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Volumn 31, Issue 2, 1999, Pages 499-510

The gene bglH present in the bgl operon of Escherichia coli, responsible for uptake and fermentation of β-glucosides encodes for a carbohydrate-specific outer membrane porin

Author keywords

[No Author keywords available]

Indexed keywords

ARBUTIN; CARBOHYDRATE; CELLOBIOSE; GLUCOSIDE; MEMBRANE PROTEIN; PORIN; SALICIN;

EID: 0032945051     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1999.01191.x     Document Type: Article
Times cited : (30)

References (45)
  • 1
    • 0032146885 scopus 로고    scopus 로고
    • Study of sugar binding to the sucrose specific ScrY-channel of enteric bacteria using current noise analysis
    • Andersen, C., Cseh, R., Schülein, K., and Benz, R. (1998) Study of sugar binding to the sucrose specific ScrY-channel of enteric bacteria using current noise analysis. J Membr Biol 164: 263-274.
    • (1998) J Membr Biol , vol.164 , pp. 263-274
    • Andersen, C.1    Cseh, R.2    Schülein, K.3    Benz, R.4
  • 2
    • 0028926959 scopus 로고
    • Evaluation of the rate constants of sugar transport through maltoprin (LamB) of Escherichia coli from the sugar-induced current noise
    • Andersen, C., Jordy, M., and Benz, R. (1995) Evaluation of the rate constants of sugar transport through maltoprin (LamB) of Escherichia coli from the sugar-induced current noise. J Gen Physiol 105: 385-401.
    • (1995) J Gen Physiol , vol.105 , pp. 385-401
    • Andersen, C.1    Jordy, M.2    Benz, R.3
  • 3
    • 0000458406 scopus 로고
    • Solute uptake through bacterial outer membranes
    • Hackenbek, R., and Ghuysen, J.-M. (eds). Amsterdam: Elsevier
    • Benz, R. (1994) Solute Uptake through Bacterial Outer Membranes. In: Bacterial Cell Wall. Hackenbek, R., and Ghuysen, J.-M. (eds). pp. 397-423. Amsterdam: Elsevier.
    • (1994) Bacterial Cell Wall , pp. 397-423
    • Benz, R.1
  • 4
    • 0019214630 scopus 로고
    • Determination of ion permeability through the channels made of porins from the outer membrane of Salmonella typhimurium in lipid bilayer membranes
    • Benz, R., Ishii, J., and Nakae, T. (1980) Determination of ion permeability through the channels made of porins from the outer membrane of Salmonella typhimurium in lipid bilayer membranes. J Membr Biol 56: 19-29.
    • (1980) J Membr Biol , vol.56 , pp. 19-29
    • Benz, R.1    Ishii, J.2    Nakae, T.3
  • 5
    • 0018139740 scopus 로고
    • Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli
    • Benz, R., Janko, K., Boos, W., and Läuger, P. (1978) Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli. Biochim Biophys Acta 511: 305-319.
    • (1978) Biochim Biophys Acta , vol.511 , pp. 305-319
    • Benz, R.1    Janko, K.2    Boos, W.3    Läuger, P.4
  • 6
    • 0022515322 scopus 로고
    • Pore formation by LamB of Escherichia coli in lipid bilayer membranes
    • Benz, R., Schmid, A., Nakae, T., and Vos-Scheperkeuter, G.H. (1986) Pore formation by LamB of Escherichia coli in lipid bilayer membranes. J Bacteriol 165: 978-986.
    • (1986) J Bacteriol , vol.165 , pp. 978-986
    • Benz, R.1    Schmid, A.2    Nakae, T.3    Vos-Scheperkeuter, G.H.4
  • 7
    • 0023472905 scopus 로고
    • Mechanism of sugar transport through the sugar-specific LamB channel of Escherichia coli outer membrane
    • Benz, R., Schmid, A., and Vos-Scheperkeuter, G.H. (1987) Mechanism of sugar transport through the sugar-specific LamB channel of Escherichia coli outer membrane. J Membr Biol 100: 12-29.
