메뉴 건너뛰기




Volumn 62, Issue 1, 1998, Pages 204-229

Maltose/maltodextrin system of Escherichia coli: Transport, metabolism, and regulation

Author keywords

[No Author keywords available]

Indexed keywords

4ALPHA GLUCANOTRANSFERASE; ABC TRANSPORTER; AMYLASE; CARRIER PROTEIN; GENE PRODUCT; GLUCOKINASE; GLUCOSE; GLUCOSIDASE; GLYCOGEN; MALTODEXTRIN; MALTOSE; MALTOSE BINDING PROTEIN; PHOSPHOGLUCOMUTASE; PHOSPHORYLASE; TREHALOSE;

EID: 0031887807     PISSN: 10922172     EISSN: None     Source Type: Journal    
DOI: 10.1128/mmbr.62.1.204-229.1998     Document Type: Review
Times cited : (531)

References (303)
  • 1
    • 0015146593 scopus 로고
    • Phosphoglucomutase mutants of Escherichia coli K12
    • Adhya, S., and M. Schwartz. 1971. Phosphoglucomutase mutants of Escherichia coli K12. J. Bacteriol. 108:621-626.
    • (1971) J. Bacteriol. , vol.108 , pp. 621-626
    • Adhya, S.1    Schwartz, M.2
  • 2
    • 0024346946 scopus 로고
    • Evidence for the importance of the phosphotransfer between the two regulatory components EnvZ and OmpR in osmoregulation in Escherichia coli
    • Aiba, H., F. Nakasa, S. Mizushima, and T, Mizuno. 1989. Evidence for the importance of the phosphotransfer between the two regulatory components EnvZ and OmpR in osmoregulation in Escherichia coli. J. Biol. Chem. 264:14090-14094.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14090-14094
    • Aiba, H.1    Nakasa, F.2    Mizushima, S.3    Mizuno, T.4
  • 3
    • 0027339573 scopus 로고
    • Transcriptional regulation of the bgl operon of Escherichia coli involves phosphotransferase system-mediated phosphorylation of a transcriptional antiterminator
    • Amster-Choder, O., and A. Wright. 1993. Transcriptional regulation of the bgl operon of Escherichia coli involves phosphotransferase system-mediated phosphorylation of a transcriptional antiterminator. J. Cell. Biochem. 51: 83-90.
    • (1993) J. Cell. Biochem. , vol.51 , pp. 83-90
    • Amster-Choder, O.1    Wright, A.2
  • 4
    • 0020541951 scopus 로고
    • Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli ADP-gfucose synthase as deduced from the nucleotide sequence of the glgC gene
    • Baecker, P. A., C. E. Furlong, and J. Preiss. 1983. Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli ADP-gfucose synthase as deduced from the nucleotide sequence of the glgC gene. J. Biol. Chem. 258:5084-5088.
    • (1983) J. Biol. Chem. , vol.258 , pp. 5084-5088
    • Baecker, P.A.1    Furlong, C.E.2    Preiss, J.3
  • 5
    • 0023025007 scopus 로고
    • Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli 1,4-α-D-glucan:1,4-α-D-glucan 6-α-D-(1,4-α-D-glucano)-transferase as deduced from the nucleotide sequence of the glgB gene
    • Baecker, P. A., E. Greenberg, and J. Preiss. 1986. Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli 1,4-α-D-glucan:1,4-α-D-glucan 6-α-D-(1,4-α-D-glucano)-transferase as deduced from the nucleotide sequence of the glgB gene. J. Biol. Chem. 261:8738-8743.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8738-8743
    • Baecker, P.A.1    Greenberg, E.2    Preiss, J.3
  • 6
    • 0027475808 scopus 로고
    • The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface
    • Baichwal, V., D. X. Liu, and G. F. L. Ames. 1993. The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface. Proc. Natl. Acad. Sci. USA 90:620-624.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 620-624
    • Baichwal, V.1    Liu, D.X.2    Ames, G.F.L.3
  • 7
    • 0019120076 scopus 로고
    • Identification of a cytoplasmic membrane-associated component of the maltose transport system of Escherichia coli
    • Bavoil, P., M. Hofhung, and H. Nikaido. 1980. Identification of a cytoplasmic membrane-associated component of the maltose transport system of Escherichia coli. J. Biol. Chem. 255:8366-8369.
    • (1980) J. Biol. Chem. , vol.255 , pp. 8366-8369
    • Bavoil, P.1    Hofhung, M.2    Nikaido, H.3
  • 8
    • 0028049476 scopus 로고
    • Dissecting differential binding in the forward and reverse reaction of Escherichia coli maitodextrin phosphorylase using 2-deoxyglucosyl substrates
    • Becker, S., D. Palm, and R. Schinzel. 1994. Dissecting differential binding in the forward and reverse reaction of Escherichia coli maitodextrin phosphorylase using 2-deoxyglucosyl substrates. J. Biol. Chem. 269:2485-2490.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2485-2490
    • Becker, S.1    Palm, D.2    Schinzel, R.3
  • 9
    • 0021052441 scopus 로고
    • Mutations in the promoter regions of the malEFG and malK-lamB operons of Escherichia coli K12
    • Bedouelle, H. 1983. Mutations in the promoter regions of the malEFG and malK-lamB operons of Escherichia coli K12. J. Mol. Biol. 170:861-882.
    • (1983) J. Mol. Biol. , vol.170 , pp. 861-882
    • Bedouelle, H.1
  • 10
    • 0020408901 scopus 로고
    • Promoters of the malEFG and malK-lamB operons in Escherichia coli K12
    • Bedoulle, H., U. Schmeissner, M. Hofnung, and M. Rosenberg. 1982. Promoters of the malEFG and malK-lamB operons in Escherichia coli K12. J. Mol. Biol. 161:519-531.
    • (1982) J. Mol. Biol. , vol.161 , pp. 519-531
    • Bedoulle, H.1    Schmeissner, U.2    Hofnung, M.3    Rosenberg, M.4
  • 11
    • 0030612595 scopus 로고    scopus 로고
    • H-1, N-15 and C-13 NMR assignments, secondary structure and overall topology of the Escherichia coli GlgS protein
    • Beglova, N., D. Fischer, R. Hengge-Aronis, and K. Gehring. 1997. H-1, N-15 and C-13 NMR assignments, secondary structure and overall topology of the Escherichia coli GlgS protein. Eur. J. Biochem. 246:301-310.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 301-310
    • Beglova, N.1    Fischer, D.2    Hengge-Aronis, R.3    Gehring, K.4
  • 12
    • 0001353133 scopus 로고
    • Evolution in biosymhetic pathways: Two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region
    • Belfaiza, J., C. Parsot, A. Martel, C. Bouthier de la Tour, D. Margarita, G. N. Cohen, and I. Saint-Girons. 1986. Evolution in biosymhetic pathways: two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region. Proc. Natl. Acad. Sci. USA 83:867-871.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 867-871
    • Belfaiza, J.1    Parsot, C.2    Martel, A.3    Bouthier de la Tour, C.4    Margarita, D.5    Cohen, G.N.6    Saint-Girons, I.7
  • 13
    • 33745466322 scopus 로고
    • Pullulan, ein extracellulãres Glucan von Pultularia pullulans
    • Bender, H., J. Lehmann, and K. Wallenfels. 1959. Pullulan, ein extracellulãres Glucan von Pultularia pullulans. Biochim. Biophys. Acta 36:309-316.
    • (1959) Biochim. Biophys. Acta , vol.36 , pp. 309-316
    • Bender, H.1    Lehmann, J.2    Wallenfels, K.3
  • 14
    • 0002331513 scopus 로고
    • Untersuchungen an Pullulan. II. Spezifischer Abbau durch ein bakterielles
    • Bender, H., and K. Wallenfels. 1961. Untersuchungen an Pullulan. II. Spezifischer Abbau durch ein bakterielles Enzyme Biochem. Z. 334:79-95.
    • (1961) Enzyme Biochem. Z. , vol.334 , pp. 79-95
    • Bender, H.1    Wallenfels, K.2
  • 15
    • 0021951798 scopus 로고
    • Temperature-sensitive catabolite activator protein in Escherichia coli BUG6
    • Benner, D., N. Müller, and W. Boos. 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
  • 16
    • 0026545214 scopus 로고
    • Investigation of the selectivity of maltoporin channels using mutant LamB proteins - Mutations changing the maltodextrin binding site
    • Benz, R., G. Francis, T. Nakae, and T. Ferenci. 1992. Investigation of the selectivity of maltoporin channels using mutant LamB proteins - mutations changing the maltodextrin binding site. Biochim. Biophys. Acta 1104:299-307.
    • (1992) Biochim. Biophys. Acta , vol.1104 , pp. 299-307
    • Benz, R.1    Francis, G.2    Nakae, T.3    Ferenci, T.4
  • 17
    • 0028944087 scopus 로고
    • Mathematical treatment of the kinetics of binding protein dependent transport systems reveals that both the substrate loaded and unloaded binding proteins interact with the membrane components
    • Bohl, E., H. A. Shuman, and W. Boos. 1995. Mathematical treatment of the kinetics of binding protein dependent transport systems reveals that both the substrate loaded and unloaded binding proteins interact with the membrane components. J. Theor. Biol. 172:83-94.
    • (1995) J. Theor. Biol. , vol.172 , pp. 83-94
    • Bohl, E.1    Shuman, H.A.2    Boos, W.3
  • 18
    • 26544469228 scopus 로고    scopus 로고
    • Unpublished observations
    • Böhm, A., and W. Boos. 1997. Unpublished observations.
    • (1997)
    • Böhm, A.1    Boos, W.2
  • 20
    • 0019443117 scopus 로고
    • Formation and excretion of acetylmaltose after accumulation of maltose in Escherichia coli
    • Boos, W., T. Ferenci, and H. A. Shuman. 1981. Formation and excretion of acetylmaltose after accumulation of maltose in Escherichia coli. J. Bacteriol. 146:725-732.
    • (1981) J. Bacteriol. , vol.146 , pp. 725-732
    • Boos, W.1    Ferenci, T.2    Shuman, H.A.3
  • 21
    • 0001769249 scopus 로고    scopus 로고
    • Periplasmic binding protein-dependent ABC transporters
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology. Washington, D.C
    • Boos, W., and J. M. Lucht. 1996. Periplasmic binding protein-dependent ABC transporters, p. 1175-1209. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. American Society for Microbiology. Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , pp. 1175-1209
    • Boos, W.1    Lucht, J.M.2
  • 22
    • 0040384143 scopus 로고    scopus 로고
    • The maltose system of Escherichia coli
    • E. C. C. Lin and A. S. Lynch (ed.), R. G. Landes Co., Austin, Tex.
    • Boos, W., R. Peist, K. Decker, and E. Zdych. 1996. The maltose system of Escherichia coli, p. 201-229. In E. C. C. Lin and A. S. Lynch (ed.), Regulation of gene expression in Escherichia coli. R. G. Landes Co., Austin, Tex.
    • (1996) Regulation of Gene Expression in Escherichia Coli , pp. 201-229
    • Boos, W.1    Peist, R.2    Decker, K.3    Zdych, E.4
  • 23
    • 0030808276 scopus 로고    scopus 로고
    • 6-Phospho-α-glucosidase from Fusobacterium mortiferum: Cloning, expression, and assignment to family 4 of the glucosylhydrolases
    • Bouma, C. L., J. Reizer, A. Reizer, S. A. Robrish, and J. Thomson. 1997. 6-Phospho-α-glucosidase from Fusobacterium mortiferum: cloning, expression, and assignment to family 4 of the glucosylhydrolases. J. Bacteriol. 179:4129-4137.
    • (1997) J. Bacteriol. , vol.179 , pp. 4129-4137
    • Bouma, C.L.1    Reizer, J.2    Reizer, A.3    Robrish, S.A.4    Thomson, J.5
  • 25
    • 0027509460 scopus 로고
    • Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions
    • Boyd, D., B. Traxler, and J. Beckwith. 1993. Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions. J. Bacteriol. 175:553-556.
    • (1993) J. Bacteriol. , vol.175 , pp. 553-556
    • Boyd, D.1    Traxler, B.2    Beckwith, J.3
  • 26
    • 0025900058 scopus 로고
    • Maltose transacetylase of Escherichia coli. Mapping and cloning of its structural gene, mac, and characterization of the enzyme as a dimer of identical polypeptides with a molecular weight of 20.000
    • Brand, B., and W, Boos. 1991. Maltose transacetylase of Escherichia coli. Mapping and cloning of its structural gene, mac, and characterization of the enzyme as a dimer of identical polypeptides with a molecular weight of 20.000. J. Biol. Chem. 266:14113-14118.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14113-14118
    • Brand, B.1    Boos, W.2
  • 27
    • 0021998366 scopus 로고
    • Maltose-binding protein does not modulate the activity of maltoporin as a general porin in Escherichia coli
    • Brass, J. M., K. Bauer, U. Ehmann, and W. Boos. 1985. Maltose-binding protein does not modulate the activity of maltoporin as a general porin in Escherichia coli. J. Bacteriol. 161:720-726.
    • (1985) J. Bacteriol. , vol.161 , pp. 720-726
    • Brass, J.M.1    Bauer, K.2    Ehmann, U.3    Boos, W.4
  • 28
    • 0021866359 scopus 로고
    • Transposable λplac Mu bacteriophages for creating lacZ operon fusions and kanamycin resistance insertions in Escherichia coli
    • Bremer, E., T. J. Silhavy, and J. M. Weinstock. 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
  • 30
    • 0026670148 scopus 로고
    • The glucose transporter of Escherichia coli. Mutants with impaired translocation activity that retain phosphorylation activity
    • Buhr, A., G. A. Daniels, and B. Erni. 1992. The glucose transporter of Escherichia coli. Mutants with impaired translocation activity that retain phosphorylation activity. J. Biol. Chem. 267:3847-3851.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3847-3851
    • Buhr, A.1    Daniels, G.A.2    Erni, B.3
  • 31
    • 0022634521 scopus 로고
    • Osmoregulation of the maltose regulon in Escherichia coli
    • Bukau, B., M. Ehrmann, and W. Boos. 1986. Osmoregulation of the maltose regulon in Escherichia coli. J. Bacteriol. 166:884-891.
    • (1986) J. Bacteriol. , vol.166 , pp. 884-891
    • Bukau, B.1    Ehrmann, M.2    Boos, W.3
  • 32
    • 0028111825 scopus 로고
    • The leucine-responsive regulatory protein, a global regulator of metabolism in Escherichia coli
    • Calvo, J. M., and R. G. Matthews. 1994. The leucine-responsive regulatory protein, a global regulator of metabolism in Escherichia coli. Microbiol. Rev. 58:466-490.
    • (1994) Microbiol. Rev. , vol.58 , pp. 466-490
    • Calvo, J.M.1    Matthews, R.G.2
  • 33
    • 0022652877 scopus 로고
    • Contrasting mechanisms of envZ control of mal and pho regulon genes in Escherichia coli
    • Case, C. C., B. Bukau, S. Granett, M. R. Villarejo, and W. Boos. 1986. Contrasting mechanisms of envZ control of mal and pho regulon genes in Escherichia coli. J. Bacteriol. 166:706-712.
    • (1986) J. Bacteriol. , vol.166 , pp. 706-712
    • Case, C.C.1    Bukau, B.2    Granett, S.3    Villarejo, M.R.4    Boos, W.5
  • 34
    • 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
  • 35
    • 0019902462 scopus 로고
    • Role of the catabolite activator protein in the maltose regulon of Escherichia coli
    • Chapon, C. 1982. Role of the catabolite activator protein in the maltose regulon of Escherichia coli. J. Bacteriol. 150:722-729.
    • (1982) J. Bacteriol. , vol.150 , pp. 722-729
    • Chapon, C.1
  • 36
    • 0021055023 scopus 로고
    • Action of CAP on the malT promoter in vitro
    • Chapon, C., and A. Kolb. 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
  • 37
    • 0027487182 scopus 로고
    • Folding of maltose-binding protein-evidence for the identity of the rate-determining step in vivo and in vitro
    • Chim, S. Y., S. Strobel, P. Bassford, and L. L. Randall. 1993. Folding of maltose-binding protein-evidence for the identity of the rate-determining step in vivo and in vitro. J. Biol. Chem. 268:20855-20862.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20855-20862
    • Chim, S.Y.1    Strobel, S.2    Bassford, P.3    Randall, L.L.4
  • 38
    • 0030595364 scopus 로고    scopus 로고
    • Crystal structure of the pyridoxal-5′-phosphate dependent cystathionine β-lyase from Escherichia coli at 1.83 Å
    • Clausen, T., R. Huber, B. Laber, H.-D. Pohlenz, and A. Messerschmidt. 1996. Crystal structure of the pyridoxal-5′-phosphate dependent cystathionine β-lyase from Escherichia coli at 1.83 Å. J. Mol. Biol. 262:202-224.
