Faires, N.2    Stülke, J.3
  • 8
    • 0031711025 scopus 로고    scopus 로고
    • Regulation of the Bacillus subtilis GlcT antiterminator protein by components of the phosphotransferase system
    • Bachem S, Stülke J (1999) Regulation of the Bacillus subtilis GlcT antiterminator protein by components of the phosphotransferase system. J Bacteriol 180:5319-5326
    • (1999) J Bacteriol , vol.180 , pp. 5319-5326
    • Bachem, S.1    Stülke, J.2
  • 9
    • 0030971645 scopus 로고    scopus 로고
    • Cloning and sequencing of two enterococcal glpK genes and regulation of the encoded glycerol kinases by phosphoenolpyruvate-dependent, phosphotransferase system-catalyzed phosphorylation of a single histidyl residue
    • Charrier V, Buckley E, Parsonage D, Galinier A, Darbon E, Jaquinod M, Forest E, Deutseher J, Claiborne A (1997a) Cloning and sequencing of two enterococcal glpK genes and regulation of the encoded glycerol kinases by phosphoenolpyruvate-dependent, phosphotransferase system-catalyzed phosphorylation of a single histidyl residue. J Biol Chem 272:14166-14174
    • (1997) J Biol Chem , vol.272 , pp. 14166-14174
    • Charrier, V.1    Buckley, E.2    Parsonage, D.3    Galinier, A.4    Darbon, E.5    Jaquinod, M.6    Forest, E.7    Deutseher, J.8    Claiborne, A.9
  • 10
    • 0031046651 scopus 로고    scopus 로고
    • Protein phosphorylation chain of a Bacillus subtilis fructose-specific phosphotransferase system and its participation in regulation of the expression of the lev operon
    • Charrier V, Deutscher J, Martin-Verstraete I (1997b) Protein phosphorylation chain of a Bacillus subtilis fructose-specific phosphotransferase system and its participation in regulation of the expression of the lev operon. Biochemistry 36:1163-1172
    • (1997) Biochemistry , vol.36 , pp. 1163-1172
    • Charrier, V.1    Deutscher, J.2    Martin-Verstraete, I.3
  • 11
    • 0030829511 scopus 로고    scopus 로고
    • BglF, the sensor of the E. coli bgl system, uses the same site to phosphorylate both a sugar and a regulatory protein
    • Chen Q, Arents JC, Bader R, Postma PW, Amster-Choder O (1997a) BglF, the sensor of the E. coli bgl system, uses the same site to phosphorylate both a sugar and a regulatory protein. EMBO J 16:4617-4627
    • (1997) EMBO J , vol.16 , pp. 4617-4627
    • Chen, Q.1    Arents, J.C.2    Bader, R.3    Postma, P.W.4    Amster-Choder, O.5
  • 12
    • 0030839958 scopus 로고
    • The localization of the phosphorylation site of BglG, the response regulator of the Escherichia coli bgl sensory system
    • Chen Q, Engelberg-Kulka H, Amster-Choder O (1947b) The localization of the phosphorylation site of BglG, the response regulator of the Escherichia coli bgl sensory system. J Biol Chem 272:17263-17268
    • (1947) J Biol Chem , vol.272 , pp. 17263-17268
    • Chen, Q.1    Engelberg-Kulka, H.2    Amster-Choder, O.3
  • 13
    • 0025128602 scopus 로고
    • Induction of levansucrase in Bacillus subtilis: An antitermination mechanism negatively controlled by the phosphotransferase system
    • Crutz AM, Steinmetz M, Aymerich S, Richter R, Le Coq D (1990) Induction of levansucrase in Bacillus subtilis: an antitermination mechanism negatively controlled by the phosphotransferase system. J Bacteriol 172:1043-1050
    • (1990) J Bacteriol , vol.172 , pp. 1043-1050
    • Crutz, A.M.1    Steinmetz, M.2    Aymerich, S.3    Richter, R.4    Le Coq, D.5
  • 14
    • 0028877211 scopus 로고
    • Contributions of XylR, CcpA and HPr to catabolite repression of the xyl operon in Bacillus subtilis
    • Dahl MK, Hillen W (1995) Contributions of XylR, CcpA and HPr to catabolite repression of the xyl operon in Bacillus subtilis. FEMS Microbiol Lett 132:79-83
    • (1995) FEMS Microbiol Lett , vol.132 , pp. 79-83
    • Dahl, M.K.1    Hillen, W.2
  • 15
    • 0025687504 scopus 로고
    • Regulation of the maltose transport system of Eseheriehia coli by the glucose-specific enzyme III of the phosphoenolpyruvate-sugar phosphotransterase system. Characterization of inducer-exclusion resistant mutants and reconstitution of inducer exclusion in proteoliposomes
    • Dean DA, Reizer J, Nikaido H, Saier MH (1990) Regulation of the maltose transport system of Eseheriehia coli by the glucose-specific enzyme III of the phosphoenolpyruvate-sugar phosphotransterase system. Characterization of inducer-exclusion resistant mutants and reconstitution of inducer exclusion in proteoliposomes. J Biol Chem 265:21005-21010
    • (1990) J Biol Chem , vol.265 , pp. 21005-21010
    • Dean, D.A.1    Reizer, J.2    Nikaido, H.3    Saier, M.H.4
  • 16
    • 0025301224 scopus 로고
    • The sacT gene regulating the sacPA operon in Bacillus subtilis shares strong homology with transcriptional antiterminators