    • (1987) J Membr Biol , vol.100 , pp. 12-29
    • Benz, R.1    Schmid, A.2    Vos-Scheperkeuter, G.H.3
  • 8
    • 0022254114 scopus 로고
    • Antigenic polymorphism of the LamB-protein among members of the family Enterobacteriaceae
    • Bloch, M., and Desaymard, C. (1985) Antigenic polymorphism of the LamB-protein among members of the family Enterobacteriaceae. J Bacteriol 163: 106-110.
    • (1985) J Bacteriol , vol.163 , pp. 106-110
    • Bloch, M.1    Desaymard, C.2
  • 9
    • 0019856948 scopus 로고
    • Gene sequence of the lambda receptor, an outer membrane protein of Escherichia coli K-12
    • Clement, J.M., and Hofnung, M. (1981) Gene sequence of the lambda receptor, an outer membrane protein of Escherichia coli K-12. Cell 27: 507-514.
    • (1981) Cell , vol.27 , pp. 507-514
    • Clement, J.M.1    Hofnung, M.2
  • 10
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., Haeberli, P., and Smithies, O. (1984) A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 12: 387-395.
    • (1984) Nucleic Acids Res , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 11
    • 0027237091 scopus 로고
    • Molecular cloning and nucleotide sequence analysis of the maltose-inducible porin gene of Aeromonas salmonicida
    • Dodsworth, S.J., Bennett, A.J., and Coleman, G. (1993) Molecular cloning and nucleotide sequence analysis of the maltose-inducible porin gene of Aeromonas salmonicida. FEMS Microbiol Lett 112: 191-197.
    • (1993) FEMS Microbiol Lett , vol.112 , pp. 191-197
    • Dodsworth, S.J.1    Bennett, A.J.2    Coleman, G.3
  • 12
    • 0029644059 scopus 로고    scopus 로고
    • Crystal structures of various malto-oligosaccharides bound to maltoporin reveal a specific sugar translocation pathway
    • Dutzler, R., Wang, Y.F., Rizkallah, P.J., Rosenbusch, J.P., and Schirmer, T. (1996) Crystal structures of various malto-oligosaccharides bound to maltoporin reveal a specific sugar translocation pathway. Structure 4: 127-134.
    • (1996) Structure , vol.4 , pp. 127-134
    • Dutzler, R.1    Wang, Y.F.2    Rizkallah, P.J.3    Rosenbusch, J.P.4    Schirmer, T.5
  • 13
    • 0026599181 scopus 로고
    • Nucleotide sequences of the arb genes, which control beta-glucoside utilization in Erwinia chrysanthemi: Comparison with the Escherichia coli bgl operon and evidence for a new beta-glycohydrolase family including enzymes from eubacteria, archeabacteria, and humans
    • El Hassouni, M., Henrissat, B., Chippaux, M., and Barras, F. (1992) Nucleotide sequences of the arb genes, which control beta-glucoside utilization in Erwinia chrysanthemi: comparison with the Escherichia coli bgl operon and evidence for a new beta-glycohydrolase family including enzymes from eubacteria, archeabacteria, and humans. J Bacteriol 174: 765-777.
    • (1992) J Bacteriol , vol.174 , pp. 765-777
    • El Hassouni, M.1    Henrissat, B.2    Chippaux, M.3    Barras, F.4
  • 14
    • 0027471832 scopus 로고
    • Crystallization and preliminary X-ray analysis of ScrY, a specific bacterial outer membrane porin
    • Forst, D., Schülein, K., Wacker, T., Kreutz, W., Benz, R., and Welte, W. (1993) Crystallization and preliminary X-ray analysis of ScrY, a specific bacterial outer membrane porin. J Mol Biol 229: 258-262.