    • (1996) J. Mol. Biol. , vol.262 , pp. 202-224
    • Clausen, T.1    Huber, R.2    Laber, B.3    Pohlenz, H.-D.4    Messerschmidt, A.5
  • 39
    • 0019856948 scopus 로고
    • Gene sequence of the lambda receptor, an outer membrane protein of Escherichia coli K-12
    • Clement, J. M., and M. Hofnung. 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
  • 40
    • 0022617696 scopus 로고
    • The nucleotide sequence of the malT gene encoding the positive regulator of the Escherichia coli maltose regulon
    • Cole, S. T., and O. Raibaud. 1986. The nucleotide sequence of the malT gene encoding the positive regulator of the Escherichia coli maltose regulon. Gene 42:201-208.
    • (1986) Gene , vol.42 , pp. 201-208
    • Cole, S.T.1    Raibaud, O.2
  • 41
    • 0028347539 scopus 로고
    • Mutations that alter the transmembrane signalling pathway in an ATP binding cassette (ABC) transporter
    • Covitz, K.M. Y., C. H. Panagiotidis, L. I. Hor, M. Reyes, N. A. Trtptow, and H. A. Shuman. 1994. Mutations that alter the transmembrane signalling pathway in an ATP binding cassette (ABC) transporter. EMBO J. 13:1752-1759.
    • (1994) EMBO J. , vol.13 , pp. 1752-1759
    • Covitz, K.M.Y.1    Panagiotidis, C.H.2    Hor, L.I.3    Reyes, M.4    Trtptow, N.A.5    Shuman, H.A.6
  • 42
    • 0029820371 scopus 로고    scopus 로고
    • Is trehalose special for preserving dry biomaterials?
    • Crowe, L. M., D. S. Reid, and J. H. Crowe. 1996. Is trehalose special for preserving dry biomaterials? Biophys. J. 71:2087-2093.
    • (1996) Biophys. J. , vol.71 , pp. 2087-2093
    • Crowe, L.M.1    Reid, D.S.2    Crowe, J.H.3
  • 43
    • 0016761881 scopus 로고
    • Phosphorylation of D-glucose in Escherichia coli mutants defective in glucophosphotransferase, mannosephosphotransfcrase, and glucokinase
    • Curtis, S. J., and W. Epstein. 1975. Phosphorylation of D-glucose in Escherichia coli mutants defective in glucophosphotransferase, mannosephosphotransfcrase, and glucokinase. J. Bacteriol. 122:1189-1199.
    • (1975) J. Bacteriol. , vol.122 , pp. 1189-1199
    • Curtis, S.J.1    Epstein, W.2
  • 44
    • 0024712936 scopus 로고
    • Comparison of sequences from the malB regions of Salmonella typhimurium and Enterobacter aerogenes with Escherichia coli K12: A potential new regulatory site in the intergenic region
    • Dahl, M. K., E. Francoz, W. Saurin, W. Boos, M. D. Manson, and M. Hofnung. 1989. Comparison of sequences from the malB regions of Salmonella typhimurium and Enterobacter aerogenes with Escherichia coli K12: a potential new regulatory site in the intergenic region. Mol. Gen. Genet. 218:199-207.
    • (1989) Mol. Gen. Genet. , vol.218 , pp. 199-207
    • Dahl, M.K.1    Francoz, E.2    Saurin, W.3    Boos, W.4    Manson, M.D.5    Hofnung, M.6
  • 45
    • 0027429537 scopus 로고
    • On the puzzling arrangement of the asymmetric MalT-bindtng sites in the MalT-dependent promoters
    • Danot, O., and O. Raibaud. 1993. On the puzzling arrangement of the asymmetric MalT-bindtng sites in the MalT-dependent promoters. Proc. Natl. Acad. Sci. USA 90:10999-11003.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10999-11003
    • Danot, O.1    Raibaud, O.2
  • 46
    • 0027943595 scopus 로고
    • Multiple protein-DNA and protein-protein interactions are involved in transcriptional activation by MalT
    • Danot, O., and O. Raibaud. 1994. Multiple protein-DNA and protein-protein interactions are involved in transcriptional activation by MalT. Mol. Microbiol. 14:335-346.
    • (1994) Mol. Microbiol. , vol.14 , pp. 335-346
    • Danot, O.1    Raibaud, O.2
  • 47
    • 0028180703 scopus 로고
    • Which nucleotides in the "-10" region are crucial to obtain a fully active MalT-dependent promoter?
    • Damit, O., and O. Raibaud. 1994. Which nucleotides in the "-10" region are crucial to obtain a fully active MalT-dependent promoter? J. Mol. Biol. 238:643-648.
    • (1994) J. Mol. Biol. , vol.238 , pp. 643-648
    • Damit, O.1    Raibaud, O.2
  • 48
    • 0030582422 scopus 로고    scopus 로고
    • Two amino acid residues from the DNA-binding domain of MalT play a crucial role in transcriptional activation
    • Danot, O., D. Vidal-Ingigliardi, and O. Raibaud. 1996. Two amino acid residues from the DNA-binding domain of MalT play a crucial role in transcriptional activation. J. Mol. Biol. 262:1-11.
    • (1996) J. Mol. Biol. , vol.262 , pp. 1-11
    • Danot, O.1    Vidal-Ingigliardi, D.2    Raibaud, O.3
  • 49
    • 0025325927 scopus 로고
    • Characterization of malT mutants that constitutively activate the maltose regulon of Escherichia coli
    • Dardonville, B., and O. Raibaud. 1990. Characterization of malT mutants that constitutively activate the maltose regulon of Escherichia coli. J. Bacteriol. 172:1846-1852.
    • (1990) J. Bacteriol. , vol.172 , pp. 1846-1852
    • Dardonville, B.1    Raibaud, O.2
  • 50
    • 0027510078 scopus 로고
    • Sequence-function relationships in MalG, an inner membrane protein from the maltose transport system in Escherichia coli
    • Dassa, E. 1993. Sequence-function relationships in MalG, an inner membrane protein from the maltose transport system in Escherichia coli. Mol. Microbiol. 7:39-47.
    • (1993) Mol. Microbiol. , vol.7 , pp. 39-47
    • Dassa, E.1
  • 51
    • 0022125681 scopus 로고
    • Sequence of gene malG in Escherichia coli K12: Homologies between integral membrane components from binding protein-dependent transport systems
    • Dassa, E., and M. Hofnung. 1985. Sequence of gene malG in Escherichia coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 4:2287-2293.
    • (1985) EMBO J. , vol.4 , pp. 2287-2293
    • Dassa, E.1    Hofnung, M.2
  • 52
    • 0027396907 scopus 로고
    • Membrane topology of MalG, an inner membrane protein from the maltose transport system of Escherichia coli
    • Dassa, E., and S. Muir. 1993. Membrane topology of MalG, an inner membrane protein from the maltose transport system of Escherichia coli. Mol. Microbiol. 7:29-38.
    • (1993) Mol. Microbiol. , vol.7 , pp. 29-38
    • Dassa, E.1    Muir, S.2
  • 53
    • 0029868327 scopus 로고    scopus 로고
    • The maltose transport system of Escherichia coli displays positive cooperatively in ATP hydrolysis
    • Davidson, A. L., S. S. Laghaeian, and D. E. Mannering. 1996. The maltose transport system of Escherichia coli displays positive cooperatively in ATP hydrolysis. J. Biol. Chem. 271:4858-4863.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4858-4863
    • Davidson, A.L.1    Laghaeian, S.S.2    Mannering, D.E.3
  • 54
    • 0025214263 scopus 로고
    • Overproduction, solubilization. and reconstitution of the maltose transport system from Escherichia coli
    • Davidson, A. L., and H. Nikaido. 1990. Overproduction, solubilization. and reconstitution of the maltose transport system from Escherichia coli. J. Biol. Chem. 265:4254-4260.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4254-4260
    • Davidson, A.L.1    Nikaido, H.2
  • 55
    • 0025738363 scopus 로고
    • Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli
    • Davidson, A. L., and H. Nikaido. 1991. Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli. J. Biol. Chem. 266:8946-8951.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8946-8951
    • Davidson, A.L.1    Nikaido, H.2
  • 56
    • 0030886132 scopus 로고    scopus 로고
    • Mutation of a single MalK subunit severely impairs maltose transport activity in Escherichia coli
    • Davidson, A. L., and S. Sharma. 1997. Mutation of a single MalK subunit severely impairs maltose transport activity in Escherichia coli. J. Bacteriol. 179:5458-5464.
    • (1997) J. Bacteriol. , vol.179 , pp. 5458-5464
    • Davidson, A.L.1    Sharma, S.2
  • 57
    • 0026549522 scopus 로고
    • Mechanism of maltose transport in Escherichia coli. Transmembrane signaling by periplasmic binding proteins
    • Davidson, A. L., H. A. Shuman, and H. Nikaido. 1992. Mechanism of maltose transport in Escherichia coli. Transmembrane signaling by periplasmic binding proteins. Proc. Natl. Acad. Sci. USA 89:2360-2364.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2360-2364
    • Davidson, A.L.1    Shuman, H.A.2    Nikaido, H.3
  • 58
    • 0025365238 scopus 로고
    • The role of ATP as the energy source for maltose transport in Escherichia coli
    • Dean, D. A., A. L. Davidson, and H. Nikaido. 1990. The role of ATP as the energy source for maltose transport in Escherichia coli. Res. Microbiol. 141:348-352.
    • (1990) Res. Microbiol. , vol.141 , pp. 348-352
    • Dean, D.A.1    Davidson, A.L.2    Nikaido, H.3
  • 59
    • 0026744442 scopus 로고
    • Interaction between maltose-binding protein and the membrane-associated maltose transporter complex in Escherichia coli
    • Dean, D. A., L. I. Hor, H. A. Shuman, and H, Nikaido. 1992. Interaction between maltose-binding protein and the membrane-associated maltose transporter complex in Escherichia coli. Mol. Microbiol. 6:2033-2040.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2033-2040
    • Dean, D.A.1    Hor, L.I.2    Shuman, H.A.3    Nikaido, H.4
  • 60
    • 0025687504 scopus 로고
    • Regulation of the maltose transport system of Escherichia coli by the glucose-specific enzyme III of the phosphoenolpyruvate-sugar phosphotransferase system. Characterization of inducer exclusion-resistant mutants and reconstitution of inducer exclusion in proteoliposomes
    • Dean, D. A., J. Reizer, H. Nikaido, and M. Saier. 1990. Regulation of the maltose transport system of Escherichia coli by the glucose-specific enzyme III of the phosphoenolpyruvate-sugar phosphotransferase 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.4
  • 61
    • 0027443973 scopus 로고
    • The importance of the binding-protein-dependent Mgl system to the transport of glucose in Escherichia coli growing on low sugar concentrations
    • Death, A., and T. Ferenci. 1993. The importance of the binding-protein-dependent Mgl system to the transport of glucose in Escherichia coli growing on low sugar concentrations. Res. Microbiol. 144:529-537.
    • (1993) Res. Microbiol. , vol.144 , pp. 529-537
    • Death, A.1    Ferenci, T.2
  • 62
    • 0028048576 scopus 로고
    • Between feast and famine: Endogenous inducer synthesis in the adaptation of Escherichia coli to growth with limiting carbohydrates
    • Death, A., and T. Ferenci. 1994. Between feast and famine: endogenous inducer synthesis in the adaptation of Escherichia coli to growth with limiting carbohydrates. J. Bacteriol. 176:5101-5107.
    • (1994) J. Bacteriol. , vol.176 , pp. 5101-5107
    • Death, A.1    Ferenci, T.2
  • 63
    • 0027457784 scopus 로고
    • Derepression of LamB protein facilitates outer membrane permeation of carbohydrates into Escherichia coli under conditions of nutrient stress
    • Death, A., L. Notley, and T. Ferenci. 1993. Derepression of LamB protein facilitates outer membrane permeation of carbohydrates into Escherichia coli under conditions of nutrient stress. J. Bacteriol. 175:1475-1483.
    • (1993) J. Bacteriol. , vol.175 , pp. 1475-1483
    • Death, A.1    Notley, L.2    Ferenci, T.3
  • 64
    • 0020631132 scopus 로고
    • Expression of the Escherichia coli malPQ operon remains unaffected after drastic alteration of its promoter
    • Débarbouillé, M., and O. Raibaud. 1983. Expression of the Escherichia coli malPQ operon remains unaffected after drastic alteration of its promoter. J. Bacteriol. 153:1221-1227.
    • (1983) J. Bacteriol. , vol.153 , pp. 1221-1227
    • Débarbouillé, M.1    Raibaud, O.2
  • 65
    • 0018791984 scopus 로고
    • The use of gene fusions to study the expression of malT, the positive regulator gene of the maltose regulon
    • Débarbouillé, M., and M, Schwartz. 1979. The use of gene fusions to study the expression of malT, the positive regulator gene of the maltose regulon. J. Mol. Biol. 132:521-534.
    • (1979) J. Mol. Biol. , vol.132 , pp. 521-534
    • Débarbouillé, M.1    Schwartz, M.2
  • 66
    • 0018953522 scopus 로고
    • Mutants which make more malT product, the activator of the maltose regulon in Escherichia coli
    • Débarbouillé, M., and M. Schwartz. 1980. Mutants which make more malT product, the activator of the maltose regulon in Escherichia coli. Mol. Gen. Genet. 178:589-595.
    • (1980) Mol. Gen. Genet. , vol.178 , pp. 589-595
    • Débarbouillé, M.1    Schwartz, M.2
  • 67
    • 0018076641 scopus 로고
    • Dominant constitutive mutations in malT, the positive regulator of the maltose regulon in Escherichia coli
    • Débarbouillé, M., H. A. Shuman, T. J. Silhavy, and M. Schwartz. 1978. Dominant constitutive mutations in malT, the positive regulator of the maltose regulon in Escherichia coli. J. Mol. Biol. 124:359-371.
    • (1978) J. Mol. Biol. , vol.124 , pp. 359-371
    • Débarbouillé, M.1    Shuman, H.A.2    Silhavy, T.J.3    Schwartz, M.4
  • 68
    • 2642702965 scopus 로고    scopus 로고
    • Ph.D. thesis. University of Konstanz, Konstanz, Germany
    • Decker, K. 1997. Ph.D. thesis. University of Konstanz, Konstanz, Germany.
    • (1997)
    • Decker, K.1
  • 69
    • 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., R. Peist, J. Reidl, M. Kossmann, B. Brand, and W. Boos. 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
  • 70
    • 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., J. Plumbridge, and W. Boos. 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
  • 71
    • 0023375651 scopus 로고
    • Export and secretion of the lipoprotein pullulanase by Klebsietla pneumoniae
    • d'Enfert, C., C. Chapon, and A. P. Pugsley. 1987. Export and secretion of the lipoprotein pullulanase by Klebsietla pneumoniae. Mol. Microbiol. 1:107-116.
    • (1987) Mol. Microbiol. , vol.1 , pp. 107-116
    • D'Enfert, C.1    Chapon, C.2    Pugsley, A.P.3
  • 72
    • 0028036559 scopus 로고
    • Control of translation by mRNA secondary structure in Escherichia coli
    • De Smit, M. H., and J. Van Duin. 1994. Control of translation by mRNA secondary structure in Escherichia coli. J. Mol. Biol. 244:144-150.
    • (1994) J. Mol. Biol. , vol.244 , pp. 144-150
    • De Smit, M.H.1    Van Duin, J.2
  • 73
    • 0028999469 scopus 로고
    • Interaction of SecB with intermediates along the folding pathway of maltose-binding protein
    • Diamond, D. L., S. Strobel, S.-Y. Chun, and L. L. Randall. 1995. Interaction of SecB with intermediates along the folding pathway of maltose-binding protein. Protein Sci. 4:1118-1123.
    • (1995) Protein Sci. , vol.4 , pp. 1118-1123
    • Diamond, D.L.1    Strobel, S.2    Chun, S.-Y.3    Randall, L.L.4
  • 74
    • 0018097321 scopus 로고
    • Pole cap formation in Escherichia coli following induction of the maltose-binding protein
    • Dietzel, I., V. Kolb, and W. Boos. 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
  • 75
    • 0029669943 scopus 로고    scopus 로고
    • Regulation of Escherichia coli adenylate cyclase activity during hexose phosphate transport
    • Dumay, V., A. Danchin, and M. Crasnier. 1996. Regulation of Escherichia coli adenylate cyclase activity during hexose phosphate transport. Microbiology 142:575-583.
    • (1996) Microbiology , vol.142 , pp. 575-583
    • Dumay, V.1    Danchin, A.2    Crasnier, M.3
  • 76
    • 0021252896 scopus 로고
    • Sequences of the malE gene and of its product, the maltose-binding protein of Escherichia coli K12
    • Duplay, P., H. Bedouelle, A. Fowler, I. Zabin, W. Saurin, and M. Hofnung. 1984. Sequences of the malE gene and of its product, the maltose-binding protein of Escherichia coli K12. J. Biol. Chem. 259:10606-10613.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10606-10613
    • Duplay, P.1    Bedouelle, H.2    Fowler, A.3    Zabin, I.4    Saurin, W.5    Hofnung, M.6
  • 77
    • 0023240668 scopus 로고
    • Silent and functional changes in the periplasmic maltose binding protein of Escherichia coli K12. II. Chemotaxis towards maltose
    • Duplay, P., and S. Szmelcman. 1987. Silent and functional changes in the periplasmic maltose binding protein of Escherichia coli K12. II. Chemotaxis towards maltose. J. Mol. Biol. 194:675-678.