    • Débarbouillé M, Fouet A, Arnaud M, Klier A, Rapoport G (1990) The sacT gene regulating the sacPA operon in Bacillus subtilis shares strong homology with transcriptional antiterminators. J Bacteriol 172:3966-3973
    • (1990) J Bacteriol , vol.172 , pp. 3966-3973
    • Débarbouillé, M.1    Fouet, A.2    Arnaud, M.3    Klier, A.4    Rapoport, G.5
  • 18
    • 0020851355 scopus 로고
    • ATP-dependent protein-kinase catalyzed phosphorylation of a seryl residue in HPr, the phosphoryl carrier protein of the phosphotransferase system in Streptococcus pyogenes
    • Deutscher J, Saier MH (1983) ATP-dependent protein-kinase catalyzed phosphorylation of a seryl residue in HPr, the phosphoryl carrier protein of the phosphotransferase system in Streptococcus pyogenes. Proc Natl Acad Sci USA 80:6790-6794
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 6790-6794
    • Deutscher, J.1    Saier, M.H.2
  • 19
    • 0000659321 scopus 로고
    • Bacterial phosphoenolpyruvate-dependent phosphotransferase system: P-Ser-HPr and its possible regulatory function
    • Deutscher J, Kessler U, Alpert CA, Hengstenberg W (1984) Bacterial phosphoenolpyruvate-dependent phosphotransferase system: P-Ser-HPr and its possible regulatory function. Biochemistry 23:4455-4460
    • (1984) Biochemistry , vol.23 , pp. 4455-4460
    • Deutscher, J.1    Kessler, U.2    Alpert, C.A.3    Hengstenberg, W.4
  • 20
    • 0028364161 scopus 로고
    • Loss of protein kinase-catalyzed phosphorylation of HPr. a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis
    • Deutscher J, Reizer J, Fischer C, Galinier A, Saier MH, Steinmetz M (1994) Loss of protein kinase-catalyzed phosphorylation of HPr. a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis. J Baeteriol 176:3336-3344
    • (1994) J Baeteriol , vol.176 , pp. 3336-3344
    • Deutscher, J.1    Reizer, J.2    Fischer, C.3    Galinier, A.4    Saier, M.H.5    Steinmetz, M.6
  • 21
    • 0028917215 scopus 로고
    • Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in gram-positive bacteria
    • Deutscher J, Küster E, Bergstedt U, Charrier V, Hillen W (1995) Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in gram-positive bacteria. Mol Microbiol 15:1049-1053
    • (1995) Mol Microbiol , vol.15 , pp. 1049-1053
    • Deutscher, J.1    Küster, E.2    Bergstedt, U.3    Charrier, V.4    Hillen, W.5
  • 23
    • 0029745668 scopus 로고    scopus 로고
    • Catabolite repression mediated by the catabolite control protein CcpA in Staphylococcus xylosus
    • Egeter O, Brückner R (1996) Catabolite repression mediated by the catabolite control protein CcpA in Staphylococcus xylosus. Mol Microbiol 21:739-749
    • (1996) Mol Microbiol , vol.21 , pp. 739-749
    • Egeter, O.1    Brückner, R.2
  • 25
    • 0018818715 scopus 로고
    • Fine control of adenylate cyclase by the phosphoenolpyruvate:sugar phosphotransferase systems in Escherichia coli and Salmonella typhimurium
    • Feucht BU, Saier MH (1980) Fine control of adenylate cyclase by the phosphoenolpyruvate:sugar phosphotransferase systems in Escherichia coli and Salmonella typhimurium. J Baeteriol 141:603-610
    • (1980) J Baeteriol , vol.141 , pp. 603-610
    • Feucht, B.U.1    Saier, M.H.2
  • 26
    • 0028827880 scopus 로고
    • Specific recognition of the Bacillus subtilis gnt cis-acting catabolite-responsive element by a protein complex formed between CcpA and seryl-phosphorylated HPr
    • Fujita Y, Miwa Y, Galinier A, Deutscher J (1995) Specific recognition of the Bacillus subtilis gnt cis-acting catabolite-responsive element by a protein complex formed between CcpA and seryl-phosphorylated HPr. Mol Microbiol 17:953-960
    • (1995) Mol Microbiol , vol.17 , pp. 953-960
    • Fujita, Y.1    Miwa, Y.2    Galinier, A.3    Deutscher, J.4
  • 29
    • 0031557402 scopus 로고    scopus 로고
    • Cooperative and non-cooperative DNA binding modes of catabolite control protein CcpA from Bacillus megaterium result from sensing two different signals
    • Gösseringer R, Küster E, Galinier A, Deutscher J, Hillen W (1997) Cooperative and non-cooperative DNA binding modes of catabolite control protein CcpA from Bacillus megaterium result from sensing two different signals. J Mol Biol 266:665-676
    • (1997) J Mol Biol , vol.266 , pp. 665-676
    • Gösseringer, R.1    Küster, E.2    Galinier, A.3    Deutscher, J.4    Hillen, W.5
  • 30
    • 0030057004 scopus 로고    scopus 로고
    • The role of the CcpA transcriptional regulator in carbon metabolism in Bacillus subtilis
    • Henkin TM (1996) The role of the CcpA transcriptional regulator in carbon metabolism in Bacillus subtilis. FEMS Microbiol Lett 135:9-15