    • (1993) J Mol Biol , vol.229 , pp. 258-262
    • Forst, D.1    Schülein, K.2    Wacker, T.3    Kreutz, W.4    Benz, R.5    Welte, W.6
  • 15
    • 0031985785 scopus 로고    scopus 로고
    • Structure of ScrY, the sucrose-specific porin from Salmonella typhimurium, and its complex with sucrose at 2.4 Å resolution
    • Forst, D., Welte, W., Wacker, T., and Diederichs, K. (1998) Structure of ScrY, the sucrose-specific porin from Salmonella typhimurium, and its complex with sucrose at 2.4 Å resolution. Nature Struct Biol 5: 37-46.
    • (1998) Nature Struct Biol , vol.5 , pp. 37-46
    • Forst, D.1    Welte, W.2    Wacker, T.3    Diederichs, K.4
  • 16
    • 0025635842 scopus 로고
    • The maltoporin of Salmonella typhimurium: Sequence and folding model
    • Francoz, E., Molla, A., Saurin, W., and Hofnung, M. (1990) The maltoporin of Salmonella typhimurium: sequence and folding model. Res Microbiol 141: 1039-1059.
    • (1990) Res Microbiol , vol.141 , pp. 1039-1059
    • Francoz, E.1    Molla, A.2    Saurin, W.3    Hofnung, M.4
  • 17
    • 0026086020 scopus 로고
    • Plasmid-mediated sucrose metabolism in Escherichia coli: Characterization of scrY, the structural gene for a phosphoenolpyruvate-dependent sucrose phosphotransferase system outer membrane porin
    • Hardesty, C., Ferran, C., and DiRienzo, J.M. (1991) Plasmid-mediated sucrose metabolism in Escherichia coli: characterization of scrY, the structural gene for a phosphoenolpyruvate-dependent sucrose phosphotransferase system outer membrane porin. J Bacteriol 173: 449-456.
    • (1991) J Bacteriol , vol.173 , pp. 449-456
    • Hardesty, C.1    Ferran, C.2    DiRienzo, J.M.3
  • 18
    • 0026495003 scopus 로고
    • Purification of Aeromonas hydrophila major outer membrane protein: N-terminal sequence analysis and channel-forming properties
    • Jeanteur, D., Gletsu, N., Pattus, F., and Buckley, J.T. (1992) Purification of Aeromonas hydrophila major outer membrane protein: N-terminal sequence analysis and channel-forming properties. Mol Microbiol 6: 3355-3362.
    • (1992) Mol Microbiol , vol.6 , pp. 3355-3362
    • Jeanteur, D.1    Gletsu, N.2    Pattus, F.3    Buckley, J.T.4
  • 19
    • 0030596521 scopus 로고    scopus 로고
    • Rate constants of sugar transport through two lamB mutants of Escherichia coli: Comparison to wild-type maltoporin and to LamB of Salmonella typhimurium
    • Jordy, M., Andersen, C., Schülein, K., Ferenci, T., and Benz, R. (1996) Rate constants of sugar transport through two lamB mutants of Escherichia coli: comparison to wild-type maltoporin and to LamB of Salmonella typhimurium. J Mol Biol 259: 666-678.
    • (1996) J Mol Biol , vol.259 , pp. 666-678
    • Jordy, M.1    Andersen, C.2    Schülein, K.3    Ferenci, T.4    Benz, R.5
  • 20
    • 0023669069 scopus 로고
    • The physical map of the whole E. coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic library
    • Kohara, Y., Akiyama, K., and Isono, K. (1987) The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell 50: 495-508.
    • (1987) Cell , vol.50 , pp. 495-508
    • Kohara, Y.1    Akiyama, K.2    Isono, K.3
  • 21
    • 0028930485 scopus 로고
    • Sequence alignment and structural modelling of the LamB glycoporin family
    • Lang, H.A., and Ferenci, T. (1995) Sequence alignment and structural modelling of the LamB glycoporin family. Biochem Biophys Res Commun 208: 927-934.
    • (1995) Biochem Biophys Res Commun , vol.208 , pp. 927-934
    • Lang, H.A.1    Ferenci, T.2
  • 22
    • 0027370018 scopus 로고
    • The ompS gene of Vibrio cholerae encodes a growth-phase-dependent maltoporin
    • Lang, H.A., and Palva, E.T. (1993) The ompS gene of Vibrio cholerae encodes a growth-phase-dependent maltoporin. Mol Microbiol 10: 891-901.