    • (1987) J. Mol. Biol. , vol.194 , pp. 675-678
    • Duplay, P.1    Szmelcman, S.2
  • 78
    • 0023274512 scopus 로고
    • Silent and functional changes in the periplasmic maltose binding protein of Escherichia coli K12. I. Transport of maltose
    • Duplay, P., S. Szmelcman, H. Bedouelle, and M. Hofnung. 1987. Silent and functional changes in the periplasmic maltose binding protein of Escherichia coli K12. I. Transport of maltose. J. Mol. Biol. 194:663-673.
    • (1987) J. Mol. Biol. , vol.194 , pp. 663-673
    • Duplay, P.1    Szmelcman, S.2    Bedouelle, H.3    Hofnung, M.4
  • 79
    • 0029644059 scopus 로고    scopus 로고
    • Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway
    • Dutzler, R., Y.-F. Wang, P. J. Rizkallah, J. P. Rosenbusch, and T. Schirmer. 1996. Crystal structures of various maltooligosaccharides 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
  • 80
    • 0029975122 scopus 로고    scopus 로고
    • Characterization of transmembrane domains 6, 7, and 8 of MalF by mutational analysis
    • Ehrle, R., C. Pick, R. Ulrich, E. Hofmann, and M. Ehrmann. 1996. Characterization of transmembrane domains 6, 7, and 8 of MalF by mutational analysis. J. Bacteriol. 178:2255-2262.
    • (1996) J. Bacteriol. , vol.178 , pp. 2255-2262
    • Ehrle, R.1    Pick, C.2    Ulrich, R.3    Hofmann, E.4    Ehrmann, M.5
  • 81
    • 0023394131 scopus 로고
    • Identification of endogenous inducers of the mal system in Escherichia coli
    • Ehrmann, M., and W. Boos. 1987. Identification of endogenous inducers of the mal system in Escherichia coli. J. Bacteriol. 169:3539-3545.
    • (1987) J. Bacteriol. , vol.169 , pp. 3539-3545
    • Ehrmann, M.1    Boos, W.2
  • 82
    • 0025052350 scopus 로고
    • Genetic analysis of membrane protein topology by a sandwich gene fusion approach
    • Ehrmann, M., D. Boyd, and J. Beckwith. 1990. Genetic analysis of membrane protein topology by a sandwich gene fusion approach. Proc. Natl. Acad. Sci. USA 87:7574-7578.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7574-7578
    • Ehrmann, M.1    Boyd, D.2    Beckwith, J.3
  • 83
    • 0027132575 scopus 로고
    • ABC transporters: Bacterial exporters
    • Fath, M. J., and R, Kolter. 1993. ABC transporters: bacterial exporters. Microbiol. Rev. 57:995-1017.
    • (1993) Microbiol. Rev. , vol.57 , pp. 995-1017
    • Fath, M.J.1    Kolter, R.2
  • 84
    • 0019194038 scopus 로고
    • The recognition of maltodexirins by Escherichia coli
    • Ferenci, T. 1980. The recognition of maltodexirins by Escherichia coli. Eur. J. Biochem. 108:631-636.
    • (1980) Eur. J. Biochem. , vol.108 , pp. 631-636
    • Ferenci, T.1
  • 85
    • 0019254027 scopus 로고
    • The role of the Escherichia coli lambda receptor in the transport of maltose and maltodextrins
    • Ferenci, T., and W. Boos. 1980. The role of the Escherichia coli lambda receptor in the transport of maltose and maltodextrins. J. Supramol. Struct. 13:101-116.
    • (1980) J. Supramol. Struct. , vol.13 , pp. 101-116
    • Ferenci, T.1    Boos, W.2
  • 86
    • 0019266916 scopus 로고
    • The role of the periplasmic maltose-binding protein and the outer-membrane phage lambda receptor in maltodextrin transport of Escherichia coli
    • Ferenci, T., J. Brass, and W. Boos. 1980. The role of the periplasmic maltose-binding protein and the outer-membrane phage lambda receptor in maltodextrin transport of Escherichia coli. Biochem. Soc. Trans. 8:680-681.
    • (1980) Biochem. Soc. Trans. , vol.8 , pp. 680-681
    • Ferenci, T.1    Brass, J.2    Boos, W.3
  • 87
    • 0022525924 scopus 로고
    • Substrate specificity of the Escherichia coli maltodextrin transport system and its component proteins
    • Ferenci, T., M. Muir, K.-S. Lee, and D. Maris. 1986. Substrate specificity of the Escherichia coli maltodextrin transport system and its component proteins. Biochim. Biophys. Acta 860:44-50.
    • (1986) Biochim. Biophys. Acta , vol.860 , pp. 44-50
    • Ferenci, T.1    Muir, M.2    Lee, K.-S.3    Maris, D.4
  • 88
    • 0018966820 scopus 로고
    • Lambda receptor in the outer membrane of Escherichia coli as a binding protein for maliodextrins and starch polysaccharides
    • Ferenci, T., M. Schwentorat, S. Ulrich, and J. Vilmart. 1980. Lambda receptor in the outer membrane of Escherichia coli as a binding protein for maliodextrins and starch polysaccharides. J. Bacteriol. 142:521-526.
    • (1980) J. Bacteriol. , vol.142 , pp. 521-526
    • Ferenci, T.1    Schwentorat, M.2    Ulrich, S.3    Vilmart, J.4
  • 89
    • 0029919677 scopus 로고    scopus 로고
    • Genetics of a novel starch utilisation pathway present in Klebsiella oxytoca
    • Fiedler, G., M. Pajatsch, and A. Böck. 1996. Genetics of a novel starch utilisation pathway present in Klebsiella oxytoca. J. Mol. Biol. 256:279-291.
    • (1996) J. Mol. Biol. , vol.256 , pp. 279-291
    • Fiedler, G.1    Pajatsch, M.2    Böck, A.3
  • 90
    • 0027255185 scopus 로고
    • prlA suppression of defective export of maltose-binding protein in secB mutants of Escherichia coli
    • Francetic, O., M. P. Hanson, and C. A. Kumamoto. 1993. prlA suppression of defective export of maltose-binding protein in secB mutants of Escherichia coli. J. Bacteriol. 175:4036-4044.
    • (1993) J. Bacteriol. , vol.175 , pp. 4036-4044
    • Francetic, O.1    Hanson, M.P.2    Kumamoto, C.A.3
  • 91
    • 0023030937 scopus 로고
    • α-Amylase of Escherichia coli, mapping and cloning of the structural gene, malS, and identification of its product as a periplasmic protein
    • Freundlieb, S., and W. Boos. 1986. α-Amylase of Escherichia coli, mapping and cloning of the structural gene, malS, and identification of its product as a periplasmic protein. J. Biol. Chem. 261:2946-2953.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2946-2953
    • Freundlieb, S.1    Boos, W.2
  • 92
    • 0023906938 scopus 로고
    • Facilitated diffusion of p-nitrophenyl-α-D-maltohexaoside through the outer membrane of Escherichia coli
    • Freundlieb, S., U. Ehmann, and W. Boos. 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
  • 93
    • 0021161867 scopus 로고
    • The nucleotide sequence of the gene for MalF protein, an inner membrane component of the maltose transport system of Escherichia coli. Repeated DNA sequences are found in the malE-malF intercistronic region
    • Froshauer, S., and J. Beckwith. 1984. The nucleotide sequence of the gene for MalF protein, an inner membrane component of the maltose transport system of Escherichia coli. Repeated DNA sequences are found in the malE-malF intercistronic region. J. Biol. Chem. 259:10896-10903.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10896-10903
    • Froshauer, S.1    Beckwith, J.2
  • 94
    • 0023883641 scopus 로고
    • Genetic analysis of the membrane insertion and topology of MalF, a cytopiasmic membrane protein of Escherichia coli
    • Froshauer, S., G. N. Green, D. Boyd, K. McGovern, and J. Beckwith. 1988. Genetic analysis of the membrane insertion and topology of MalF, a cytopiasmic membrane protein of Escherichia coli. J. Mol. Biol. 200:501-511.
    • (1988) J. Mol. Biol. , vol.200 , pp. 501-511
    • Froshauer, S.1    Green, G.N.2    Boyd, D.3    McGovern, K.4    Beckwith, J.5
  • 96
    • 0030978479 scopus 로고    scopus 로고
    • Thermodynamic characterization of the reversible, two-state unfolding of maltose binding protein, a large two-domain protein
    • Ganesh, C., A. N. Shah, C. P. Swaminathan, A. Surolia, and R. Varadarajan. 1997. Thermodynamic characterization of the reversible, two-state unfolding of maltose binding protein, a large two-domain protein. Biochemistry 36:5020-5028.
    • (1997) Biochemistry , vol.36 , pp. 5020-5028
    • Ganesh, C.1    Shah, A.N.2    Swaminathan, C.P.3    Surolia, A.4    Varadarajan, R.5
  • 97
    • 0026521574 scopus 로고
    • Aspartate and maltose-binding protein interact with adjacent sites in the tar chemotactic signal transducer of Escherichia coli
    • Gardina, P., C. Conway, M. Kossman, and M. Manson. 1992. Aspartate and maltose-binding protein interact with adjacent sites in the tar chemotactic signal transducer of Escherichia coli. J. Bacteriol. 174:1528-1536.
    • (1992) J. Bacteriol. , vol.174 , pp. 1528-1536
    • Gardina, P.1    Conway, C.2    Kossman, M.3    Manson, M.4
  • 98
    • 0030971441 scopus 로고    scopus 로고
    • Maltose-binding protein interacts simultaneously and asymmetrically with both subunits of the Tar chemoreceptor
    • Gardina, P. J., A. F. Bormans, M. A. Hawkins, J. W. Meeker, and M. D. Manson. 1997. Maltose-binding protein interacts simultaneously and asymmetrically with both subunits of the Tar chemoreceptor. Mol. Microbiol. 23:1181-1191.
    • (1997) Mol. Microbiol. , vol.23 , pp. 1181-1191
    • Gardina, P.J.1    Bormans, A.F.2    Hawkins, M.A.3    Meeker, J.W.4    Manson, M.D.5
  • 99
    • 2642608238 scopus 로고    scopus 로고
    • 1997. Unpublished observations
    • Gerhardt, F., and W. Boos. 1997. Unpublished observations.
    • Gerhardt, F.1    Boos, W.2
  • 100
    • 0030926443 scopus 로고    scopus 로고
    • Spectroscopic properties of an engineered maltose binding protein
    • Gilardi, G., G. Mei, N. Rosato, A. F. Agrò, and A. E. G. Cass. 1997. Spectroscopic properties of an engineered maltose binding protein. Protein Eng. 10:479-486.
    • (1997) Protein Eng. , vol.10 , pp. 479-486
    • Gilardi, G.1    Mei, G.2    Rosato, N.3    Agrò, A.F.4    Cass, A.E.G.5
  • 101
    • 0028538941 scopus 로고
    • Engineering the maltose binding protein for reagentless fluorescence sensing
    • Gilardi, G., L. Q. Zhou, L. Hibbert, and A. E. G. Cass. 1994. Engineering the maltose binding protein for reagentless fluorescence sensing. Anal. Chem. 66:3840-3847.
    • (1994) Anal. Chem. , vol.66 , pp. 3840-3847
    • Gilardi, G.1    Zhou, L.Q.2    Hibbert, L.3    Cass, A.E.G.4
  • 102
    • 0024198129 scopus 로고
    • Evidence for high affinity binding-protein dependent transport systems in gram-positive bacteria and in Mycoplasma
    • Gilson, E., G. Alloing, T. Schmidt, J. P. Claverys, R. Dudler, and M. Hofnung. 1988. Evidence for high affinity binding-protein dependent transport systems in gram-positive bacteria and in Mycoplasma. EMBO J. 7:3971-3974.
    • (1988) EMBO J. , vol.7 , pp. 3971-3974
    • Gilson, E.1    Alloing, G.2    Schmidt, T.3    Claverys, J.P.4    Dudler, R.5    Hofnung, M.6
  • 103
    • 0020491365 scopus 로고
    • Sequence of the malK gene in Escherichia coli K12
    • Gilson, E., H. Nikaido, and M. Hofnung. 1982. Sequence of the malK gene in Escherichia coli K12. Nucleic Acids Res. 10:7449-7458.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 7449-7458
    • Gilson, E.1    Nikaido, H.2    Hofnung, M.3
  • 104
    • 0023042761 scopus 로고
    • malM, a new gene of the maltose regulon in Escherichia coli K12. I. malM is the last gene of the malK-lamB operon and encodes a periplasmic protein
    • Gilson, E., J.-P. Roussel, A. Charbit, D. Perrin, and M. Hofnung. 1986. malM, a new gene of the maltose regulon in Escherichia coli K12. I. malM is the last gene of the malK-lamB operon and encodes a periplasmic protein. J. Mol. Biol. 191:303-311.
    • (1986) J. Mol. Biol. , vol.191 , pp. 303-311
    • Gilson, E.1    Roussel, J.-P.2    Charbit, A.3    Perrin, D.4    Hofnung, M.5
  • 105
    • 0020483946 scopus 로고
    • Regulation of gene expression in Escherichia coli by the local anesthetic procaine
    • Graneti, S., and M. Villarejo. 1982. Regulation of gene expression in Escherichia coli by the local anesthetic procaine. J. Mol. Biol. 160:363-367.
    • (1982) J. Mol. Biol. , vol.160 , pp. 363-367
    • Graneti, S.1    Villarejo, M.2
  • 106
    • 0021591656 scopus 로고
    • Point mutations that reduce the expression of malPQ, a positively controlled operon of Escherichia coli
    • Gutierrez, C., and O. Raibaud. 1984. Point mutations that reduce the expression of malPQ, a positively controlled operon of Escherichia coli. J. Mol. Biol. 177:69-86.
    • (1984) J. Mol. Biol. , vol.177 , pp. 69-86
    • Gutierrez, C.1    Raibaud, O.2
  • 107
    • 0030758073 scopus 로고    scopus 로고
    • Two modes of ligand binding in maltose-binding protein of Escherichia coli. Functional significance in active transport
    • Hall, J. A., A. K. Ganesan, J. Chen, and H. Nikaido. 1997. Two modes of ligand binding in maltose-binding protein of Escherichia coli. Functional significance in active transport. J. Biol. Chem. 272:17615-17622.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17615-17622
    • Hall, J.A.1    Ganesan, A.K.2    Chen, J.3    Nikaido, H.4
  • 108
    • 0030764656 scopus 로고    scopus 로고
    • Two modes of ligand binding in maltose-binding protein of Escherichia coli. Correlation with the structure of ligands and the structure of binding protein
    • Hall, J. A., K. Gehring, and H. Nikaido. 1997. Two modes of ligand binding in maltose-binding protein of Escherichia coli. Correlation with the structure of ligands and the structure of binding protein. J. Biol. Chem. 272: 17605-17609.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17605-17609
    • Hall, J.A.1    Gehring, K.2    Nikaido, H.3
  • 109
    • 0030757501 scopus 로고    scopus 로고
    • Two modes of ligand binding in maltose-binding protein of Escherichia coli. Electron paramagnetic resonance study of ligand-induced global conformational changes by site-directed spin labeling
    • Hall, J. A., T. E. Thorgeirsson, J. Liu, Y.-K. Shin, and H. Nikaido. 1997. Two modes of ligand binding in maltose-binding protein of Escherichia coli. Electron paramagnetic resonance study of ligand-induced global conformational changes by site-directed spin labeling. J. Biol. Chem. 272:17610-17614.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17610-17614
    • Hall, J.A.1    Thorgeirsson, T.E.2    Liu, J.3    Shin, Y.-K.4    Nikaido, H.5
  • 110
    • 0020486135 scopus 로고
    • A role for mRNA secondary structure in the control of translation initiation
    • Hall, M. N., J. Gabay, M. Débarbouillé, and M. Schwartz. 1982. A role for mRNA secondary structure in the control of translation initiation. Nature 295:616-618.
    • (1982) Nature , vol.295 , pp. 616-618
    • Hall, M.N.1    Gabay, J.2    Débarbouillé, M.3    Schwartz, M.4
  • 111
    • 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 W. Boos. 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
  • 112
    • 0014518843 scopus 로고
    • Genetic analysis of the maltose A region in Escherichia coli
    • Hatfield, D., M. Hofnung, and M. Schwartz. 1969. Genetic analysis of the maltose A region in Escherichia coli. J. Bacteriol. 98:559-567.
    • (1969) J. Bacteriol. , vol.98 , pp. 559-567
    • Hatfield, D.1    Hofnung, M.2    Schwartz, M.3
  • 113
    • 0014624086 scopus 로고
    • Nonsense mutations in the maltose A region of the genetic map of Escherichia coli
    • Harheld, D., M. Hofnung, and M. Schwartz. 1969. Nonsense mutations in the maltose A region of the genetic map of Escherichia coli. J. Bacteriol. 100:1311-1315.