    • (1996) FEMS Microbiol Lett , vol.135 , pp. 9-15
    • Henkin, T.M.1
  • 31
    • 0026033650 scopus 로고
    • Catabolite repression of a-amylase gene expression in Bacillus subtilis involves a trans-acting gene product homologous to the Escherichia coli lacI and galR repressors
    • Henkin TM, Grundy FJ, Nicholson WL, Chambliss GH (1991) Catabolite repression of a-amylase gene expression in Bacillus subtilis involves a trans-acting gene product homologous to the Escherichia coli lacI and galR repressors. Mol Microbiol 5:575-584
    • (1991) Mol Microbiol , vol.5 , pp. 575-584
    • Henkin, T.M.1    Grundy, F.J.2    Nicholson, W.L.3    Chambliss, G.H.4
  • 32
    • 0029797221 scopus 로고    scopus 로고
    • Cloning, expression and isolation of the mannitol transport protein from the thermophilic bacterium Bacillus stearothermophilus
    • Henstra SA, Tolner B, ten Hoeve Duurkens RH, Konings WN, Robillard GT (1996) Cloning, expression and isolation of the mannitol transport protein from the thermophilic bacterium Bacillus stearothermophilus. J Bacteriol 178:5586-5591
    • (1996) J Bacteriol , vol.178 , pp. 5586-5591
    • Henstra, S.A.1    Tolner, B.2    Ten Hoeve Duurkens, R.H.3    Konings, W.N.4    Robillard, G.T.5
  • 33
    • 0028907495 scopus 로고
    • Catabolite repression in Bacillus subtilis: A global regulatory mechanism for the gram-positive bacteria?
    • Hueck CJ, Hillen W (1995) Catabolite repression in Bacillus subtilis: a global regulatory mechanism for the gram-positive bacteria? Mol Microbiol 15:395-401
    • (1995) Mol Microbiol , vol.15 , pp. 395-401
    • Hueck, C.J.1    Hillen, W.2
  • 34
    • 0028086366 scopus 로고
    • Analysis of a cis-active sequence mediating catabolite repression in gram-positive bacteria
    • Hueck CJ, Hillen W, Saier MH (1994) Analysis of a cis-active sequence mediating catabolite repression in gram-positive bacteria. Res Microbiol 145:503-518
    • (1994) Res Microbiol , vol.145 , pp. 503-518
    • Hueck, C.J.1    Hillen, W.2    Saier, M.H.3
  • 35
    • 0029113013 scopus 로고
    • Cloning, expression and functional analyses of the catabolite control protein CcpA from Bacillus megaterium
    • Hueck CJ, Kraus A, Schmiedel D, Hillen W (1995) Cloning, expression and functional analyses of the catabolite control protein CcpA from Bacillus megaterium. Mol Microbiol 16:855-864
    • (1995) Mol Microbiol , vol.16 , pp. 855-864
    • Hueck, C.J.1    Kraus, A.2    Schmiedel, D.3    Hillen, W.4
  • 36
    • 0031912636 scopus 로고    scopus 로고
    • SacY, a transcriptional antiterminator from Bacillus subtilis, is regulated by phosphorylation in vivo
    • Idelson M, Amster-Choder O (1998) SacY, a transcriptional antiterminator from Bacillus subtilis, is regulated by phosphorylation in vivo. J Bacteriol 180:660-666
    • (1998) J Bacteriol , vol.180 , pp. 660-666
    • Idelson, M.1    Amster-Choder, O.2
  • 37
    • 0030089476 scopus 로고    scopus 로고
    • Mechanism responsible for glucose-lactose diauxie in Escherichia coli: Challenge to the cAMP model
    • Inada T, Kimata K, Aiba H (1996) Mechanism responsible for glucose-lactose diauxie in Escherichia coli: challenge to the cAMP model. Genes Cells 1:293-301
    • (1996) Genes Cells , vol.1 , pp. 293-301
    • Inada, T.1    Kimata, K.2    Aiba, H.3
  • 38
    • 0025953332 scopus 로고
    • Catabolite repression of the operon for xylose utilization from Bacillus subtilis W23 is mediated at the level of transcription and depends on a cis site in the xylA reading frame
    • Jacob S, Allmansberger R, Gärtner D, Hillen W (1991) Catabolite repression of the operon for xylose utilization from Bacillus subtilis W23 is mediated at the level of transcription and depends on a cis site in the xylA reading frame. Mol Gen Genet 229:189-196
    • (1991) Mol Gen Genet , vol.229 , pp. 189-196
    • Jacob, S.1    Allmansberger, R.2    Gärtner, D.3    Hillen, W.4
  • 39
    • 0030725260 scopus 로고    scopus 로고
    • Binding of the catabolite repressor protein CcpA to its DNA target is regulated by phosphorylation of its corepressor HPr
    • Jones BE, Dossonnet V, Küster E, Hillen W, Deutscher J, Klevit RE (1997) Binding of the catabolite repressor protein CcpA to its DNA target is regulated by phosphorylation of its corepressor HPr. J Biol Chem 272:26530-26535
    • (1997) J Biol Chem , vol.272 , pp. 26530-26535
    • Jones, B.E.1    Dossonnet, V.2    Küster, E.3    Hillen, W.4    Deutscher, J.5    Klevit, R.E.6
  • 40
    • 0030904521 scopus 로고    scopus 로고
    • Pathogenicity island sequences of pyelonephritogenic Escherichia coli CFT073 are associated with virulent uropathogenic strains