    • (1993) Mol Microbiol , vol.10 , pp. 891-901
    • Lang, H.A.1    Palva, E.T.2
  • 23
    • 0009551491 scopus 로고
    • Specificity of diffusion channels produced by lambda-phage receptor protein of Escherichia coli
    • Luckey, M., and Nikaido, H. (1980) Specificity of diffusion channels produced by lambda-phage receptor protein of Escherichia coli. Proc Natl Acad Sci USA 77: 165-171.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 165-171
    • Luckey, M.1    Nikaido, H.2
  • 24
    • 0023852792 scopus 로고
    • Pore-forming activity of Tsx protein from the outer membrane of Escherichia coli. Demonstration of a nucleoside-specific binding site
    • Maier, C., Bremer, E., Schmid, A., and Benz, R. (1988) Pore-forming activity of Tsx protein from the outer membrane of Escherichia coli. Demonstration of a nucleoside-specific binding site. J Biol Chem 263: 2493-2499.
    • (1988) J Biol Chem , vol.263 , pp. 2493-2499
    • Maier, C.1    Bremer, E.2    Schmid, A.3    Benz, R.4
  • 25
    • 0031557404 scopus 로고    scopus 로고
    • Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside
    • Meyer, J.E.W., Hofnung, M., and Schulz, G.E. (1997) Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside. J Mol Biol 266: 761-775.
    • (1997) J Mol Biol , vol.266 , pp. 761-775
    • Meyer, J.E.W.1    Hofnung, M.2    Schulz, G.E.3
  • 26
    • 0028266944 scopus 로고
    • Noise analysis of ion current through the open and the sugar-induced closed state of the LamB-channel of Escherichia coli outer membrane: Evaluation of the sugar binding kinetics to the channel interior
    • Nekolla, S., Andersen, C., and Benz, R. (1994) Noise analysis of ion current through the open and the sugar-induced closed state of the LamB-channel of Escherichia coli outer membrane: evaluation of the sugar binding kinetics to the channel interior. Biophys J 86: 1388-1397.
    • (1994) Biophys J , vol.86 , pp. 1388-1397
    • Nekolla, S.1    Andersen, C.2    Benz, R.3
  • 27
    • 0026538553 scopus 로고
    • Porins and specific channels of bacterial outer membranes
    • Nikaido, H. (1992) Porins and specific channels of bacterial outer membranes. Mol Microbiol 6: 435-442.
    • (1992) Mol Microbiol , vol.6 , pp. 435-442
    • Nikaido, H.1
  • 28
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido, H., and Vaara, M. (1985) Molecular basis of bacterial outer membrane permeability. Microbiol Rev 49: 1-32.
    • (1985) Microbiol Rev , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 29
    • 0016123587 scopus 로고
    • Regulation of the β-glucoside system in Escherichia coli K-12
    • Prasad, I., and Schaefler, S. (1974) Regulation of the β-glucoside system in Escherichia coli K-12. J Bacteriol 120: 638-650.
    • (1974) J Bacteriol , vol.120 , pp. 638-650
    • Prasad, I.1    Schaefler, S.2
  • 30
    • 0019772965 scopus 로고
    • Insertion of DNA activates the cryptic bgl operon of E. coli K12
    • Reynolds, A.E., and Wright, A. (1981) Insertion of DNA activates the cryptic bgl operon of E. coli K12. Nature 293: 625-629.
    • (1981) Nature , vol.293 , pp. 625-629
    • Reynolds, A.E.1    Wright, A.2
  • 31
    • 0026344024 scopus 로고
    • Purification of glucose-inducible outer membrane protein OprB of Pseudomonas putita and reconstitution of glucose-specific pores
    • Saravolac, E.G., Taylor, N.F., Benz, R., and Hancock, R.E.W. (1991) Purification of glucose-inducible outer membrane protein OprB of Pseudomonas putita and reconstitution of glucose-specific pores. J Bacteriol 173: 4970-4976.