    • (1969) J. Bacteriol. , vol.100 , pp. 1311-1315
    • Harheld, D.1    Hofnung, M.2    Schwartz, M.3
  • 114
    • 0016608768 scopus 로고
    • The maltose chemoreceptor of Escherichia coli
    • Hazelbauer, G. L. 1975. The maltose chemoreceptor of Escherichia coli. J. Bacteriol. 122:206-214.
    • (1975) J. Bacteriol. , vol.122 , pp. 206-214
    • Hazelbauer, G.L.1
  • 115
    • 0027360468 scopus 로고
    • Functional exchangeability of the ABC proteins of the periplasmic binding protein-dependent transport systems Ugp and Mal
    • Hekstra, D., and J. Tommassen. 1993. Functional exchangeability of the ABC proteins of the periplasmic binding protein-dependent transport systems Ugp and Mal. J. Bacteriol. 175:6546-6552.
    • (1993) J. Bacteriol. , vol.175 , pp. 6546-6552
    • Hekstra, D.1    Tommassen, J.2
  • 116
    • 0021101144 scopus 로고
    • Maltose and lactose transport in Escherichia coli. Examples of two different types of concentra five transport systems
    • Hengge, R., and W. Boos. 1983. Maltose and lactose transport in Escherichia coli. Examples of two different types of concentra five transport systems. Biochim. Biophys, Acta 737:443-478.
    • (1983) Biochim. Biophys, Acta , vol.737 , pp. 443-478
    • Hengge, R.1    Boos, W.2
  • 117
    • 0029843811 scopus 로고    scopus 로고
    • s as a global regulator in the osmotic control of gene expression in Escherichia coli
    • s as a global regulator in the osmotic control of gene expression in Escherichia coli. Mol. Microbiol. 21:887-893.
    • (1996) Mol. Microbiol. , vol.21 , pp. 887-893
    • Hengge-Aronis, R.1
  • 118
    • 0026681771 scopus 로고
    • Identification and molecular analysis of glgS, a novel growth-phase-regulated and rpoS-dependent gene involved in glycogen synthesis in Escherichia coli
    • Hengge-Aronis, R., and D. Fischer. 1992. Identification and molecular analysis of glgS, a novel growth-phase-regulated and rpoS-dependent gene involved in glycogen synthesis in Escherichia coli. Mol. Microbiol. 6:1877-1886.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1877-1886
    • Hengge-Aronis, R.1    Fischer, D.2
  • 119
    • 0026330981 scopus 로고
    • Trehalose synthesis genes are controlled by the putative sigma-factor encoded by rpoS and are involved in stationary-phase thermotolerance in Escherichia coli
    • Hengge-Aronis, R., W. Klein, R. Lange, M. Rimmele, and W. Boos, 1991. Trehalose synthesis genes are controlled by the putative sigma-factor encoded by rpoS and are involved in stationary-phase thermotolerance in Escherichia coli. J. Bacieriol. 173:7918-7924.
    • (1991) J. Bacieriol. , vol.173 , pp. 7918-7924
    • Hengge-Aronis, R.1    Klein, W.2    Lange, R.3    Rimmele, M.4    Boos, W.5
  • 120
    • 0030276148 scopus 로고    scopus 로고
    • Biochemical identification of a lipoprotein with maltose-binding activity in the thermoacidophilic Gram-positive bacterium Aiicyctobacillus acidocaldarius
    • Herrmann, A., A. Schlösser, R. Schmid, and E. Schneider. 1996. Biochemical identification of a lipoprotein with maltose-binding activity in the thermoacidophilic Gram-positive bacterium Aiicyctobacillus acidocaldarius. Res. Microbiol. 147:733-737.
    • (1996) Res. Microbiol. , vol.147 , pp. 733-737
    • Herrmann, A.1    Schlösser, A.2    Schmid, R.3    Schneider, E.4
  • 121
    • 0025945286 scopus 로고
    • Identification of Escherichia coli genes whose expression increases as a function of external pH
    • Heyde, M., J. L. Coll, and R. Portalier. 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
  • 122
    • 0026621245 scopus 로고
    • ABC transporters-from microorganisms to man
    • Higgins, C. F. 1992. ABC transporters-from microorganisms to man. Annu. Rev. Cell Biol. 8:67-113.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 124
    • 0028933982 scopus 로고
    • An intelligent channel (and more)
    • Hofnung, M. 1995. An intelligent channel (and more). Science 267:473-474.
    • (1995) Science , vol.267 , pp. 473-474
    • Hofnung, M.1
  • 125
    • 0015969332 scopus 로고
    • malB region in Escherichia coli K-12: Characterization of new mutations
    • Hofnung, M., D. Hatneld, and M. Schwartz. 1974. malB region in Escherichia coli K-12: characterization of new mutations. J. Bacteriol. 117:40-47.
    • (1974) J. Bacteriol. , vol.117 , pp. 40-47
    • Hofnung, M.1    Hatneld, D.2    Schwartz, M.3
  • 126
    • 0015171906 scopus 로고
    • Mutations allowing growth on maltose of Escherichia coli K 12 strains with a deleted malT gene
    • Hofnung, M., and M. Schwartz. 1971. Mutations allowing growth on maltose of Escherichia coli K 12 strains with a deleted malT gene. Mol. Gen. Genet. 112:117-132.
    • (1971) Mol. Gen. Genet. , vol.112 , pp. 117-132
    • Hofnung, M.1    Schwartz, M.2
  • 127
    • 0015223531 scopus 로고
    • Complementation studies in the maltose-A region of Escherichia coli K12 genetic map
    • Hofnung, M., M. Schwartz, and D. Hatfield. 1971. Complementation studies in the maltose-A region of Escherichia coli K12 genetic map. J. Mol. Biol. 61:681-694.
    • (1971) J. Mol. Biol. , vol.61 , pp. 681-694
    • Hofnung, M.1    Schwartz, M.2    Hatfield, D.3
  • 128
    • 0027490784 scopus 로고
    • Genetic analysis of periplasmic binding protein dependent transport in Escherichia coli. Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK2 membrane transport complex
    • Hor, L. I., and H. A. Shuman. 1993. Genetic analysis of periplasmic binding protein dependent transport in Escherichia coli. Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK2 membrane transport complex. J. Mol. Biol. 233:659-670.
    • (1993) J. Mol. Biol. , vol.233 , pp. 659-670
    • Hor, L.I.1    Shuman, H.A.2
  • 129
    • 0031009431 scopus 로고    scopus 로고
    • Characterization of TreR, the major regulator of the Escherichia coli trehalose system
    • Horlacher, R., and W. Boos. 1997. Characterization of TreR, the major regulator of the Escherichia coli trehalose system. J. Biol. Chem. 272:13026-13032.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13026-13032
    • Horlacher, R.1    Boos, W.2
  • 130
    • 0031888811 scopus 로고    scopus 로고
    • Archaeal binding protein-dependent ABC transporter: Molecular and biochemical analysis of the trehalose/maltose transport system of the hyperthermophilic archaeon Thermococcus litoralis
    • Horlacher, R., K. B. Xavier, H. Santos, J. DiRuggiero, M. Kossmann, and W. Boos. 1998. Archaeal binding protein-dependent ABC transporter: molecular and biochemical analysis of the trehalose/maltose transport system of the hyperthermophilic archaeon Thermococcus litoralis. J. Bacteriol. 180: 680-689.
    • (1998) J. Bacteriol. , vol.180 , pp. 680-689
    • Horlacher, R.1    Xavier, K.B.2    Santos, H.3    DiRuggiero, J.4    Kossmann, M.5    Boos, W.6
  • 131
    • 85007744911 scopus 로고
    • Decreasing accumulation of acetate in a rich medium by Escherichia coli on introduction of genes on a multicopy plasmid
    • Hosono, K., H. Kakuda, and S. Ichihara. 1995. Decreasing accumulation of acetate in a rich medium by Escherichia coli on introduction of genes on a multicopy plasmid. Biosci. Biotechnol. Biochem. 59:256-261.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 256-261
    • Hosono, K.1    Kakuda, H.2    Ichihara, S.3
  • 132
    • 0029644725 scopus 로고
    • Repressor fusions as a tool to study protein-protein interactions
    • Hu, J. C. 1995. Repressor fusions as a tool to study protein-protein interactions. Structure 3:431-433.
    • (1995) Structure , vol.3 , pp. 431-433
    • Hu, J.C.1
  • 133
    • 0030580087 scopus 로고    scopus 로고
    • Identification of the bases in the ompF regulatory region, which interact with the transcription factor OmpR
    • Huang, K.-J., and M. M. Igo. 1996. Identification of the bases in the ompF regulatory region, which interact with the transcription factor OmpR. J. Mol. Biol. 262:615-628.
    • (1996) J. Mol. Biol. , vol.262 , pp. 615-628
    • Huang, K.-J.1    Igo, M.M.2
  • 134
    • 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., H. Takahashi, T. Mizuno, and H. Aiba. 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
  • 135
    • 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., A. Hanamura, T. Inada, and H. Aiba. 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
  • 136
    • 0030596521 scopus 로고    scopus 로고
    • Rate constants of sugar transport through two LamB mutants of Escherichia coli: Comparison with wild-type maltoporin and LamB of Salmonella typhimurium
    • Jordy, M., C. Andersen, K. Schülein, T. Ferenci, and R. Benz. 1996. Rate constants of sugar transport through two LamB mutants of Escherichia coli: comparison with wild-type maltoporin and 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
  • 137
    • 0026541540 scopus 로고
    • Molecular cloning and physical mapping of the otsBA genes, which encode the osmoregulatory trehalose pathway of Escherichia coli. Evidence that transcription is activated by KatF (AppR)
    • Kaasen, I., P. Falkenberg, O. B. Styrvold, and A. R. Strøm. 1992. Molecular cloning and physical mapping of the otsBA genes, which encode the osmoregulatory trehalose pathway of Escherichia coli. Evidence that transcription is activated by KatF (AppR). J. Bacteriol. 174:889-898.
    • (1992) J. Bacteriol. , vol.174 , pp. 889-898
    • Kaasen, I.1    Falkenberg, P.2    Styrvold, O.B.3    Strøm, A.R.4
  • 138
    • 0016151381 scopus 로고
    • Active transport of maltose in Escherichia coli K-12. Involvement of a periplasmic maltose-binding protein
    • Kellerraan, O., and S. Szmelcman. 1974. Active transport of maltose in Escherichia coli K-12. Involvement of a periplasmic maltose-binding protein. Eur. J. Biochem. 47:139-149.
    • (1974) Eur. J. Biochem. , vol.47 , pp. 139-149
    • Kellerraan, O.1    Szmelcman, S.2
  • 139
    • 0031035649 scopus 로고    scopus 로고
    • Transcription induction of the ferric citrate transport genes via the N-terminus of the FecA outer membrane protein, the Ton system and the electrochemical potential of the cytoplasmic membrane
    • Kim, I., A. Stiefel, S. Planter, A. Angerer, and V. Braun. 1997. Transcription induction of the ferric citrate transport genes via the N-terminus of the FecA outer membrane protein, the Ton system and the electrochemical potential of the cytoplasmic membrane. Mol. Microbiol. 23:333-344.
    • (1997) Mol. Microbiol. , vol.23 , pp. 333-344
    • Kim, I.1    Stiefel, A.2    Planter, S.3    Angerer, A.4    Braun, V.5
  • 140
    • 0027956170 scopus 로고
    • SecA protein is exposed to the periplasmic surface of the E. coli inner membrane in its active state
    • Kim, Y. J., T. Rajapandi, and D. Oliver. 1994. SecA protein is exposed to the periplasmic surface of the E. coli inner membrane in its active state. Cell 78:845-853.
    • (1994) Cell , vol.78 , pp. 845-853
    • Kim, Y.J.1    Rajapandi, T.2    Oliver, D.3
  • 141
    • 0027536158 scopus 로고
    • Induction of the A receptor is essential for the effective uptake of trehalose in Escherichia coli
    • Klein, W., and W. Boos. 1993. Induction of the A receptor is essential for the effective uptake of trehalose in Escherichia coli. J. Bacteriol. 175:1682-1686.
    • (1993) J. Bacteriol. , vol.175 , pp. 1682-1686
    • Klein, W.1    Boos, W.2
  • 142
    • 0029013340 scopus 로고
    • Molecular analysis of treB encoding the Escherichia coli enzyme II specific for trehalose
    • Klein, W., R. Horlacher, and W. Boos. 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
  • 143
    • 0027236999 scopus 로고
    • Transcriptional regulation by cAMP and its receptor protein
    • Kolb, A., S. Busby, H. Buc, S. Garges, and S. Adhya. 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
  • 144
    • 2642673950 scopus 로고    scopus 로고
    • 1997. Unpublished observations
    • Kolbus, T., and W. Boos. 1997. Unpublished observations.
    • Kolbus, T.1    Boos, W.2
  • 146
    • 0025833825 scopus 로고
    • Evidence for a new Escherichia coli protein resembling a lysyl-tRNA synthetase
    • Kong, L., M. Fromant, S. Blanquet, and P. Plateau. 1991. Evidence for a new Escherichia coli protein resembling a lysyl-tRNA synthetase. Gene 108:163-164.
    • (1991) Gene , vol.108 , pp. 163-164
    • Kong, L.1    Fromant, M.2    Blanquet, S.3    Plateau, P.4
  • 147
    • 0025904264 scopus 로고
    • The activities of the Escherichia coli MalK protein in maltose transport, regulation and inducer exclusion can be separated by mutations
    • Kühnau, S., M. Reyes, A. Sievertsen, H. A. Shuman, and W. Boos. 1991. The activities of the Escherichia coli MalK protein in maltose transport, regulation and inducer exclusion can be separated by mutations. J. Bacteriol. 173:2180-2186.
    • (1991) J. Bacteriol. , vol.173 , pp. 2180-2186
    • Kühnau, S.1    Reyes, M.2    Sievertsen, A.3    Shuman, H.A.4    Boos, W.5
  • 148
    • 0022993290 scopus 로고
    • Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli ADP-glucose:α-1,4-glucan, 4-glucosyltransferase as deduced from the nucleotide sequence of the gtgA gene
    • Kumar, A., C. E. Larsen, and J. Preiss. 1986. Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli ADP-glucose:α-1,4-glucan, 4-glucosyltransferase as deduced from the nucleotide sequence of the gtgA gene. J. Biol. Chem. 261:16256-16259.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16256-16259
    • Kumar, A.1    Larsen, C.E.2    Preiss, J.3
  • 149
    • 0028034006 scopus 로고
    • The maltose regulon of Vibrio cholerae affects production and secretion of virulence factors
    • Lang, H., G. Jonson, J. Holmgren, and E. T. Palva. 1994. The maltose regulon of Vibrio cholerae affects production and secretion of virulence factors. Infect. Immun. 62:4781-4788.
    • (1994) Infect. Immun. , vol.62 , pp. 4781-4788
    • Lang, H.1    Jonson, G.2    Holmgren, J.3    Palva, E.T.4
  • 150
    • 0026899819 scopus 로고
    • Studies of the interaction of the maltose-binding protein of Escherichia coli, a closed-groove binder, with 4,6-O-ethylidenemalto-oligosaccharides (dp 2-5) and its regioselective labelling with 3-azibutyl 1-thio-alpha-(6-H-3) maltoside
    • Lehmann, J., E. Schiltz, and J. Steck. 1992. Studies of the interaction of the maltose-binding protein of Escherichia coli, a closed-groove binder, with 4,6-O-ethylidenemalto-oligosaccharides (dp 2-5) and its regioselective labelling with 3-azibutyl 1-thio-alpha-(6-H-3) maltoside. Carbohydr. Res. 232:77-87.
    • (1992) Carbohydr. Res. , vol.232 , pp. 77-87
    • Lehmann, J.1    Schiltz, E.2    Steck, J.3
  • 151
    • 0031039347 scopus 로고    scopus 로고
    • MalFGK complex assembly and transport and regulatory characteristics of MalK insertion mutants
    • Lippincott, J., and B. Traxler. 1997. MalFGK complex assembly and transport and regulatory characteristics of MalK insertion mutants. J. Bacteriol. 179:1337-1343.
    • (1997) J. Bacteriol. , vol.179 , pp. 1337-1343
    • Lippincott, J.1    Traxler, B.2
  • 152
    • 0031021530 scopus 로고    scopus 로고
    • Characterization of transport through the periplasmic histidine permease using proteoliposomes reconstituted by dialysis
    • Liu, C. E., and G. F. L. Ames. 1997. Characterization of transport through the periplasmic histidine permease using proteoliposomes reconstituted by dialysis. J. Biol. Chem. 272:859-866.
    • (1997) J. Biol. Chem. , vol.272 , pp. 859-866
    • Liu, C.E.1    Ames, G.F.L.2
  • 153
    • 0028148056 scopus 로고
    • Molecular cloning and characterization of the pgm gene encoding phosphoglucomutase of Escherichia coli
    • Lu, M., and N. Kleckner. 1994. Molecular cloning and characterization of the pgm gene encoding phosphoglucomutase of Escherichia coli. J. Bacteriol. 176:5847-5851.