    • Kao JS, Stucker DM, Warren JW, Mobley HLT (1997) Pathogenicity island sequences of pyelonephritogenic Escherichia coli CFT073 are associated with virulent uropathogenic strains. Infect Immun 65:2812-2820
    • (1997) Infect Immun , vol.65 , pp. 2812-2820
    • Kao, J.S.1    Stucker, D.M.2    Warren, J.W.3    Mobley, H.L.T.4
  • 41
    • 0030798006 scopus 로고    scopus 로고
    • Contacts between Bacillus subtilis catabolite regulatory protein CcpA and amyO target site
    • Kim JH, Chambliss GH (1997) Contacts between Bacillus subtilis catabolite regulatory protein CcpA and amyO target site. Nucleic Acids Res 25:3490-3496
    • (1997) Nucleic Acids Res , vol.25 , pp. 3490-3496
    • Kim, J.H.1    Chambliss, G.H.2
  • 42
    • 0029092003 scopus 로고
    • Specificity of DNA binding activity of the Bacillus subtilis catabolite control protein CcpA
    • Kim JH, Guvener ZT, Cho JY, Chung KC, Chambliss GH (1995) Specificity of DNA binding activity of the Bacillus subtilis catabolite control protein CcpA. J Bacteriol 177:5129-5134
    • (1995) J Bacteriol , vol.177 , pp. 5129-5134
    • Kim, J.H.1    Guvener, Z.T.2    Cho, J.Y.3    Chung, K.C.4    Chambliss, G.H.5
  • 43
    • 0032483005 scopus 로고    scopus 로고
    • NADP, corepressor for the Bacillus subtilis catabolite control protein CcpA
    • Kim JH, Voskuil MI, Chambliss GH (1998) NADP, corepressor for the Bacillus subtilis catabolite control protein CcpA. Proc Natl Acad Sci USA 95:9590-9595
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9590-9595
    • Kim, J.H.1    Voskuil, M.I.2    Chambliss, G.H.3
  • 44
    • 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, 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
  • 45
    • 0028264818 scopus 로고
    • Catabolite repression of the Bacillus subtilis xyl operon involves a cis element functional in the context of an unrelated sequence, and glucose exerts additional xylR-dependent repression
    • Kraus A, Hueck C, Gärtner D, Hillen W (1994) Catabolite repression of the Bacillus subtilis xyl operon involves a cis element functional in the context of an unrelated sequence, and glucose exerts additional xylR-dependent repression. J Bacteriol 176:1738-1745
    • (1994) J Bacteriol , vol.176 , pp. 1738-1745
    • Kraus, A.1    Hueck, C.2    Gärtner, D.3    Hillen, W.4
  • 46
    • 0029619251 scopus 로고
    • Regulation of the putative bglPH operon for aryl-β-glucoside utilization in Bacillus subtilis
    • Krüger S, Hecker M (1995) Regulation of the putative bglPH operon for aryl-β-glucoside utilization in Bacillus subtilis. J Bacteriol 177:5590-5597
    • (1995) J Bacteriol , vol.177 , pp. 5590-5597
    • Krüger, S.1    Hecker, M.2
  • 47
    • 0029916568 scopus 로고    scopus 로고
    • Transcriptional analysis of bglPH expression in Bacillus subtilis: Evidence for two distinct pathways mediating carbon catabolite repression
    • Krüger S, Gertz S, Hecker M (1996) Transcriptional analysis of bglPH expression in Bacillus subtilis: Evidence for two distinct pathways mediating carbon catabolite repression. J Bacteriol 178:2637-2644
    • (1996) J Bacteriol , vol.178 , pp. 2637-2644
    • Krüger, S.1    Gertz, S.2    Hecker, M.3
  • 48
    • 0027365675 scopus 로고
    • Catabolite repression of β-glucanase synthesis in Bacillus subtilis
    • Krüger S, Stülke J, Hecker M (1993) Catabolite repression of β-glucanase synthesis in Bacillus subtilis. J Gen Microbiol 139:2047-2054
    • (1993) J Gen Microbiol , vol.139 , pp. 2047-2054
    • Krüger, S.1    Stülke, J.2    Hecker, M.3
  • 49
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the gram-positive bacterium Bacillus subtilis
    • Kunst F, Ogasawara N, Moszer I, Albertini AM, Alloni G, Azevedo V, et al (1997) The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature 390:249-256
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, F.1    Ogasawara, N.2    Moszer, I.3    Albertini, A.M.4    Alloni, G.5    Azevedo, V.6
  • 50
    • 0343182993 scopus 로고    scopus 로고
    • Immunological crossreactivity to the catabolite control protein CcpA from Bacillus megaterium is found in many gram-positive bacteria
    • Küster E, Luesink EJ, de Vos WM, Hillen W (1996) Immunological crossreactivity to the catabolite control protein CcpA from Bacillus megaterium is found in many gram-positive bacteria. FEMS Microbiol Lett 139:109-115
    • (1996) FEMS Microbiol Lett , vol.139 , pp. 109-115
    • Küster, E.1    Luesink, E.J.2    De Vos, W.M.3    Hillen, W.4
  • 51
    • 0027366581 scopus 로고
    • Cloning and sequencing of a cellobiose phosphotransferase operon from Bacillus stearothermophilus XL-65-6 and functional expression in Escherichia coli