    • (1991) J Bacteriol , vol.173 , pp. 4970-4976
    • Saravolac, E.G.1    Taylor, N.F.2    Benz, R.3    Hancock, R.E.W.4
  • 32
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation maltoporin channels at 3.1 Å resolution
    • Schirmer, T., Keller, T.A., Wang, Y.-F., and Rosenbusch, J.P. (1995) Structural basis for sugar translocation maltoporin channels at 3.1 Å resolution. Science 267: 512-514.
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.-F.3    Rosenbusch, J.P.4
  • 33
    • 0023754638 scopus 로고
    • Plasmid-mediated sucrose metabolism in Escherichia coli K-12: Mapping of the scr genes of pUR400
    • Schmid, K., Ebner, R., Altenbuchner, J., Schmitt, R., and Lengeler, J.W. (1988) Plasmid-mediated sucrose metabolism in Escherichia coli K-12: mapping of the scr genes of pUR400. Mol Microbiol 2: 1-8.
    • (1988) Mol Microbiol , vol.2 , pp. 1-8
    • Schmid, K.1    Ebner, R.2    Altenbuchner, J.3    Schmitt, R.4    Lengeler, J.W.5
  • 34
    • 0025869336 scopus 로고
    • A sugar-specific porin, ScrY, is involved in sucrose uptake in enteric bacteria
    • Schmid, K., Ebner, R., Jahreis, K., Lengeler, J.W., and Titgemeyer, F. (1991) A sugar-specific porin, ScrY, is involved in sucrose uptake in enteric bacteria. Mol Microbiol 5: 941-950.
    • (1991) Mol Microbiol , vol.5 , pp. 941-950
    • Schmid, K.1    Ebner, R.2    Jahreis, K.3    Lengeler, J.W.4    Titgemeyer, F.5
  • 35
    • 0024094602 scopus 로고
    • Regulation of the bgl operon of Escherichia coli by transcriptional antitermination
    • Schnetz, K., and Rak, B. (1988) Regulation of the bgl operon of Escherichia coli by transcriptional antitermination. EMBO J 7: 3271-3277.
    • (1988) EMBO J , vol.7 , pp. 3271-3277
    • Schnetz, K.1    Rak, B.2
  • 36
    • 0025366839 scopus 로고
    • glc, the key element in catabolite control
    • glc, the key element in catabolite control. Proc Natl Acad Sci USA 87: 5074-5078.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5074-5078
    • Schnetz, K.1    Rak, B.2
  • 37
    • 0026502127 scopus 로고
    • IS5: A mobile enhancer of transcription in Escherichia coli
    • Schnetz, K., and Rak, B. (1992) IS5: a mobile enhancer of transcription in Escherichia coli. Proc Natl Acad Sci USA 89: 1244-1248.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 1244-1248
    • Schnetz, K.1    Rak, B.2
  • 38
    • 0025025875 scopus 로고
    • Identification of catalytic residues in the β-glucoside permease of Escherichia coli by site-specific mutagenesis and demonstration of interdomain cross reactivity between the β-glucoside and glucose systems
    • Schnetz, K., Sutrina, S.L., Saier, M.H. Jr and Rak, B. (1990) Identification of catalytic residues in the β-glucoside permease of Escherichia coli by site-specific mutagenesis and demonstration of interdomain cross reactivity between the β-glucoside and glucose systems. J Biol Chem 265: 13464-13471.
    • (1990) J Biol Chem , vol.265 , pp. 13464-13471
    • Schnetz, K.1    Sutrina, S.L.2    Saier M.H., Jr.3    Rak, B.4
  • 39
    • 0023188223 scopus 로고
    • β-glucoside (bgl) operon of Escherichia coli K-12: Nucleotide sequence, genetic organization, and possible evolutionary relationship to regulatory components of two Bacillus subtilis genes
    • Schnetz, K., Toloczyki, C., and Rak, B. (1987) β-Glucoside (bgl) operon of Escherichia coli K-12: nucleotide sequence, genetic organization, and possible evolutionary relationship to regulatory components of two Bacillus subtilis genes. J Bacteriol 169: 2579-2590.