    • (1994) J. Bacteriol. , vol.176 , pp. 5847-5851
    • Lu, M.1    Kleckner, N.2
  • 154
    • 0020674087 scopus 로고
    • Bacteriophage lambda receptor protein in Escherichia coli K-12: Lowered affinity of some mutant proteins for maltose-binding protein in vitro
    • Luckey, M., and H. Nikaido. 1983. Bacteriophage lambda receptor protein in Escherichia coli K-12: lowered affinity of some mutant proteins for maltose-binding protein in vitro. J. Bacteriol. 153:1056-1059.
    • (1983) J. Bacteriol. , vol.153 , pp. 1056-1059
    • Luckey, M.1    Nikaido, H.2
  • 155
    • 0026218418 scopus 로고
    • Activation of the osmoregulated ompC gene by the OmpR protein in Escherichia coli: A study involving synthetic OmpR-binding sequences
    • Maeda, S., K. Takayanagi, Y. Nishimura, T. Maruyama, K. Sato, and T. Mizuno. 1991. Activation of the osmoregulated ompC gene by the OmpR protein in Escherichia coli: a study involving synthetic OmpR-binding sequences. J. Biochem. (Tokyo) 110:324-327.
    • (1991) J. Biochem. (Tokyo) , vol.110 , pp. 324-327
    • Maeda, S.1    Takayanagi, K.2    Nishimura, Y.3    Maruyama, T.4    Sato, K.5    Mizuno, T.6
  • 156
    • 0023028051 scopus 로고
    • A genetic approach to analyzing membrane protein topology
    • Manoil, C., and J. Beckwith. 1986. A genetic approach to analyzing membrane protein topology. Science 233:1403-1408.
    • (1986) Science , vol.233 , pp. 1403-1408
    • Manoil, C.1    Beckwith, J.2
  • 157
    • 0027223571 scopus 로고
    • Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formation in vivo
    • Martin, J. L., G. Waksman, J. C. A. Bardwell, J. Beckwith, and J. Kuriyan. 1993. Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formation in vivo. J. Mol. Biol. 230:1097-1100.
    • (1993) J. Mol. Biol. , vol.230 , pp. 1097-1100
    • Martin, J.L.1    Waksman, G.2    Bardwell, J.C.A.3    Beckwith, J.4    Kuriyan, J.5
  • 158
    • 0029557690 scopus 로고
    • The inhibition of maltose transport by the unliganded form of the maltose-binding protein of Escherichia coli: Experimental findings and mathematical treatment
    • Merino, G., W. Boos, H. A. Shuman, and E. Bohl. 1995. The inhibition of maltose transport by the unliganded form of the maltose-binding protein of Escherichia coli: experimental findings and mathematical treatment. J. Theor. Biol. 177:171-179.
    • (1995) J. Theor. Biol. , vol.177 , pp. 171-179
    • Merino, G.1    Boos, W.2    Shuman, H.A.3    Bohl, E.4
  • 159
    • 0031939756 scopus 로고    scopus 로고
    • Truncation of MalF results in lactose transport via the maltose transport system of Escherichia coli
    • in press
    • Merino, G., and H. A. Shuman. Truncation of MalF results in lactose transport via the maltose transport system of Escherichia coli. J. Biol. Chem., in press.
    • J. Biol. Chem.
    • Merino, G.1    Shuman, H.A.2
  • 160
    • 0030736861 scopus 로고    scopus 로고
    • Unliganded maltose-binding protein triggers lactose transport in an Escherichia coli mutant with an alteration in the maltose transport system
    • Merino, G., and H. A. Shuman. 1997. Unliganded maltose-binding protein triggers lactose transport in an Escherichia coli mutant with an alteration in the maltose transport system. J. Bacteriol. 179:7687-7694.
    • (1997) J. Bacteriol. , vol.179 , pp. 7687-7694
    • Merino, G.1    Shuman, H.A.2
  • 162
    • 0031557404 scopus 로고    scopus 로고
    • Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside
    • Meyer, J. E. W., M. Hofnung, and G. E. Schulz. 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
  • 163
    • 0022365856 scopus 로고
    • Characterization and expression of the structural gene for pullulanase, a maltose-inducible secreted protein of Klebsiella pneumoniae
    • Michaelis, S., C. Chapon, C. D'Enfert, A. P. Pugsley, and M. Schwartz. 1985. Characterization and expression of the structural gene for pullulanase, a maltose-inducible secreted protein of Klebsiella pneumoniae. J. Bacteriol. 164:633-638.
    • (1985) J. Bacteriol. , vol.164 , pp. 633-638
    • Michaelis, S.1    Chapon, C.2    D'Enfert, C.3    Pugsley, A.P.4    Schwartz, M.5
  • 164
    • 0025804026 scopus 로고
    • Isolation and characterization of visible light-sensitive mutants of Escherichia coli K12
    • Miyamoto, K., K. Nakahigashi, K. Nishimura, and H. Inokuchi. 1991. Isolation and characterization of visible light-sensitive mutants of Escherichia coli K12. J. Mol. Biol. 219:393-398.
    • (1991) J. Mol. Biol. , vol.219 , pp. 393-398
    • Miyamoto, K.1    Nakahigashi, K.2    Nishimura, K.3    Inokuchi, H.4
  • 166
    • 0027272354 scopus 로고
    • The ATP-binding cassette (ABC) transporter for maltose/maltodextrins of Salmonella typhimurium. Characterization of the ATPase activity associated with the purified MalK subunit
    • Morbath, S., S. Tebbe, and E. Schneider. 1993. The ATP-binding cassette (ABC) transporter for maltose/maltodextrins of Salmonella typhimurium. Characterization of the ATPase activity associated with the purified MalK subunit. J. Biol. Chem. 268:18617-18621.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18617-18621
    • Morbath, S.1    Tebbe, S.2    Schneider, E.3
  • 167
    • 0030910930 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: A conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits
    • Mourez, M., N. Hofnung, and E. Dassa. 1997. Subunit interactions in ABC transporters: a conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits. EMBO J. 16:3066-3077.
    • (1997) EMBO J. , vol.16 , pp. 3066-3077
    • Mourez, M.1    Hofnung, N.2    Dassa, E.3
  • 168
    • 0030976040 scopus 로고    scopus 로고
    • Regulation of gene expression by represser localization: Biochemical evidence that membrane and DNA binding by the PutA protein are mutually exclusive
    • Muro-Pastor, A. M., P. Ostrovsky, and S. Maloy. 1997. Regulation of gene expression by represser localization: biochemical evidence that membrane and DNA binding by the PutA protein are mutually exclusive. J. Bacteriol. 179:2788-2791.
    • (1997) J. Bacteriol. , vol.179 , pp. 2788-2791
    • Muro-Pastor, A.M.1    Ostrovsky, P.2    Maloy, S.3
  • 169
    • 0001175878 scopus 로고    scopus 로고
    • Export of proteins to the cell envelope in Escherichia coli
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D.C.
    • Murphy, C. K., and J. Beckwith. 1996. Export of proteins to the cell envelope in Escherichia coli. p. 967-978. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. American Society for Microbiology, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , pp. 967-978
    • Murphy, C.K.1    Beckwith, J.2
  • 170
    • 0027374109 scopus 로고
    • Control and function of lysyl-tRNA synthase: Diversity and coordination
    • Nakamura, Y., and K. Ito. 1993. Control and function of lysyl-tRNA synthase: diversity and coordination. Mol. Microbiol. 10:225-231.
    • (1993) Mol. Microbiol. , vol.10 , pp. 225-231
    • Nakamura, Y.1    Ito, K.2
  • 171
    • 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., C. Andersen, and R. Benz. 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. 66:1388-1397.
    • (1994) Biophys. J. , vol.66 , pp. 1388-1397
    • Nekolla, S.1    Andersen, C.2    Benz, R.3
  • 172
    • 0028357471 scopus 로고
    • Mechanism of maltose uptake and glucose excretion in Lactohacillus sanfrancisco
    • Neubauer, H., E. Glaasker, W. P. Hammes, B. Fuolmaa, and W. N. Konings. 1994. Mechanism of maltose uptake and glucose excretion in Lactohacillus sanfrancisco. J. Bacteriol. 176:3007-3012.
    • (1994) J. Bacteriol. , vol.176 , pp. 3007-3012
    • Neubauer, H.1    Glaasker, E.2    Hammes, W.P.3    Fuolmaa, B.4    Konings, W.N.5
  • 173
    • 0009481844 scopus 로고
    • Maltose transport system of Escherichia coli as a member of ABC
    • A. Torriani, E. Yagil, and S. Silver (ed.), American Society for Microbiology, Washington, D.C.
    • Nikaido, H., I. D. Pokrovskaya, L. Reyes, A. K. Ganesan, and J. A. Hall. 1994. Maltose transport system of Escherichia coli as a member of ABC transporters, p. 91-96. In A. Torriani, E. Yagil, and S. Silver (ed.), Phosphate in microorganisms: cellular and molecular biology. American Society for Microbiology, Washington, D.C.
    • (1994) Phosphate in Microorganisms: Cellular and Molecular Biology , pp. 91-96
    • Nikaido, H.1    Pokrovskaya, I.D.2    Reyes, L.3    Ganesan, A.K.4    Hall, J.A.5
  • 174
    • 0028932110 scopus 로고
    • Differential expression of mal genes under cAMP and endogenous inducer control in nutrient-stressed Escherichia coli
    • Notley, L., and T. Ferenci. 1995. Differential expression of mal genes under cAMP and endogenous inducer control in nutrient-stressed Escherichia coli. Mol. Microbiol. 16:121-129.
    • (1995) Mol. Microbiol. , vol.16 , pp. 121-129
    • Notley, L.1    Ferenci, T.2
  • 175
    • 0031030202 scopus 로고    scopus 로고
    • Thermodynamics of maltose binding protein unfolding
    • Novokhatny, V., and K. Ingham. 1997. Thermodynamics of maltose binding protein unfolding. Protein Sci. 6:141-146.
    • (1997) Protein Sci. , vol.6 , pp. 141-146
    • Novokhatny, V.1    Ingham, K.2
  • 176
    • 0019468906 scopus 로고
    • Biosynthesis of bacterial glycogen: Cloning of the glycogen enzyme structural genes of Escherichia coli
    • Okita, T. W., R. L. Rodriguez, and J. Preiss. 1981. Biosynthesis of bacterial glycogen: cloning of the glycogen enzyme structural genes of Escherichia coli. J. Biol. Chem. 256:6944-6952.
    • (1981) J. Biol. Chem. , vol.256 , pp. 6944-6952
    • Okita, T.W.1    Rodriguez, R.L.2    Preiss, J.3
  • 177
    • 0030890246 scopus 로고    scopus 로고
    • Oligosaccharide substrate binding in Escherichia coli maltodextrin phosphorylase
    • O'Reilly, M., K. A. Watson, R. Schinzel, D. Palm, and L. N. Johnson. 1997. Oligosaccharide substrate binding in Escherichia coli maltodextrin phosphorylase. Nat. Struct. Biol. 4:405-412.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 405-412
    • O'Reilly, M.1    Watson, K.A.2    Schinzel, R.3    Palm, D.4    Johnson, L.N.5
  • 178
    • 0024120551 scopus 로고
    • Nucleotide sequence of the ugp genes of Escherichia coli K-12: Homology to the maltose system
    • Overduin, P., W. Boos, and J. Tommassen. 1988. Nucleotide sequence of the ugp genes of Escherichia coli K-12: homology to the maltose system. Mol. Microbiol. 2:767-775.
    • (1988) Mol. Microbiol. , vol.2 , pp. 767-775
    • Overduin, P.1    Boos, W.2    Tommassen, J.3
  • 179
    • 2642709582 scopus 로고    scopus 로고
    • 1997. Unpublished observations
    • Pajatsch, M., and A. Bock. 1997. Unpublished observations.
    • Pajatsch, M.1    Bock, A.2
  • 181
    • 0021964124 scopus 로고
    • Evolution of catalytic and regulatory sites in phosphorylases
    • Palm, D., R. Goerl, and K. J. Burger. 1985. Evolution of catalytic and regulatory sites in phosphorylases. Nature 313:500-502.
    • (1985) Nature , vol.313 , pp. 500-502
    • Palm, D.1    Goerl, R.2    Burger, K.J.3
  • 182
    • 0017082211 scopus 로고
    • The action pattern of amylomaltase from Escherichia coli
    • Palmer, N. T., B. E. Ryman, and W. J. Whelan. 1976. The action pattern of amylomaltase from Escherichia coli. Eur. J. Biochem. 69:105-115.
    • (1976) Eur. J. Biochem. , vol.69 , pp. 105-115
    • Palmer, N.T.1    Ryman, B.E.2    Whelan, W.J.3
  • 184
    • 0027375813 scopus 로고
    • Characterization of the structural requirements for assembly and nucleotide binding of an ATP-binding cassette transporter-the maltose transport system of Escherichia coli
    • Panagiotidis, C. H., M. Reyes, A. Sievertsen, W. Boos, and H. A. Shuman. 1993. Characterization of the structural requirements for assembly and nucleotide binding of an ATP-binding cassette transporter-the maltose transport system of Escherichia coli. J. Biol. Chem. 268:23685-23696.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23685-23696
    • Panagiotidis, C.H.1    Reyes, M.2    Sievertsen, A.3    Boos, W.4    Shuman, H.A.5
  • 185
    • 17544372725 scopus 로고    scopus 로고
    • The MalT-dependent and malZ-encoded maltodextrin glucosidase of Escherichia coli can be converted into a dextrinyltransferase by a single mutation
    • Peist, R., C. Schneider-Fresenius, and W. Boos. 1996. The MalT-dependent and malZ-encoded maltodextrin glucosidase of Escherichia coli can be converted into a dextrinyltransferase by a single mutation. J. Biol. Chem. 271:10681-10689.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10681-10689
    • Peist, R.1    Schneider-Fresenius, C.2    Boos, W.3
  • 186
    • 0030781626 scopus 로고    scopus 로고
    • Characterization of the aes gene of Escherichia coli encoding an enzyme with esterase activity
    • Peist, R., A. Koch, P. Bolek, T. Kolbus, and W. Boos. 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    Kolbus, T.4    Boos, W.5
  • 187
    • 0024327471 scopus 로고
    • Regulation of Escherichia coli adenylate cyclase activity by the phosphoenolpyruvate:sugar phosphotransferase system
    • Peterkofsky, A., I. Svenson, and N. Amin. 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
  • 188
    • 0029145921 scopus 로고
    • Co-ordinated regulation of amino sugar biosynthesis and degradation: The NagC repressor acts as both an activator and a repressor for the transcription of the glmUS operon and requires two separated NagC binding sites
    • Plumbridge, J. 1995. Co-ordinated regulation of amino sugar biosynthesis and degradation: the NagC repressor acts as both an activator and a repressor for the transcription of the glmUS operon and requires two separated NagC binding sites. EMBO J. 14:3958-3965.
    • (1995) EMBO J. , vol.14 , pp. 3958-3965
    • Plumbridge, J.1
  • 189
    • 0031973888 scopus 로고    scopus 로고
    • Control of the expression of the manXYZ operon in Escherichia coli: Mlc is a negative regulator of the mannose PTS
    • Plumbridge, J. 1998. Control of the expression of the manXYZ operon in Escherichia coli: Mlc is a negative regulator of the mannose PTS. Mol. Microbiol. 27:369-380.
    • (1998) Mol. Microbiol. , vol.27 , pp. 369-380
    • Plumbridge, J.1
  • 190
    • 0026757347 scopus 로고
    • Structure of the gene encoding cyclomaltodextrinasc from Clostridium thermohydrosulfuricum 39E and characterization of the enzyme purified from Escherichia coli
    • Podkovyrov, S. M., and J. G. Zeikus. 1992. Structure of the gene encoding cyclomaltodextrinasc from Clostridium thermohydrosulfuricum 39E and characterization of the enzyme purified from Escherichia coli. J. Bacteriol. 174:5400-5405.
    • (1992) J. Bacteriol. , vol.174 , pp. 5400-5405
    • Podkovyrov, S.M.1    Zeikus, J.G.2
  • 191
    • 0001014412 scopus 로고    scopus 로고
    • Phosphoenol-pyruvate:carbohydrate phosphotransferase system
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D.C.
    • Postma, P. W., J. W. Lengeler, and G. R. Jacobson. 1996. Phosphoenol-pyruvate:carbohydrate phosphotransferase system, p. 1149-1174. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology. American Society for Microbiology, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 1149-1174
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 192
    • 0025866923 scopus 로고
    • Determination of a region of the HisJ binding protein involved in the recognition of the membrane complex of the histidine transport system of Salmonella typhtmurium
    • Prossnitz, E. 1991. Determination of a region of the HisJ binding protein involved in the recognition of the membrane complex of the histidine transport system of Salmonella typhtmurium. J. Biol. Chem. 266:9673-9677.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9673-9677
    • Prossnitz, E.1
  • 193
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gramnegative bacteria
    • Pugsley, A. P. 1993. The complete general secretory pathway in gramnegative bacteria. Microbiol. Rev. 57:50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 194
    • 0024042231 scopus 로고
    • Molecular characterization of malQ, the structural gene for the Escherichia coli enzyme amylomaltase
    • Pugsley, A. P., and C. Dubreuil. 1988. Molecular characterization of malQ, the structural gene for the Escherichia coli enzyme amylomaltase. Mol. Microbiol. 2:473-479.