    • Lai X, Ingram LO (1993) Cloning and sequencing of a cellobiose phosphotransferase operon from Bacillus stearothermophilus XL-65-6 and functional expression in Escherichia coli. J Bacteriol 175:6441-6450
    • (1993) J Bacteriol , vol.175 , pp. 6441-6450
    • Lai, X.1    Ingram, L.O.2
  • 52
    • 0028986940 scopus 로고
    • New β-glucoside (bgl) genes in Bacillus subtilis: The bglP gene product has both transport and regulatory functions, similar to those of BglF, its Escherichia coli homolog
    • Le Coq D, Lindner C, Krüger S, Steinmetz M, Stülke J (1995) New β-glucoside (bgl) genes in Bacillus subtilis: the bglP gene product has both transport and regulatory functions, similar to those of BglF, its Escherichia coli homolog. J Bacteriol 177:1527-1535
    • (1995) J Bacteriol , vol.177 , pp. 1527-1535
    • Le Coq, D.1    Lindner, C.2    Krüger, S.3    Steinmetz, M.4    Stülke, J.5
  • 53
    • 0028330705 scopus 로고
    • Regulation of xylanolytic enzymes in Bacillus subtilis
    • Lindner C, Stülke J, Hecker M (1994) Regulation of xylanolytic enzymes in Bacillus subtilis. Microbiology 140:753-757
    • (1994) Microbiology , vol.140 , pp. 753-757
    • Lindner, C.1    Stülke, J.2    Hecker, M.3
  • 55
    • 0030746108 scopus 로고    scopus 로고
    • From genetic to structural characterization of a new class of RNA-binding domain within the SacY/BglG family of antiterminator proteins
    • Manival X, Yang Y, Strub MP, Kochoyan M, Steinmetz M, Aymerich S (1997) From genetic to structural characterization of a new class of RNA-binding domain within the SacY/BglG family of antiterminator proteins. EMBO J 16:5019-5029
    • (1997) EMBO J , vol.16 , pp. 5019-5029
    • Manival, X.1    Yang, Y.2    Strub, M.P.3    Kochoyan, M.4    Steinmetz, M.5    Aymerich, S.6
  • 57
    • 0024523666 scopus 로고
    • Induction and metabolite regulation of levanase synthesis in Bacillus subtilis
    • Martin I, Débarbouillé M, Klier A Rapoport G (1989) Induction and metabolite regulation of levanase synthesis in Bacillus subtilis. J Bacteriol 171:1885-1892
    • (1989) J Bacteriol , vol.171 , pp. 1885-1892
    • Martin, I.1    Débarbouillé, M.2    Klier, A.3    Rapoport, G.4
  • 58
    • 0028038196 scopus 로고
    • Interactions of wild-type and truncated LevR of Bacillus subtilis with the upstream activating sequence of the levanase operon
    • Martin-Verstracte I, Débarbouillé M, Klier A Rapoport G (1994) Interactions of wild-type and truncated LevR of Bacillus subtilis with the upstream activating sequence of the levanase operon. J Mol Biol 241:178-192
    • (1994) J Mol Biol , vol.241 , pp. 178-192
    • Martin-Verstracte, I.1    Débarbouillé, M.2    Klier, A.3    Rapoport, G.4
  • 59
    • 0028859554 scopus 로고
    • Two different mechanisms mediate catabolite repression of the Bacillus subtilis levanase operon
    • Martin-Verstraete I, Stülke J, Klier A, Rapoport G (1995) Two different mechanisms mediate catabolite repression of the Bacillus subtilis levanase operon. J Bacteriol 177:6919-6927
    • (1995) J Bacteriol , vol.177 , pp. 6919-6927
    • Martin-Verstraete, I.1    Stülke, J.2    Klier, A.3    Rapoport, G.4
  • 61
    • 0027213246 scopus 로고
    • Promoter-independent catabolite repression of the Bacillus subtilis gnt operon
    • Tokyo
    • Miwa Y, Fujita Y (1993) Promoter-independent catabolite repression of the Bacillus subtilis gnt operon. J Biochem (Tokyo) 113:665-671
    • (1993) J Biochem , vol.113 , pp. 665-671
    • Miwa, Y.1    Fujita, Y.2
  • 62
    • 0030660143 scopus 로고    scopus 로고
    • Catabolite repression in Lactobacillus casei ATCC 393 is mediated by CcpA
    • Monedero V, Gosalbes MJ, Perez-Martinez G (1997) Catabolite repression in Lactobacillus casei ATCC 393 is mediated by CcpA. J Bacteriol 179:6657-6664
    • (1997) J Bacteriol , vol.179 , pp. 6657-6664
    • Monedero, V.1    Gosalbes, M.J.2    Perez-Martinez, G.3
  • 63
    • 0023579076 scopus 로고
    • Catabolite-repression resistant mutations of the Bacillus subtilis alpha amylase promoter affect transcription levels and are in an operator-like sequence
    • Nicholson WL, Park YK, Henkin TM, Won M, Weickert MJ, Gaskell JA, Chambliss GH (1987) Catabolite-repression resistant mutations of the Bacillus subtilis alpha amylase promoter affect transcription levels and are in an operator-like sequence. J Mol Biol 198:609-618
    • (1987) J Mol Biol , vol.198 , pp. 609-618
    • Nicholson, W.L.1    Park, Y.K.2    Henkin, T.M.3    Won, M.4    Weickert, M.J.5    Gaskell, J.A.6    Chambliss, G.H.7
  • 66
    • 0024572660 scopus 로고
    • Lactose transport system of Streptococcus thermophilus: A hybrid protein with homology to the melibiose carrier and enzyme III of the phosphoenolpyruvate-dependent phosphotransferase systems