    • (1987) J Bacteriol , vol.169 , pp. 2579-2590
    • Schnetz, K.1    Toloczyki, C.2    Rak, B.3
  • 40
    • 0029087726 scopus 로고
    • The deletion of 70 N-terminal amino acids of the sugar-specific sucrose-porin ScrY causes its functional similarity to LamB in vivo and in vitro
    • Schülein, K., Andersen, C., and Benz, R. (1995) The deletion of 70 N-terminal amino acids of the sugar-specific sucrose-porin ScrY causes its functional similarity to LamB in vivo and in vitro. Mol Microbiol 17: 757-767.
    • (1995) Mol Microbiol , vol.17 , pp. 757-767
    • Schülein, K.1    Andersen, C.2    Benz, R.3
  • 41
    • 0025893079 scopus 로고
    • The sugar specific outer membrane channel ScrY contains functional characteristics of general diffusion pores and substrate-specific porins
    • Schülein, K., Schmid, K., and Benz, R. (1991) The sugar specific outer membrane channel ScrY contains functional characteristics of general diffusion pores and substrate-specific porins. Mol Microbiol 5: 2233-2241.
    • (1991) Mol Microbiol , vol.5 , pp. 2233-2241
    • Schülein, K.1    Schmid, K.2    Benz, R.3
  • 42
    • 0000706936 scopus 로고
    • The maltose regulon
    • Neidhardt, F.C., Ingraham, J.L., Low, K.B., Magasanik, B., Schaechter, M., and Umbarger, H.E. (eds). Washington, DC: American Society for Microbiology Press
    • Schwartz, M. (1987) The maltose regulon. In Escherichia coli and Salmonella typhimurium. Cellular and Molecular Biology. Neidhardt, F.C., Ingraham, J.L., Low, K.B., Magasanik, B., Schaechter, M., and Umbarger, H.E. (eds). Washington, DC: American Society for Microbiology Press.
    • (1987) Escherichia Coli and Salmonella Typhimurium. Cellular and Molecular Biology
    • Schwartz, M.1
  • 43
    • 0022517918 scopus 로고
    • Models for the structure of outer-membrane proteins of Escherichia coli derived from Raman spectroscopy and prediction methods
    • Vogel, H., and Jähnig, F. (1986) Models for the structure of outer-membrane proteins of Escherichia coli derived from Raman spectroscopy and prediction methods. J Mol Biol 190: 191-199.
    • (1986) J Mol Biol , vol.190 , pp. 191-199
    • Vogel, H.1    Jähnig, F.2
  • 44
    • 0013482155 scopus 로고    scopus 로고
    • Identification of a cryptic gene in the Escherichia coli genome and insertion of a monomeric form of the protein into the outer membrane
    • Wang, J., Betton, J.-M., Michel, V., Hofnung, M., and Charbit, A. (1997) Identification of a cryptic gene in the Escherichia coli genome and insertion of a monomeric form of the protein into the outer membrane. Mol Microbiol 23: 2233-2241.
    • (1997) Mol Microbiol , vol.23 , pp. 2233-2241
    • Wang, J.1    Betton, J.-M.2    Michel, V.3    Hofnung, M.4    Charbit, A.5
  • 45
    • 0026628674 scopus 로고
    • DNA sequence analysis of the lamB gene from Klebsiella pneumoniae: Implications for the topology and the pore functions in maltoporin
    • Werts, C., Charbit, A., Bachellier, S., and Hofnung, M. (1992) DNA sequence analysis of the lamB gene from Klebsiella pneumoniae: implications for the topology and the pore functions in maltoporin. Mol Gen Genet 233: 372-378.
    • (1992) Mol Gen Genet , vol.233 , pp. 372-378
    • Werts, C.1    Charbit, A.2    Bachellier, S.3    Hofnung, M.4


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