    • (1988) Mol. Microbiol. , vol.2 , pp. 473-479
    • Pugsley, A.P.1    Dubreuil, C.2
  • 195
    • 0030976146 scopus 로고    scopus 로고
    • Recent progress and future directions in studies of the main terminal branch of the general secretory pathway in Gram-negative bacteria - A review
    • Pugsley, A. P., O. Francetic, O. M. Possot, N. Sauvonnet, and K. R. Hardie. 1997. Recent progress and future directions in studies of the main terminal branch of the general secretory pathway in Gram-negative bacteria - a review. Gene 192:13-19.
    • (1997) Gene , vol.192 , pp. 13-19
    • Pugsley, A.P.1    Francetic, O.2    Possot, O.M.3    Sauvonnet, N.4    Hardie, K.R.5
  • 196
    • 0027159810 scopus 로고
    • Structure of the maltodextrin-uptake locus of Streptococcus pneumoniae. Correlation to the Escherichia coli maltose regulon
    • Puyet, A., and M. Espinosa. 1993. Structure of the maltodextrin-uptake locus of Streptococcus pneumoniae. Correlation to the Escherichia coli maltose regulon. J. Mol. Biol. 230:800-811.
    • (1993) J. Mol. Biol. , vol.230 , pp. 800-811
    • Puyet, A.1    Espinosa, M.2
  • 197
    • 0031571605 scopus 로고    scopus 로고
    • Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor
    • Quiucho, F. A., J. C. Spurlino, and L. E. Rodseth. 1997. Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor. Structure 5:997-1015.
    • (1997) Structure , vol.5 , pp. 997-1015
    • Quiucho, F.A.1    Spurlino, J.C.2    Rodseth, L.E.3
  • 199
    • 0024633629 scopus 로고
    • Nucleoprotein structures at positively regulated bacterial promoters: Homology with replication origins and some hypotheses on the quaternary structure of the activator proteins in these complexes
    • Raibaud, O. 1989. Nucleoprotein structures at positively regulated bacterial promoters: homology with replication origins and some hypotheses on the quaternary structure of the activator proteins in these complexes. Mol. Microbiol. 3:455-458.
    • (1989) Mol. Microbiol. , vol.3 , pp. 455-458
    • Raibaud, O.1
  • 200
    • 0020540489 scopus 로고
    • Use of deletions created in vitro to map transcriptional regulatory signals in the malA region of Escherichia coli
    • Raibaud, O., M. Débarbouillé, and M. Schwartz. 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
  • 201
    • 0021957946 scopus 로고
    • Essential and nonessential sequences in malPp, a positively controlled promoter in Escherichia coli
    • Raibaud, O., C. Gutierrez, and M. Schwartz. 1985. Essential and nonessential sequences in malPp, a positively controlled promoter in Escherichia coli. J. Bacteriol. 161:1201-1208.
    • (1985) J. Bacteriol. , vol.161 , pp. 1201-1208
    • Raibaud, O.1    Gutierrez, C.2    Schwartz, M.3
  • 202
    • 0023192487 scopus 로고
    • Maltotriose is the inducer of the maltose regulon
    • Raibaud, O., and E. Richel. 1987. Maltotriose is the inducer of the maltose regulon. J. Bacteriol. 169:3059-3061.
    • (1987) J. Bacteriol. , vol.169 , pp. 3059-3061
    • Raibaud, O.1    Richel, E.2
  • 203
    • 0018307240 scopus 로고
    • Structure of the malB region in Escherichia coli K.12. I. Genetic map of the malK-lamB operon
    • Raibaud, O., M. Roa, C. Braun-Breton, and M. Schwartz. 1979. Structure of the malB region in Escherichia coli K.12. I. Genetic map of the malK-lamB operon. Mol. Gen. Genet. 174:241-248.
    • (1979) Mol. Gen. Genet. , vol.174 , pp. 241-248
    • Raibaud, O.1    Roa, M.2    Braun-Breton, C.3    Schwartz, M.4
  • 204
    • 0018930194 scopus 로고
    • Restriction map of the Escherichia coli malA region and identification of the malT product
    • Raibaud, O., and M. Schwartz. 1980. Restriction map of the Escherichia coli malA region and identification of the malT product. J. Bacteriol. 143:761-771.
    • (1980) J. Bacteriol. , vol.143 , pp. 761-771
    • Raibaud, O.1    Schwartz, M.2
  • 205
    • 0026329253 scopus 로고
    • Genetic studies on the promoter of malT, the gene that encodes the activator of the Escherichia coli maltose regulon
    • Raibaud, O., D. Vidal-Ingigliardi, and A. Kolb. 1991. Genetic studies on the promoter of malT, the gene that encodes the activator of the Escherichia coli maltose regulon. Res. Microbiol. 142:937-942.
    • (1991) Res. Microbiol. , vol.142 , pp. 937-942
    • Raibaud, O.1    Vidal-Ingigliardi, D.2    Kolb, A.3
  • 206
    • 0024594574 scopus 로고
    • A complex nucleoprotein structure involved in activation of transcription of two divergent Escherichia coli promoters
    • Raibaud, O., D. Vidal-Ingigliardi, and E. Riebet. 1989. A complex nucleoprotein structure involved in activation of transcription of two divergent Escherichia coli promoters. J. Mol. Biol. 205:471-485.
    • (1989) J. Mol. Biol. , vol.205 , pp. 471-485
    • Raibaud, O.1    Vidal-Ingigliardi, D.2    Riebet, E.3
  • 207
    • 0015713398 scopus 로고
    • Isolation of the bacteriophage lambda receptor from Escherichia coli
    • Randall-Hazelbauer, L., and M. Schwartz. 1973. Isolation of the bacteriophage lambda receptor from Escherichia coli. J. Bacteriol. 116:1436-1446.
    • (1973) J. Bacteriol. , vol.116 , pp. 1436-1446
    • Randall-Hazelbauer, L.1    Schwartz, M.2
  • 208
    • 0025848324 scopus 로고
    • The malX malY operon of Escherichia coli encodes a novel enzyme II of the phosphotransferase system recognizing glucose and maltose and an enzyme abolishing the endogenous induction of the maltose system
    • Reidl, J., and W. Boos. 1991. The malX malY operon of Escherichia coli encodes a novel enzyme II of the phosphotransferase system recognizing glucose and maltose and an enzyme abolishing the endogenous induction of the maltose system. J. Bacteriol. 173:4862-4876.
    • (1991) J. Bacteriol. , vol.173 , pp. 4862-4876
    • Reidl, J.1    Boos, W.2
  • 209
    • 0024729941 scopus 로고
    • MalI, a novel protein involved in regulation of the maltose system of Escherichia coli, is highly homologous to the represser proteins GalR, CytR, and LacI
    • Reidl, J., K. Römisch, M. Ehrmann, and W. Boos. 1989. MalI, a novel protein involved in regulation of the maltose system of Escherichia coli, is highly homologous to the represser proteins GalR, CytR, and LacI. J. Bacteriol. 171:4888-4899.
    • (1989) J. Bacteriol. , vol.171 , pp. 4888-4899
    • Reidl, J.1    Römisch, K.2    Ehrmann, M.3    Boos, W.4
  • 210
    • 0024095619 scopus 로고
    • Overproduction of MalK protein prevents expression of the Escherichia coli mal regulon
    • Reyes, M., and H. A. Shuman. 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
  • 211
    • 0022456176 scopus 로고
    • Transport of p-nitrophenyl-α-maltoside by the maltose transport system of Escherichia coli and its subsequent hydrolysis by a cytoplasmic maltosidase
    • Reyes, M., N. A. Treptow, and H. A. Shuman. 1986. Transport of p-nitrophenyl-α-maltoside by the maltose transport system of Escherichia coli and its subsequent hydrolysis by a cytoplasmic maltosidase. J. Bacteriol. 165: 918-922.
    • (1986) J. Bacteriol. , vol.165 , pp. 918-922
    • Reyes, M.1    Treptow, N.A.2    Shuman, H.A.3
  • 212
    • 0031004715 scopus 로고    scopus 로고
    • Chaperone properties of the bacterial periplasmic substrate-binding proteins
    • Richarme, G., and T. D. Caldas. 1997. Chaperone properties of the bacterial periplasmic substrate-binding proteins. J. Biol. Chem. 272:15607-15612.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15607-15612
    • Richarme, G.1    Caldas, T.D.2
  • 213
    • 0030596146 scopus 로고    scopus 로고
    • On the role of the multiple regulatory elements involved in the activation of the Escherichia coli malEp promoter
    • Riebet, 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
    • Riebet, E.1
  • 214
    • 0023656085 scopus 로고
    • Purification and properties of the MalT protein, the transcription activator of the Escherichia coli maltose regulon
    • Richet, E., and O. Raibaud. 1987. Purification and properties of the MalT protein, the transcription activator of the Escherichia coli maltose regulon. J. Biol. Chem. 262:12647-12653.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12647-12653
    • Richet, E.1    Raibaud, O.2
  • 215
    • 0024424649 scopus 로고
    • MalT, the regulatory protein of the Escherichia coli maltose system, is an ATP-dependent transcriptional activator
    • Richet, E., and O. Raibaud. 1989. MalT, the regulatory protein of the Escherichia coli maltose system, is an ATP-dependent transcriptional activator. EMBO J. 8:981-987.
    • (1989) EMBO J. , vol.8 , pp. 981-987
    • Richet, E.1    Raibaud, O.2
  • 216
    • 0025736729 scopus 로고
    • Supercoiling is essential for the formation and stability of the initiation complex at the divergent malEp and malKp promoters
    • Richer, E., and O. Raibaud. 1991. Supercoiling is essential for the formation and stability of the initiation complex at the divergent malEp and malKp promoters. J. Mol. Biol. 218:529-542.
    • (1991) J. Mol. Biol. , vol.218 , pp. 529-542
    • Richer, E.1    Raibaud, O.2
  • 217
    • 0027983641 scopus 로고
    • CRP induces the repositioning of MalT at the Escherichia coli malKp promoter primarily through DNA bending
    • Richet, E., and L. Søgaard-Andersen. 1994. CRP induces the repositioning of MalT at the Escherichia coli malKp promoter primarily through DNA bending. EMBO J. 13:4558-4567.
    • (1994) EMBO J. , vol.13 , pp. 4558-4567
    • Richet, E.1    Søgaard-Andersen, L.2
  • 218
    • 0025886425 scopus 로고
    • A new mechanism for coactivation of transcription initiation: Repositioning of an activator triggered by the binding of a second activator
    • Riebet, E., D. Vidal-Ingigliardi, and O. Raibaud. 1991. A new mechanism for coactivation of transcription initiation: repositioning of an activator triggered by the binding of a second activator. Cell 66:1185-1195.
    • (1991) Cell , vol.66 , pp. 1185-1195
    • Riebet, E.1    Vidal-Ingigliardi, D.2    Raibaud, O.3
  • 219
    • 0028061196 scopus 로고
    • Trehalose-6-phosphate hydrolase of Escherichia coli
    • Rimmele, M., and W. Boos. 1994. Trehalose-6-phosphate hydrolase of Escherichia coli. J. Bacteriol. 176:5654-5664.
    • (1994) J. Bacteriol. , vol.176 , pp. 5654-5664
    • Rimmele, M.1    Boos, W.2
  • 220
    • 0018366726 scopus 로고
    • New maltose blue mutations in Escherichia coli K-12
    • Roehl, R. A., and R. T. Vinopal. 1979. New maltose blue mutations in Escherichia coli K-12. J. Bacteriol. 139:683-685.
    • (1979) J. Bacteriol. , vol.139 , pp. 683-685
    • Roehl, R.A.1    Vinopal, R.T.2
  • 221
    • 0023792288 scopus 로고
    • Analysis of the Escherichia coli glycogen gene cluster suggests that catabolic enzymes are encoded among the biosynthetic genes
    • Romeo, T., A. Kumar, and J. Preiss. 1988. Analysis of the Escherichia coli glycogen gene cluster suggests that catabolic enzymes are encoded among the biosynthetic genes. Gene 70:363-376.
    • (1988) Gene , vol.70 , pp. 363-376
    • Romeo, T.1    Kumar, A.2    Preiss, J.3
  • 222
    • 0022976924 scopus 로고
    • malM, a new gene of the maltose regulon in Escherichia coli K12. II. Mutations affecting the signal peptide of the MalM protein
    • Kousset, J.-P., E. Gilson, and M. Hofnung. 1986. malM, a new gene of the maltose regulon in Escherichia coli K12. II. Mutations affecting the signal peptide of the MalM protein. J. Mol. Biol. 191:313-320.
    • (1986) J. Mol. Biol. , vol.191 , pp. 313-320
    • Kousset, J.-P.1    Gilson, E.2    Hofnung, M.3
  • 223
    • 0030476750 scopus 로고    scopus 로고
    • SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins
    • Rouvière, P. E., and C. A. Gross. 1996. SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins. Genes Dev. 10:3170-3182.
    • (1996) Genes Dev. , vol.10 , pp. 3170-3182
    • Rouvière, P.E.1    Gross, C.A.2
  • 224
    • 0026333013 scopus 로고
    • EnvZ controls the concentration of phosphorylated OmpR to mediate osmoregulation of the porin genes
    • Russo, F. D., and T. J. Silhavy. 1991. EnvZ controls the concentration of phosphorylated OmpR to mediate osmoregulation of the porin genes. J. Mol. Biol. 222:567-580.
    • (1991) J. Mol. Biol. , vol.222 , pp. 567-580
    • Russo, F.D.1    Silhavy, T.J.2
  • 225
    • 0030039646 scopus 로고    scopus 로고
    • Molecular analysis of the amy gene locus of Thermoanaerobacterium thermosulfurigenes EM1 encoding starch-degrading enzymes and a binding protein-dependent maltose transport system
    • Sahm, K., M. Matuschek, H. Müller, W. J. Mitchell, and H. Bahl. 1996. Molecular analysis of the amy gene locus of Thermoanaerobacterium thermosulfurigenes EM1 encoding starch-degrading enzymes and a binding protein-dependent maltose transport system. J. Bacteriol. 178:1039-1046.
    • (1996) J. Bacteriol. , vol.178 , pp. 1039-1046
    • Sahm, K.1    Matuschek, M.2    Müller, H.3    Mitchell, W.J.4    Bahl, H.5
  • 226
    • 0031031878 scopus 로고    scopus 로고
    • Crystal structure of a recombinant form of the maltodextrin-binding protein carrying an inserted sequence of a B-cell epitope from the preS2 region of hepatitis B virus
    • Saal, F. A., B. Vulliez-le Normand, F. Lema, and G. A. Bentley. 1997. Crystal structure of a recombinant form of the maltodextrin-binding protein carrying an inserted sequence of a B-cell epitope from the preS2 region of hepatitis B virus. Protein Struct. Fund. Genet. 27:1-8.
    • (1997) Protein Struct. Fund. Genet. , vol.27 , pp. 1-8
    • Saal, F.A.1    Vulliez-le Normand, B.2    Lema, F.3    Bentley, G.A.4
  • 227
    • 0028215587 scopus 로고
    • Sequence relationships between integral inner membrane proteins of binding protein-dependent transport systems-evolution by recurrent gene duplications
    • Saurin, W., and E. Dassa. 1994. Sequence relationships between integral inner membrane proteins of binding protein-dependent transport systems-evolution by recurrent gene duplications. Protein Sci. 3:325-344.
    • (1994) Protein Sci. , vol.3 , pp. 325-344
    • Saurin, W.1    Dassa, E.2
  • 228
    • 0028240216 scopus 로고
    • Bacterial binding protein-dependent permeases: Characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins
    • Saurin, W., W. Köster, and E. Dassa. 1994. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 12:993-1004.
    • (1994) Mol. Microbiol. , vol.12 , pp. 993-1004
    • Saurin, W.1    Köster, W.2    Dassa, E.3
  • 229
    • 0025154906 scopus 로고
    • Escherichia coli maltodextrin phosphorylase: Contribution of active site residues glutamate-637 and tyrosine-538 to the phosphorolytic cleavage of α-glucans
    • Schinzel, R., and D. Palm. 1990. Escherichia coli maltodextrin phosphorylase: contribution of active site residues glutamate-637 and tyrosine-538 to the phosphorolytic cleavage of α-glucans. Biochemistry 29:9956-9962.
    • (1990) Biochemistry , vol.29 , pp. 9956-9962
    • Schinzel, R.1    Palm, D.2
  • 230
    • 0027161268 scopus 로고
    • Prediction of membrane spanning β-strands and its application to maltoporin
    • Schirmer, T., and S. W. Cowan. 1993. Prediction of membrane spanning β-strands and its application to maltoporin. Protein Sci. 2:1361-1363.
    • (1993) Protein Sci. , vol.2 , pp. 1361-1363
    • Schirmer, T.1    Cowan, S.W.2
  • 231
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution
    • Schirmer, T., T. A. Keller, Y. F. Wang, and J. P. Rosenbusch. 1995. Structural basis for sugar translocation through 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
  • 232
    • 0000625461 scopus 로고    scopus 로고
    • Two positively regulated systems, ara and mal
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D.C.