    • Poolman B, Rover TJ, Mainzer SE, Schmidt BF (1989) Lactose transport system of Streptococcus thermophilus: a hybrid protein with homology to the melibiose carrier and enzyme III of the phosphoenolpyruvate-dependent phosphotransferase systems. J Bacteriol 171:244-253
    • (1989) J Bacteriol , vol.171 , pp. 244-253
    • Poolman, B.1    Rover, T.J.2    Mainzer, S.E.3    Schmidt, B.F.4
  • 67
    • 0026802129 scopus 로고
    • Lactose transport system of Streptococcus thermophilus: The role of histidine residues
    • Poolman B, Modderman R, Reizer J (1992) Lactose transport system of Streptococcus thermophilus: The role of histidine residues. J Biol Chem 267:9150-9157
    • (1992) J Biol Chem , vol.267 , pp. 9150-9157
    • Poolman, B.1    Modderman, R.2    Reizer, J.3
  • 69
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria
    • Postma PW, Lengeler JW, Jacobson GR (1993) Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. Microbiol Rev 57:543-594
    • (1993) Microbiol Rev , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 70
    • 0025946735 scopus 로고
    • Identification and characterization of two Alcaligenes eutrophus gene loci relevant to the poly(β-hydroxybutyric acid)-leaky phenotype which exhibit homology to ptsH and ptsI of Escherichia coli
    • Pries A, Priefert H, Krüger N, Steinbüchel A (1991) Identification and characterization of two Alcaligenes eutrophus gene loci relevant to the poly(β-hydroxybutyric acid)-leaky phenotype which exhibit homology to ptsH and ptsI of Escherichia coli. J Bacteriol 173:5843-5853
    • (1991) J Bacteriol , vol.173 , pp. 5843-5853
    • Pries, A.1    Priefert, H.2    Krüger, N.3    Steinbüchel, A.4
  • 71
    • 0031912637 scopus 로고    scopus 로고
    • Glc of the phosphoenolpyruvate:sugar phosphotransferase system
    • Glc of the phosphoenolpyruvate:sugar phosphotransferase system. J Bacteriol 180:732-736
    • (1998) J Bacteriol , vol.180 , pp. 732-736
    • Reddy, P.1    Kamireddi, M.2
  • 72
    • 0021278017 scopus 로고
    • Regulation of glycerol uptake by the phosphoenolpyruvate-sugar phosphotransferase system m Bacillus subtilis
    • Reizer J, Novotny MJ, Stuiver I, Saier MH (1984) Regulation of glycerol uptake by the phosphoenolpyruvate-sugar phosphotransferase system m Bacillus subtilis. J Bacteriol 159:243-250
    • (1984) J Bacteriol , vol.159 , pp. 243-250
    • Reizer, J.1    Novotny, M.J.2    Stuiver, I.3    Saier, M.H.4
  • 73
    • 0027419642 scopus 로고
    • Sequence analyses and evolutionary relationships among the energy-coupling proteins Enzyme I and HPr of the bacterial phosphoenolpyruvate:sugar phosphotransferase system
    • Reizer J, Hoischen C, Reizer A, Pham TN, Saier MH (1993) Sequence analyses and evolutionary relationships among the energy-coupling proteins Enzyme I and HPr of the bacterial phosphoenolpyruvate:sugar phosphotransferase system. Protein Sci 2:506-521
    • (1993) Protein Sci , vol.2 , pp. 506-521
    • Reizer, J.1    Hoischen, C.2    Reizer, A.3    Pham, T.N.4    Saier, M.H.5
  • 75
    • 0031029049 scopus 로고    scopus 로고
    • Antitermination of transcription of catabolic operons
    • Rutberg B (1997) Antitermination of transcription of catabolic operons. Mol Microbiol 23:413-421
    • (1997) Mol Microbiol , vol.23 , pp. 413-421
    • Rutberg, B.1
  • 76
    • 0023665338 scopus 로고
    • Sugar transport by the bacterial phosphotransferase system. Molecular cloning and structural analysis of the Escherichia coli ptsH, ptsI, and crr genes
    • Saffen DW, Presper KA, Doering TL, Roseman S (1987) Sugar transport by the bacterial phosphotransferase system. Molecular cloning and structural analysis of the Escherichia coli ptsH, ptsI, and crr genes. J Biol Chem 262:16241-16253
    • (1987) J Biol Chem , vol.262 , pp. 16241-16253
    • Saffen, D.W.1    Presper, K.A.2    Doering, T.L.3    Roseman, S.4
  • 77
    • 0024554141 scopus 로고
    • Protein phosphorylation and allosteric control of inducer exclusion and catabolite repression by the bacterial phosphoenolpyruvate:sugar phosphotransferase system
    • Saier, MH (1989) Protein phosphorylation and allosteric control of inducer exclusion and catabolite repression by the bacterial phosphoenolpyruvate:sugar phosphotransferase system. Microbiol Rev 53:109-120
    • (1989) Microbiol Rev , vol.53 , pp. 109-120
    • Saier, M.H.1
  • 78
    • 0026546539 scopus 로고
    • Proposed uniform nomenclature for the proteins and protein domains of the bacterial phospoenolpyruvate:sugar phosphotransterase system
    • Saier MH, Reizer J (1992) Proposed uniform nomenclature for the proteins and protein domains of the bacterial phospoenolpyruvate:sugar phosphotransterase system. J Bacteriol 174:1433-1438.