    • Schleif, R. 1996. Two positively regulated systems, ara and mal, p. 1300-1309. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. American Society for Microbiology, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , pp. 1300-1309
    • Schleif, R.1
  • 233
    • 0030896572 scopus 로고    scopus 로고
    • The Streptomyces ATP-binding component MsiK assists in cellobiose and maltose transport
    • Schlösser, A., T. Kampers, and H. Schrempf. 1997. The Streptomyces ATP-binding component MsiK assists in cellobiose and maltose transport. J. Bacteriol. 179:2092-2095.
    • (1997) J. Bacteriol. , vol.179 , pp. 2092-2095
    • Schlösser, A.1    Kampers, T.2    Schrempf, H.3
  • 234
    • 0026544212 scopus 로고
    • Completion of the nucleotide sequence of the 'maltose B' region in Salmonella typhimuriurn: The high conservation of the malM gene suggests a selected physiological role for its product
    • Schneider, E., E. Francoz, and E. Dassa. 1992. Completion of the nucleotide sequence of the 'maltose B' region in Salmonella typhimuriurn: the high conservation of the malM gene suggests a selected physiological role for its product. Biochim. Biophys. Acta 1129:223-227.
    • (1992) Biochim. Biophys. Acta , vol.1129 , pp. 223-227
    • Schneider, E.1    Francoz, E.2    Dassa, E.3
  • 235
    • 0026703159 scopus 로고
    • Molecular characterization of the MalT-dependent periplasmic α-amylase of Escherichia coli encoded by malS
    • Schneider, E., S. Freundlieb, S. Tapio, and W. Boos. 1992. Molecular characterization of the MalT-dependent periplasmic α-amylase of Escherichia coli encoded by malS. J. Biol. Chem. 267:5148-5154.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5148-5154
    • Schneider, E.1    Freundlieb, S.2    Tapio, S.3    Boos, W.4
  • 236
    • 0029092262 scopus 로고
    • The MalK protein of the ATP-binding cassette transporter for maltose of Escherichia coli is accessible to protease digestion from the periplasmic side of the membrane
    • Schneider, E., S. Hunke, and S. Tebbe. 1995. The MalK protein of the ATP-binding cassette transporter for maltose of Escherichia coli is accessible to protease digestion from the periplasmic side of the membrane. J. Bacteriol. 177:5364-5367.
    • (1995) J. Bacteriol. , vol.177 , pp. 5364-5367
    • Schneider, E.1    Hunke, S.2    Tebbe, S.3
  • 237
    • 0025740666 scopus 로고
    • A chimeric nucleotide-binding protein, encoded by a hisP-malK hybrid gene, is functional in maltose transport in Salmonella typhimurium
    • Schneider, E., and C. Walter. 1991. A chimeric nucleotide-binding protein, encoded by a hisP-malK hybrid gene, is functional in maltose transport in Salmonella typhimurium. Mol. Microbiol. 5:1375-1383.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1375-1383
    • Schneider, E.1    Walter, C.2
  • 238
    • 78651190596 scopus 로고
    • Aspects biochimiques et génétiques du metabolisme du maltose chez Escherichia coli K12
    • Schwartz, M. 1965. Aspects biochimiques et génétiques du metabolisme du maltose chez Escherichia coli K12. C R. Acad. Sci. 260:2613-2616.
    • (1965) C R. Acad. Sci. , vol.260 , pp. 2613-2616
    • Schwartz, M.1
  • 239
    • 0014096234 scopus 로고
    • Phenotypic expression and genetic localization of mutations affecting maltose metabolism in Escherichia coli K 12
    • Schwartz, M. 1967. Phenotypic expression and genetic localization of mutations affecting maltose metabolism in Escherichia coli K 12. Ann. Inst. Pasteur (Paris) 112:673-698.
    • (1967) Ann. Inst. Pasteur (Paris) , vol.112 , pp. 673-698
    • Schwartz, M.1
  • 240
    • 0014149432 scopus 로고
    • Sur l'existence chez Escherichia coli K12 d'une régulation commune à la biosynthèse des récepteurs du bacteriophage λ et au métabolisme du maltose
    • Schwartz, M. 1967. Sur l'existence chez Escherichia coli K12 d'une régulation commune à la biosynthèse des récepteurs du bacteriophage λ et au métabolisme du maltose. Ann. Inst. Pasteur (Paris) 113:687-704.
    • (1967) Ann. Inst. Pasteur (Paris) , vol.113 , pp. 687-704
    • Schwartz, M.1
  • 241
    • 0000706936 scopus 로고
    • The maltose regulon
    • F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D.C.
    • Schwartz, M. 1987. The maltose regulon, p. 1482-1502. In F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology. American Society for Microbiology, Washington, D.C.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 1482-1502
    • Schwartz, M.1
  • 242
    • 0014133549 scopus 로고
    • La maltodextrin phosphorylase d'Escherichia coli
    • Schwartz, M., and M. Hofnung. 1967. La maltodextrin phosphorylase d'Escherichia coli. Eur. J. Biochem. 2:132-145.
    • (1967) Eur. J. Biochem. , vol.2 , pp. 132-145
    • Schwartz, M.1    Hofnung, M.2
  • 243
    • 0027364214 scopus 로고
    • Refined 1.8-Å structure reveals the mode of binding of β-cyclodextrin to the maltodextrin binding protein
    • Sharff, A. J., L. F. Rodseth, and F. A. Quiocho. 1993. Refined 1.8-Å structure reveals the mode of binding of β-cyclodextrin to the maltodextrin binding protein. Biochemistry 32:10553-10559.
    • (1993) Biochemistry , vol.32 , pp. 10553-10559
    • Sharff, A.J.1    Rodseth, L.F.2    Quiocho, F.A.3
  • 244
    • 0026493924 scopus 로고
    • Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis
    • Sharff, A. J., L. E. Rodseth, J. C. Spurlino, and F. A. Quiocho. 1992. Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis. Biochemistry 31:10657-10663.
    • (1992) Biochemistry , vol.31 , pp. 10657-10663
    • Sharff, A.J.1    Rodseth, L.E.2    Spurlino, J.C.3    Quiocho, F.A.4
  • 245
    • 0028956297 scopus 로고
    • Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein
    • Sharff, A. J., L. E. Rodseth, S. Szmelcman, M. Hofnung, and F. A. Quiocho. 1995. Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein. J. Mol. Biol. 246:8-13.
    • (1995) J. Mol. Biol. , vol.246 , pp. 8-13
    • Sharff, A.J.1    Rodseth, L.E.2    Szmelcman, S.3    Hofnung, M.4    Quiocho, F.A.5
  • 246
    • 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 W. Boos. 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
  • 247
    • 0030606240 scopus 로고    scopus 로고
    • Conformational changes of three periplasmic receptors for bacterial chemotaxis and transport: The maltose-, glucose/galactose- And ribose-binding proteins
    • Shilton, B. H., M. M. Flocco, M. Nilsson, and S. L. Mowbray. 1996. Conformational changes of three periplasmic receptors for bacterial chemotaxis and transport: the maltose-, glucose/galactose- and ribose-binding proteins. J. Mol. Biol. 264:350-363.
    • (1996) J. Mol. Biol. , vol.264 , pp. 350-363
    • Shilton, B.H.1    Flocco, M.M.2    Nilsson, M.3    Mowbray, S.L.4
  • 248
    • 0030606256 scopus 로고    scopus 로고
    • Crystal structures and solution conformations of a dominant-negative mutant of Escherichia coli maltose-binding protein
    • Shilton, B. H., H. A. Shuman, and S. L. Mowbray. 1996. Crystal structures and solution conformations of a dominant-negative mutant of Escherichia coli maltose-binding protein. J. Mol. Biol. 264:364-376.
    • (1996) J. Mol. Biol. , vol.264 , pp. 364-376
    • Shilton, B.H.1    Shuman, H.A.2    Mowbray, S.L.3
  • 249
    • 0020320406 scopus 로고
    • Active transport of maltose in Escherichia coli K12. Role of the periplasmic maltose-binding protein and evidence for a substrate recognition site in the cytoplasmic membrane
    • Shuman, H. A. 1982. Active transport of maltose in Escherichia coli K12. Role of the periplasmic maltose-binding protein and evidence for a substrate recognition site in the cytoplasmic membrane. J. Biol. Chem. 257: 5455-5461.
    • (1982) J. Biol. Chem. , vol.257 , pp. 5455-5461
    • Shuman, H.A.1
  • 250
    • 0027763278 scopus 로고
    • Tinkering with transporters: Periplasmic binding protein-dependent maltose transport in Escherichia coli
    • Shuman, H. A., and C. H. Panagiotidis. 1993. Tinkering with transporters: periplasmic binding protein-dependent maltose transport in Escherichia coli. J. Bioenerg, Biomembr. 25:613-620.
    • (1993) J. Bioenerg, Biomembr. , vol.25 , pp. 613-620
    • Shuman, H.A.1    Panagiotidis, C.H.2
  • 251
    • 0019464719 scopus 로고
    • Identification of the malK gene product. A peripheral membrane component of the Escherichia coli maltose transport system
    • Shuman, H. A., and T. J. Silhavy. 1981. Identification of the malK gene product. A peripheral membrane component of the Escherichia coli maltose transport system. J. Biol. Chem. 256:560-562.
    • (1981) J. Biol. Chem. , vol.256 , pp. 560-562
    • Shuman, H.A.1    Silhavy, T.J.2
  • 252
    • 0018879284 scopus 로고
    • Labeling of proteins with β-galactosidase by gene fusion. Identification of a cytoplasmic membrane component of the Escherichia coli maltose transport system
    • Shuman, H. A., T. J. Silhavy, and J. R. Beckwith. 1980. Labeling of proteins with β-galactosidase by gene fusion. Identification of a cytoplasmic membrane component of the Escherichia coli maltose transport system. J. Biol. Chem. 255:168-174.
    • (1980) J. Biol. Chem. , vol.255 , pp. 168-174
    • Shuman, H.A.1    Silhavy, T.J.2    Beckwith, J.R.3
  • 253
    • 0017163756 scopus 로고
    • Periplasmic protein related to the sn-glycerol-3-phosphate transport system of Escherichia coli
    • Silhavy, T. J., I. Hartig-Beecken, and W. Boos. 1976. Periplasmic protein related to the sn-glycerol-3-phosphate transport system of Escherichia coli. J. Bacteriol. 126:951-958.
    • (1976) J. Bacteriol. , vol.126 , pp. 951-958
    • Silhavy, T.J.1    Hartig-Beecken, I.2    Boos, W.3
  • 255
    • 0001794959 scopus 로고    scopus 로고
    • The porin regulon: A paradigm for the two-component regulatory system
    • E. C. C. Lin and A. S. Lynch (ed.). R. G. Landes Co., Austin, Tex.
    • Slauch, J. M., and T. J. Silhavy. 1996. The porin regulon: a paradigm for the two-component regulatory system, p. 383-417. In E. C. C. Lin and A. S. Lynch (ed.). Regulation of gene expression in Escherichia coli. R. G. Landes Co., Austin, Tex.
    • (1996) Regulation of Gene Expression in Escherichia Coli , pp. 383-417
    • Slauch, J.M.1    Silhavy, T.J.2
  • 256
    • 0030771489 scopus 로고    scopus 로고
    • Biochemical characterization and mass spectrometric disuifide bond mapping of periplasmic α-amylase of Escherichia coli
    • Spiess, S., H. P. Happersberger, M. O. Glocker, E. Spiess, K. Rippe, and M. Ehnnann. 1997. Biochemical characterization and mass spectrometric disuifide bond mapping of periplasmic α-amylase of Escherichia coli. J. Biol. Chem. 272:22125-22133.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22125-22133
    • Spiess, S.1    Happersberger, H.P.2    Glocker, M.O.3    Spiess, E.4    Rippe, K.5    Ehnnann, M.6
  • 257
    • 0025754301 scopus 로고
    • The 2.3-Å resolution structure of the maltose- Or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis
    • Spurlino, J. C., G.-Y. Lu, and F. A. Quiocho. 1991. The 2.3-Å resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J. Biol. Chem. 266:5202-5219.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5202-5219
    • Spurlino, J.C.1    Lu, G.-Y.2    Quiocho, F.A.3
  • 258
    • 0014409826 scopus 로고
    • Phosphoramidates. VI. Purification and characterization of a phosphoryl transfer enzyme from Escherichia coli
    • Stevens-Clark, J. S., M. C. Theisen, K. A. Conklin, and R. A. Smith. 1968. Phosphoramidates. VI. Purification and characterization of a phosphoryl transfer enzyme from Escherichia coli. J. Biol. Chem. 243:4468-4473.
    • (1968) J. Biol. Chem. , vol.243 , pp. 4468-4473
    • Stevens-Clark, J.S.1    Theisen, M.C.2    Conklin, K.A.3    Smith, R.A.4
  • 260
  • 261
    • 0027486004 scopus 로고
    • Regions of maltose-binding protein that influence SecB-dependent and SecA-dependent export in Escherichia coli
    • Strobel, S. M., J. G. Cannon, and P. J. J. Bassford. 1993. Regions of maltose-binding protein that influence SecB-dependent and SecA-dependent export in Escherichia coli. J. Bacteriol. 175:6988-6995.
    • (1993) J. Bacteriol. , vol.175 , pp. 6988-6995
    • Strobel, S.M.1    Cannon, J.G.2    Bassford, P.J.J.3
  • 262
    • 0021941805 scopus 로고
    • Antisuppressor mutation in Escherichia coli defective in biosynthesis of 5-methylaminomethyl-2-thiouridine
    • Sullivan, M. A., J. F. Cannon, F. H. Webb, and R. M. Bock. 1985. Antisuppressor mutation in Escherichia coli defective in biosynthesis of 5-methylaminomethyl-2-thiouridine. J. Bacteriol. 161:368-376.
    • (1985) J. Bacteriol. , vol.161 , pp. 368-376
    • Sullivan, M.A.1    Cannon, J.F.2    Webb, F.H.3    Bock, R.M.4
  • 263
    • 0016678144 scopus 로고
    • Maltose transport in Escherichia coli K12. Involvement of the bacteriophage lambda receptor
    • Szmelcman, S., and M. Hofnung. 1975. Maltose transport in Escherichia coli K12. Involvement of the bacteriophage lambda receptor. J. Bacteriol. 124:112-118.
    • (1975) J. Bacteriol. , vol.124 , pp. 112-118
    • Szmelcman, S.1    Hofnung, M.2
  • 264
    • 0030995975 scopus 로고    scopus 로고
    • Residues in the α helix 7 of the bacterial maltose binding protein which are important in interactions with the Mal FGK2 complex
    • Szmelcman, S., N. Sassoon, and M. Hofnung. 1997. Residues in the α helix 7 of the bacterial maltose binding protein which are important in interactions with the Mal FGK2 complex. Protein Sci. 6:628-636.
    • (1997) Protein Sci. , vol.6 , pp. 628-636
    • Szmelcman, S.1    Sassoon, N.2    Hofnung, M.3
  • 265
    • 0017127269 scopus 로고
    • Maltose transport in Escherichia coli K.12. A comparison of transport kinetics in wild-type and λ-resistant mutants with the dissociation constants of the maltose binding protein as measured by fluorescence quenching
    • Szmelcman, S., M. Schwartz, T. J. Silhavy, and W. Boos. 1976. Maltose transport in Escherichia coli K.12. A comparison of transport kinetics in wild-type and λ-resistant mutants with the dissociation constants of the maltose binding protein as measured by fluorescence quenching. Eur. J. Biochem. 65:13-19.
    • (1976) Eur. J. Biochem. , vol.65 , pp. 13-19
    • Szmelcman, S.1    Schwartz, M.2    Silhavy, T.J.3    Boos, W.4
  • 267
    • 0025985499 scopus 로고
    • The malZ gene of Escherichia coli, a member of the maltose regulon, encodes a maltodextrin glucosidase
    • Tapio, S., F. Yen, H. A. Shuman, and W. Boos. 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    Yen, F.2    Shuman, H.A.3    Boos, W.4
  • 268
    • 0029040998 scopus 로고
    • Identification of lrp-regulated genes by inverse PCR and sequencing: Regulation of two mal operons of Escherichia coli by leucine-responsive regulatory protein
    • Tchetina, E., and E. B. Newman. 1995. Identification of lrp-regulated genes by inverse PCR and sequencing: regulation of two mal operons of Escherichia coli by leucine-responsive regulatory protein. J. Bacteriol. 177:2679-2683.
    • (1995) J. Bacteriol. , vol.177 , pp. 2679-2683
    • Tchetina, E.1    Newman, E.B.2
  • 269
    • 0022794836 scopus 로고
    • 3-Azi-l-methoxybutyl D-maltooligosaccharides specifically bind to the maltose/maltooligosaccharide-binding protein of Escherichia coli and can be used as photoaffinity labels
    • Thieme, R., H. Lay, A. Oser, J. Lehmann, S. Wrissenberg, and W. Boos. 1986. 3-Azi-l-methoxybutyl D-maltooligosaccharides specifically bind to the maltose/maltooligosaccharide-binding protein of Escherichia coli and can be used as photoaffinity labels. Eur. J. Biochem. 160:83-91.