    • (1992) J Bacteriol , vol.174 , pp. 1433-1438
    • Saier, M.H.1    Reizer, J.2
  • 79
    • 0021030406 scopus 로고
    • Glc of the phosphotransferase system) to the lactose and melibiose permeases in Escherichia coli and Salmonella typhimurium
    • Glc of the phosphotransferase system) to the lactose and melibiose permeases in Escherichia coli and Salmonella typhimurium. J Bacteriol 155:1351-1357
    • (1983) J Bacteriol , vol.155 , pp. 1351-1357
    • Saier, M.H.1    Novotny, M.J.2    Comeau-Fuhrmann, D.3    Osumi, T.4    Desai, J.D.5
  • 80
    • 0029981992 scopus 로고    scopus 로고
    • Contributions of XyIR, CcpA and cre to diauxic growth of Bacillus megaterium and to xylose isomerase expression in the presence of glucose and xylose
    • Schmiedel D, Hilien W (1996) Contributions of XyIR, CcpA and cre to diauxic growth of Bacillus megaterium and to xylose isomerase expression in the presence of glucose and xylose. Mol Gen Genet 250:259-266
    • (1996) Mol Gen Genet , vol.250 , pp. 259-266
    • Schmiedel, D.1    Hilien, W.2
  • 81
    • 0030724011 scopus 로고    scopus 로고
    • High affinity binding and allosteric regulation of Escherichia coli glycogen phosphorylase by the histidine phosphocarrier protein
    • Seok YJ, Sondej M, Badawi P, Lewis MS, Briggs MC, Jaffe Y, Peterkofsky A (1997) High affinity binding and allosteric regulation of Escherichia coli glycogen phosphorylase by the histidine phosphocarrier protein. HPr. J Biol Chem 272:26511-26521
    • (1997) HPr. J Biol Chem , vol.272 , pp. 26511-26521
    • Seok, Y.J.1    Sondej, M.2    Badawi, P.3    Lewis, M.S.4    Briggs, M.C.5    Jaffe, Y.6    Peterkofsky, A.7
  • 82
    • 0031922267 scopus 로고    scopus 로고
    • Identification of a homolog of CcpA Catabolite repressor protein in Streptococcus mutans
    • Simpson CL, Russell RRB (1998) Identification of a homolog of CcpA Catabolite repressor protein in Streptococcus mutans. Infect Immun 66:2085-2092
    • (1998) Infect Immun , vol.66 , pp. 2085-2092
    • Simpson, C.L.1    Russell, R.R.B.2
  • 83
    • 0024600959 scopus 로고
    • Induction of saccharolytic enzymes by sucrose in Bacillus subtilis: Evidence for two partially interchangeable regulatory pathways
    • Steinmetz M, Le Coq D, Aymerich S (1989) Induction of saccharolytic enzymes by sucrose in Bacillus subtilis: Evidence for two partially interchangeable regulatory pathways. J Bacteriol 171:1519-1523
    • (1989) J Bacteriol , vol.171 , pp. 1519-1523
    • Steinmetz, M.1    Le Coq, D.2    Aymerich, S.3
  • 85
    • 0028783423 scopus 로고
    • The HPr protein of the phosphotransferase system links induction and catabolite repression of the Bacillus subtilis levanase operon
    • Stülke J, Martin-Verstraete I, Charrier V, Klier A, Deutscher J, Rapoport G (1995) The HPr protein of the phosphotransferase system links induction and catabolite repression of the Bacillus subtilis levanase operon. J Bacteriol 177:6928-6936
    • (1995) J Bacteriol , vol.177 , pp. 6928-6936
    • Stülke, J.1    Martin-Verstraete, I.2    Charrier, V.3    Klier, A.4    Deutscher, J.5    Rapoport, G.6
  • 86
    • 0030742667 scopus 로고    scopus 로고
    • Induction of the Bacillus subtilis ptsHHI operon by glucose is controlled by a novel antiterminator. GlcT
    • Stülke J, Martin-Verstraete I, Zagorec M, Rose M, Klier A, Rapoport G (1997) Induction of the Bacillus subtilis ptsHHI operon by glucose is controlled by a novel antiterminator. GlcT. Mol Microbiol 25:65-78
    • (1997) Mol Microbiol , vol.25 , pp. 65-78
    • Stülke, J.1    Martin-Verstraete, I.2    Zagorec, M.3    Rose, M.4    Klier, A.5    Rapoport, G.6
  • 87
    • 0031808469 scopus 로고    scopus 로고
    • PRD-A protein domain involved in PTS-dependent induction and carbon catabolite repression of catabolic operons in bacteria
    • Stülke J, Arnaud M, Rapoport G, Martin-Verstraete I (1998) PRD-A protein domain involved in PTS-dependent induction and carbon catabolite repression of catabolic operons in bacteria. Mol Microbiol 28:865-874
    • (1998) Mol Microbiol , vol.28 , pp. 865-874
    • Stülke, J.1    Arnaud, M.2    Rapoport, G.3    Martin-Verstraete, I.4
  • 88
    • 0027972706 scopus 로고
    • Regulation of the raffinose permease of Escherichia coli by the glucose-specific IIA of the phosphoenolpyruvate:sugar phosphotransferase system
    • Titgemeyer F, Mason RE, Saier MH (1994) Regulation of the raffinose permease of Escherichia coli by the glucose-specific IIA of the phosphoenolpyruvate:sugar phosphotransferase system. J Bacteriol 176:543-546
    • (1994) J Bacteriol , vol.176 , pp. 543-546
    • Titgemeyer, F.1    Mason, R.E.2    Saier, M.H.3
  • 89
    • 0031032671 scopus 로고    scopus 로고
    • Identification and characterization of a new β-glucoside utilization system in Bacillus subtilis
    • Tobisch S, Glaser P, Krüger S, Hecker M (1997) Identification and characterization of a new β-glucoside utilization system in Bacillus subtilis. J Bacteriol 179:496-506
    • (1997) J Bacteriol , vol.179 , pp. 496-506
    • Tobisch, S.1    Glaser, P.2    Krüger, S.3    Hecker, M.4
  • 90
    • 0030758035 scopus 로고    scopus 로고
    • Multiple phosphorylation of SacY, a Bacillus subtilis antiterminator negatively controlled by the phosphotransferase system
    • Tortosa P, Aymerich S, Lindner C, Saier MM, Reizer J, Le Coq D (1997) Multiple phosphorylation of SacY, a Bacillus subtilis antiterminator negatively controlled by the phosphotransferase system. J Biol Chem 272:17230-17237
    • (1997) J Biol Chem , vol.272 , pp. 17230-17237
    • Tortosa, P.1    Aymerich, S.2    Lindner, C.3    Saier, M.M.4    Reizer, J.5    Le Coq, D.6
  • 91
    • 0030832399 scopus 로고    scopus 로고
    • Crystal structure of a new RNA-binding domain from the antiterminator protein SacY of Bacillus subtilis
    • van Tilbeurgh H, Manival X, Aymerich S, Lhoste JM, Dumas C, Kochoyan M (1997) Crystal structure of a new RNA-binding domain from the antiterminator protein SacY of Bacillus subtilis. EMBO J. 16:5030-5036
    • (1997) EMBO J. , vol.16 , pp. 5030-5036
    • Van Tilbeurgh, H.1    Manival, X.2    Aymerich, S.3    Lhoste, J.M.4    Dumas, C.5    Kochoyan, M.6
  • 92
    • 0029809181 scopus 로고    scopus 로고
    • Significance of HPr in catabolite repression of a-amylase
    • Voskuil MI, Chambliss GH (1996) Significance of HPr in catabolite repression of a-amylase. J Bacteriol 178:7014-7015
    • (1996) J Bacteriol , vol.178 , pp. 7014-7015
    • Voskuil, M.I.1    Chambliss, G.H.2
  • 93
    • 0029065058 scopus 로고
    • Mutations in the glycerol kinase gene restore the ability of a ptsGHI mutant of Bacillus subtilis to grow on glycerol
    • Wehtje C, Beijer L, Nilsson RP, Rutberg B (1995) Mutations in the glycerol kinase gene restore the ability of a ptsGHI mutant of Bacillus subtilis to grow on glycerol. Microbiology 141:1193-1198
    • (1995) Microbiology , vol.141 , pp. 1193-1198
    • Wehtje, C.1    Beijer, L.2    Nilsson, R.P.3    Rutberg, B.4
  • 94
    • 0026724966 scopus 로고
    • A family of bacterial regulators homologous to Gal and Lac repressors
    • Weickert J, Adhya S (1992) A family of bacterial regulators homologous to Gal and Lac repressors. J Biol Chem 267:15869-15874
    • (1992) J Biol Chem , vol.267 , pp. 15869-15874
    • Weickert, J.1    Adhya, S.2
  • 95
    • 0028205413 scopus 로고
    • Calabolite repression of the Bacillus subtilis hut operon requires a cis-acting site located downstream of the transcription initiation site
    • Wray LW, Pettengill FK, Fisher SH (1994) Calabolite repression of the Bacillus subtilis hut operon requires a cis-acting site located downstream of the transcription initiation site. J Bacteriol 176:1894-1902
    • (1994) J Bacteriol , vol.176 , pp. 1894-1902
    • Wray, L.W.1    Pettengill, F.K.2    Fisher, S.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.