    • (1986) Eur. J. Biochem. , vol.160 , pp. 83-91
    • Thieme, R.1    Lay, H.2    Oser, A.3    Lehmann, J.4    Wrissenberg, S.5    Boos, W.6
  • 270
    • 0000110242 scopus 로고
    • Regulation of sugar transport and metabolism in lactic acid bacteria
    • Thompson, J. 1987. Regulation of sugar transport and metabolism in lactic acid bacteria. FEMS Microbiol. Rev. 46:221-231.
    • (1987) FEMS Microbiol. Rev. , vol.46 , pp. 221-231
    • Thompson, J.1
  • 271
    • 2642645758 scopus 로고    scopus 로고
    • 1995. Unpublished observations
    • Tommassen, J., and W. Boos. 1995. Unpublished observations.
    • Tommassen, J.1    Boos, W.2
  • 272
    • 0030798169 scopus 로고    scopus 로고
    • Chaperone SecB from Escherichia coli mediates kinetic partitioning via a dynamic equilibrium with its ligands
    • Topping, T. B., and L. L. Randall. 1997. Chaperone SecB from Escherichia coli mediates kinetic partitioning via a dynamic equilibrium with its ligands. J. Biol. Chem. 272:19314-19318.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19314-19318
    • Topping, T.B.1    Randall, L.L.2
  • 273
    • 0022259474 scopus 로고
    • Genetic evidence for substrate and periplasmic binding-protein recognition by MalF and MalG proteins, cytoplasmic membrane components of the Escherichia coli maltose transport system
    • Treptow, N., and H. Shuman. 1985. Genetic evidence for substrate and periplasmic binding-protein recognition by MalF and MalG proteins, cytoplasmic membrane components of the Escherichia coli maltose transport system. J. Bacteriol. 163:654-660.
    • (1985) J. Bacteriol. , vol.163 , pp. 654-660
    • Treptow, N.1    Shuman, H.2
  • 274
    • 0023787957 scopus 로고
    • Allele-specific malE mutations that restore interactions between maltose-binding protein and the inner-membrane components of the maltose transport system
    • Treptow, N. A., and H. A. Shuman. 1988. Allele-specific malE mutations that restore interactions between maltose-binding protein and the inner-membrane components of the maltose transport system. J. Mol. Biol. 202: 809-822.
    • (1988) J. Mol. Biol. , vol.202 , pp. 809-822
    • Treptow, N.A.1    Shuman, H.A.2
  • 275
    • 0028365828 scopus 로고
    • Glc of the phosphoenolpyruvate-dependent glucose phosphotransferase system in Salmonella typhimurium
    • Glc of the phosphoenolpyruvate-dependent glucose phosphotransferase system in Salmonella typhimurium. J. Bacteriol. 176:3518-3526.
    • (1994) J. Bacteriol. , vol.176 , pp. 3518-3526
    • Van Der Vlag, J.1    Van Dam, K.2    Postma, P.W.3
  • 276
    • 0031018158 scopus 로고    scopus 로고
    • Substrate induction and glucose repression of maltose utilization by Streptomyces coelicolor A3(2) is controlled by malR, a member of the lad-galR family of regulatory genes
    • van Wezel, G. P., J. White, P. Young, P. W. Postma, and M. J. Bibb. 1997. Substrate induction and glucose repression of maltose utilization by Streptomyces coelicolor A3(2) is controlled by malR, a member of the lad-galR family of regulatory genes. Mol. Microbiol. 23:537-549.
    • (1997) Mol. Microbiol. , vol.23 , pp. 537-549
    • Van Wezel, G.P.1    White, J.2    Young, P.3    Postma, P.W.4    Bibb, M.J.5
  • 278
    • 0029671310 scopus 로고    scopus 로고
    • 2+ as an extracellular signal: Environmental regulation of Salmonella virulence
    • 2+ as an extracellular signal: environmental regulation of Salmonella virulence. Cell 84:165-174.
    • (1996) Cell , vol.84 , pp. 165-174
    • Véscovi, E.G.1    Soncini, F.C.2    Groisman, E.A.3
  • 279
    • 0026032790 scopus 로고
    • Three adjacent binding sites for cAMP receptor protein are involved in the activation of the divergent malEp-malKp promoters
    • Vidal-Ingigliardi, D., and O. Raibaud. 1991. Three adjacent binding sites for cAMP receptor protein are involved in the activation of the divergent malEp-malKp promoters, Proc. Natl. Acad. Sci. USA 88:229-233.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 229-233
    • Vidal-Ingigliardi, D.1    Raibaud, O.2
  • 280
    • 0027362061 scopus 로고
    • A small C-terminal region of the Escherichia coli MalT protein contains the DNA-binding domain
    • Vidal-Ingigliardi, D., E. Rieht I. O. Danot, and O. Raibaud. 1993. A small C-terminal region of the Escherichia coli MalT protein contains the DNA-binding domain. J. Biol. Chem. 268:24527-24530.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24527-24530
    • Vidal-Ingigliardi, D.1    Rieht, E.2    Danot, O.3    Raibaud, O.4
  • 281
    • 0025849091 scopus 로고
    • Two MalT binding sites in direct repeat. A structural motif involved in the activation of all the promoters of the maltose regulons in Escherichia coli and Klebsiella pneumoniae
    • Vidal-Ingigliardi, D., E. Richet, and O. Raibaud. 1991. Two MalT binding sites in direct repeat. A structural motif involved in the activation of all the promoters of the maltose regulons in Escherichia coli and Klebsiella pneumoniae. J. Mol. Biol. 218:323-334.
    • (1991) J. Mol. Biol. , vol.218 , pp. 323-334
    • Vidal-Ingigliardi, D.1    Richet, E.2    Raibaud, O.3
  • 283
    • 0029967951 scopus 로고    scopus 로고
    • Signal detection by the PhoQ sensor-transmitter. Characterization of the sensor domain and a response-impaired mutant that identifies ligand-binding determinants
    • Waldburger, C. D., and R. T. Sauer. 1996. Signal detection by the PhoQ sensor-transmitter. Characterization of the sensor domain and a response-impaired mutant that identifies ligand-binding determinants. J. Biol. Chem. 271:26630-26636.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26630-26636
    • Waldburger, C.D.1    Sauer, R.T.2
  • 284
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- And beta-subunits of ATP synthase, myosin kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., M. Saraste, J. M. Runswik, and N. J. Gay. 1982. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1:945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswik, J.M.3    Gay, N.J.4
  • 285
    • 0014004642 scopus 로고
    • Pullulanase from Aerobacter aerogenes; production in a cell-bound state. Purification and properties of the enzyme
    • Wallenfels, K., H. Bender, and I. Rached. 1966. Pullulanase from Aerobacter aerogenes; production in a cell-bound state. Purification and properties of the enzyme. Biochem. Biophys. Res. Commun. 22:254-261.
    • (1966) Biochem. Biophys. Res. Commun. , vol.22 , pp. 254-261
    • Wallenfels, K.1    Bender, H.2    Rached, I.3
  • 286
    • 0019220506 scopus 로고
    • Pleiotropic mutations rendering Escherichia coli K-12 resistant tobacteriophageTP1
    • Wandersman, C., F. Moreno, and M. Schwartz. 1980. Pleiotropic mutations rendering Escherichia coli K-12 resistant tobacteriophageTP1. J. Bacteriol. 143:1374-1383.
    • (1980) J. Bacteriol. , vol.143 , pp. 1374-1383
    • Wandersman, C.1    Moreno, F.2    Schwartz, M.3
  • 287
    • 0031565721 scopus 로고    scopus 로고
    • Channel specificity: Structural basis for sugar discrimination and differential flux rates in maltoporin
    • Wang, Y. F., R. Dutzler, P. J. Rizkallah, J. P. Rosenbusch, and T. Schirmer. 1997. Channel specificity: structural basis for sugar discrimination and differential flux rates in maltoporin. J. Mol. Biol. 272:56-63.
    • (1997) J. Mol. Biol. , vol.272 , pp. 56-63
    • Wang, Y.F.1    Dutzler, R.2    Rizkallah, P.J.3    Rosenbusch, J.P.4    Schirmer, T.5
  • 288
    • 0042796229 scopus 로고    scopus 로고
    • Are the multiple signals transduction pathways of the Pho regulon due to cross talk or cross regulation?
    • E. C. C. Lin and A. S. Lynch (ed.), R. G. Landes Co., Austin, Tex.
    • Wanner, B. L., W. Jiang, S.-K. Kim, S. Yamagata, A. Haldimunn, and L. L. Daniels. 1996. Are the multiple signals transduction pathways of the Pho regulon due to cross talk or cross regulation? p. 287-315. In E. C. C. Lin and A. S. Lynch (ed.), Regulation of gene expression in Escherichia coli. R. G. Landes Co., Austin, Tex.
    • (1996) Regulation of Gene Expression in Escherichia Coli , pp. 287-315
    • Wanner, B.L.1    Jiang, W.2    Kim, S.-K.3    Yamagata, S.4    Haldimunn, A.5    Daniels, L.L.6
  • 289
    • 0018668898 scopus 로고
    • Escherichia coli mutant that reduces amounts of several periplasmic and outer membrane proteins
    • Wanner, B. L., A. Sarthy, and J. Beckwith. 1979. Escherichia coli mutant that reduces amounts of several periplasmic and outer membrane proteins. J. Bacteriol. 140:229-239.
    • (1979) J. Bacteriol. , vol.140 , pp. 229-239
    • Wanner, B.L.1    Sarthy, A.2    Beckwith, J.3
  • 290
    • 0031014875 scopus 로고    scopus 로고
    • The crystal structure of Escherichia coli maltodextrin phosphorylase provides an explanation for the activity without control in this basic archetype of a phosphorylase
    • Watson, K. A., R. Schinzel, D. Palm, and L. N. Johnson. 1997. The crystal structure of Escherichia coli maltodextrin phosphorylase provides an explanation for the activity without control in this basic archetype of a phosphorylase. EMBO J. 16:1-14.
    • (1997) EMBO J. , vol.16 , pp. 1-14
    • Watson, K.A.1    Schinzel, R.2    Palm, D.3    Johnson, L.N.4
  • 291
    • 0026603863 scopus 로고
    • Molecular analysis of the signaling pathway between EnvZ and OmpR in Escherichia coli
    • Waukau, J., and S. Forst. 1992. Molecular analysis of the signaling pathway between EnvZ and OmpR in Escherichia coli. J. Bacteriol. 174:1522-1527.
    • (1992) J. Bacteriol. , vol.174 , pp. 1522-1527
    • Waukau, J.1    Forst, S.2
  • 292
    • 0028181852 scopus 로고
    • UTP: α-D-glucose-1-phosphate uridylyltransferase of Escherichia coli: isolation and DNA sequence of the galU gene and purification of the enzyme
    • Weissborn, A. C., Q. Liu, M. K. Rumley, and E. P. Kennedy. 1994. UTP: α-D-glucose-1-phosphate uridylyltransferase of Escherichia coli: isolation and DNA sequence of the galU gene and purification of the enzyme. J. Bacteriol. 176:2611-2618.
    • (1994) J. Bacteriol. , vol.176 , pp. 2611-2618
    • Weissborn, A.C.1    Liu, Q.2    Rumley, M.K.3    Kennedy, E.P.4
  • 293
    • 0029909480 scopus 로고    scopus 로고
    • Escherichia coli preprotein translocase
    • Wickner, W., and M. R. Leonard. 1996. Escherichia coli preprotein translocase. J. Biol. Chem. 271:29514-29516.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29514-29516
    • Wickner, W.1    Leonard, M.R.2
  • 294
    • 1842271033 scopus 로고
    • The characterization of the pathway of maltose utilization by Escherichia coli. II. General properties and mechanism of action of amylomaltase
    • Wiesmeyer, H., and M. Cohn. 1960. The characterization of the pathway of maltose utilization by Escherichia coli. II. General properties and mechanism of action of amylomaltase. Biochim. Biophys. Acta 39:427-439.
    • (1960) Biochim. Biophys. Acta , vol.39 , pp. 427-439
    • Wiesmeyer, H.1    Cohn, M.2
  • 295
    • 2642638300 scopus 로고
    • The characterization of the pathway of maltose utilization by Escherichia coli. J. Purification and physical chemical properties of the enzyme amylomaltase
    • Wiesmeyer, H., and M. Cohn. 1960. The characterization of the pathway of maltose utilization by Escherichia coli. J. Purification and physical chemical properties of the enzyme amylomaltase. Biochim. Biophys. Acta 39:417-426.
    • (1960) Biochim. Biophys. Acta , vol.39 , pp. 417-426
    • Wiesmeyer, H.1    Cohn, M.2
  • 296
    • 0029830549 scopus 로고    scopus 로고
    • A putative helical domain in the MalK subunit of the ATP-binding-cassette transport system for maltose of Salmonella typhimurium (MalFGK2) is crucial for interaction with MalF and MalG. A study using the LacK protein of Agrobacterium radiobacter as a tool
    • Wilken, S., G. Schmees, and E. Schneider. 1996. A putative helical domain in the MalK subunit of the ATP-binding-cassette transport system for maltose of Salmonella typhimurium (MalFGK2) is crucial for interaction with MalF and MalG. A study using the LacK protein of Agrobacterium radiobacter as a tool. Mol. Microbiol. 22:655-666.
    • (1996) Mol. Microbiol. , vol.22 , pp. 655-666
    • Wilken, S.1    Schmees, G.2    Schneider, E.3
  • 297
    • 0013890307 scopus 로고
    • Endogenous induction of the galactose operon in Escherichia coli K12
    • Wu, H. C. P., and H. M. Kalckar. 1966. Endogenous induction of the galactose operon in Escherichia coli K12. Proc. Natl. Acad. Sci. USA 55: 622-629.
    • (1966) Proc. Natl. Acad. Sci. USA , vol.55 , pp. 622-629
    • Wu, H.C.P.1    Kalckar, H.M.2
  • 298
    • 0028952583 scopus 로고
    • i during the uptake of sn-glycerol-3-phosphate by the pho regulon-dependent Ugp system and the glp regulon-dependent GlpT system
    • i during the uptake of sn-glycerol-3-phosphate by the pho regulon-dependent Ugp system and the glp regulon-dependent GlpT system. J. Bacteriol. 177:699-704.
    • (1995) J. Bacteriol. , vol.177 , pp. 699-704
    • Xavier, K.B.1    Kossmann, M.2    Santos, H.3    Boos, W.4
  • 299
    • 0029779716 scopus 로고    scopus 로고
    • High-affinity maltose/trehalose transport system in the hyperthermophilic archaeon Thermococcus litoralis
    • Xavier, K. B., L. O. Martins, R. Peist, M. Kossmann, W. Boos, and H. Santos. 1996. High-affinity maltose/trehalose transport system in the hyperthermophilic archaeon Thermococcus litoralis. J. Bacteriol. 178:4773-4777.
    • (1996) J. Bacteriol. , vol.178 , pp. 4773-4777
    • Xavier, K.B.1    Martins, L.O.2    Peist, R.3    Kossmann, M.4    Boos, W.5    Santos, H.6
  • 300
    • 0023819292 scopus 로고
    • α-Glucan phosphorylase from Escherichia coli. Cloning of the gene and purification and characterization of the protein
    • Yu, F., J. Jen, E. Takeuchi, M. Inouye, H. Nakayama, M. Tagaya, and T. Fukui. 1988. α-Glucan phosphorylase from Escherichia coli. Cloning of the gene and purification and characterization of the protein. J. Biol. Chem. 263:13706-13711.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13706-13711
    • Yu, F.1    Jen, J.2    Takeuchi, E.3    Inouye, M.4    Nakayama, H.5    Tagaya, M.6    Fukui, T.7
  • 301
    • 0029127483 scopus 로고
    • MalY of Escherichia coli is an enzyme with the activity of a βC-S lyase (cystathionase)
    • Zdych, E., R. Peist, J. Reidl, and W. Boos. 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
  • 302
    • 0026445704 scopus 로고
    • Maltose chemotaxis involves residues in the N-terminal and C-terminal domains on the same face of maltose-binding protein
    • Zhang, Y. H., C. Conway, M. Rosato, Y. Suh, and M. D. Manson. 1992. Maltose chemotaxis involves residues in the N-terminal and C-terminal domains on the same face of maltose-binding protein. J. Biol. Chem. 267: 22813-22820.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22813-22820
    • Zhang, Y.H.1    Conway, C.2    Rosato, M.3    Suh, Y.4    Manson, M.D.5
  • 303
    • 0029905277 scopus 로고    scopus 로고
    • Maltose-binding protein containing an interdomain disulfide bridge confers a dominant-negative phenotype for transport and chemotaxis
    • Zhang, Y. H., D. E. Mannering, A. L. Davidson, N. H. Yao, and M. D. Manson. 1996. Maltose-binding protein containing an interdomain disulfide bridge confers a dominant-negative phenotype for transport and chemotaxis. J. Biol. Chem. 271:17881-17889.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17881-17889
    • Zhang, Y.H.1    Mannering, D.E.2    Davidson, A.L.3    Yao, N.H.4    Manson, M.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.