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Volumn 271, Issue 5, 2004, Pages 545-553

Mutational analysis of the binding affinity and transport activity for N-acetylglucosamine of the novel ABC transporter Ngc in the chitin-degrader Streptomyces olivaceoviridis

Author keywords

ABC transporter; Chitin degradation; Lectins; N acetylglucosamine; NgcE

Indexed keywords

ABC TRANSPORTER; ABC TRANSPORTER NGC; AMINO ACID; CHITIN; LECTIN; N ACETYLGLUCOSAMINE; UNCLASSIFIED DRUG;

EID: 3142738881     PISSN: 16174615     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00438-004-0981-0     Document Type: Article
Times cited : (21)

References (39)
  • 1
    • 0022344425 scopus 로고
    • The chitinase system of Streptomyces sp. ATCC 11238 and its significance for fungal cell wall degradation
    • Beyer M, Diekmann H (1985) The chitinase system of Streptomyces sp. ATCC 11238 and its significance for fungal cell wall degradation. Appl Microbiol Biotechnol 23:140-146
    • (1985) Appl Microbiol Biotechnol , vol.23 , pp. 140-146
    • Beyer, M.1    Diekmann, H.2
  • 2
    • 0027323001 scopus 로고
    • Characteristics of an exochitinase from Streptomyces olivaceoviridis, its corresponding gene, putative protein domains and relationship to other chitinases
    • Blaak H, Schnellmann J, Walter S, Henrissat B, Schrempf H (1993) Characteristics of an exochitinase from Streptomyces olivaceoviridis, its corresponding gene, putative protein domains and relationship to other chitinases. Eur J Biochem 214:659-669
    • (1993) Eur J Biochem , vol.214 , pp. 659-669
    • Blaak, H.1    Schnellmann, J.2    Walter, S.3    Henrissat, B.4    Schrempf, H.5
  • 3
    • 0031006412 scopus 로고    scopus 로고
    • Antibiotic resistance gene cassettes derived from the omega interposon for use in E. coli and Streptomyces
    • Blondelet-Rouault MH, Weiser J, Lebrihi A, Branny P, Pernodet JL (1997) Antibiotic resistance gene cassettes derived from the omega interposon for use in E. coli and Streptomyces. Gene 190:315-317
    • (1997) Gene , vol.190 , pp. 315-317
    • Blondelet-Rouault, M.H.1    Weiser, J.2    Lebrihi, A.3    Branny, P.4    Pernodet, J.L.5
  • 4
    • 0036479107 scopus 로고    scopus 로고
    • Structural model of MalK, the ABC subunit of the maltose transporter in Escherichia coli
    • Böhm A, Diez J, Diederichs K, Weite W, Boos W (2002) Structural model of MalK, the ABC subunit of the maltose transporter in Escherichia coli. J Biol Chem 277:3708-3717
    • (2002) J Biol Chem , vol.277 , pp. 3708-3717
    • Böhm, A.1    Diez, J.2    Diederichs, K.3    Weite, W.4    Boos, W.5
  • 5
    • 0001769249 scopus 로고    scopus 로고
    • Periplasmic binding protein-dependent ABC transporters
    • Neidhardt FC, Curtiss R, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (eds) American Society of Microbiology, Washington, D.C.
    • Boos W, Lucht JM (1996) Periplasmic binding protein-dependent ABC transporters. In: Neidhardt FC, Curtiss R, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (eds) Escherichia coli and Salmonella typhimurium: cellular and molecular biology. American Society of Microbiology, Washington, D.C., pp 1175-1209
    • (1996) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 1175-1209
    • Boos, W.1    Lucht, J.M.2
  • 6
    • 0035852667 scopus 로고    scopus 로고
    • Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concentrated mechanism of maltose transport
    • Cheng J, Sharma S, Quiocho FA, Davidson AL (2001) Trapping the transition state of an ATP-binding cassette transporter: evidence for a concentrated mechanism of maltose transport. Proc Natl Adad Sci USA 98:1525-153
    • (2001) Proc Natl Adad Sci USA , vol.98 , pp. 1525-2153
    • Cheng, J.1    Sharma, S.2    Quiocho, F.A.3    Davidson, A.L.4
  • 7
    • 0034669176 scopus 로고    scopus 로고
    • Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis
    • Diederichs K, Diez J, Greller G, Müller C, Breed J, Schnell C, Vonrhein C, Boos W, Welte W (2000) Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis. EMBO J 19:5951-5961
    • (2000) EMBO J , vol.19 , pp. 5951-5961
    • Diederichs, K.1    Diez, J.2    Greller, G.3    Müller, C.4    Breed, J.5    Schnell, C.6    Vonrhein, C.7    Boos, W.8    Welte, W.9
  • 8
    • 0035951304 scopus 로고    scopus 로고
    • The crystal structure of a liganded trehalose/maltose-binding protein from the hyperthermophilic Archaeon Thermococcus litoralis at 1.85 Å
    • Diez J, Diederichs K, Greller G, Horlacher R, Boos W, Welte W (2001) The crystal structure of a liganded trehalose/maltose-binding protein from the hyperthermophilic Archaeon Thermococcus litoralis at 1.85 Å. J Mol Biol 305:905-915
    • (2001) J Mol Biol , vol.305 , pp. 905-915
    • Diez, J.1    Diederichs, K.2    Greller, G.3    Horlacher, R.4    Boos, W.5    Welte, W.6
  • 9
    • 0033918059 scopus 로고    scopus 로고
    • NMR investigations of protein-carbohydrate interactions binding studies and refined three-dimensional solution structure of the complex between the B domain of wheat germ agglutinin and N,N′,N″-triacetylchitotriose
    • Espinosa JF, Asensio JL, Garcia JL, Laynez J, Bruix M, Wright C, Siebert HC, Gabius HJ, Canada FJ, Jimenez-Barbero J (2000) NMR investigations of protein-carbohydrate interactions binding studies and refined three-dimensional solution structure of the complex between the B domain of wheat germ agglutinin and N,N′,N″-triacetylchitotriose. Eur J Biochem 267:3965-3978
    • (2000) Eur J Biochem , vol.267 , pp. 3965-3978
    • Espinosa, J.F.1    Asensio, J.L.2    Garcia, J.L.3    Laynez, J.4    Bruix, M.5    Wright, C.6    Siebert, H.C.7    Gabius, H.J.8    Canada, F.J.9    Jimenez-Barbero, J.10
  • 10
    • 0035951289 scopus 로고    scopus 로고
    • Structural basis for oligosaccharide recognition by Pyrococcus furiosus maltodextrin-binding protein
    • Evdokimov AG, Anderson DE, Routzahn KM, Waugh DS (2001) Structural basis for oligosaccharide recognition by Pyrococcus furiosus maltodextrin-binding protein. J Mol Biol 305:891-904
    • (2001) J Mol Biol , vol.305 , pp. 891-904
    • Evdokimov, A.G.1    Anderson, D.E.2    Routzahn, K.M.3    Waugh, D.S.4
  • 11
    • 0034737303 scopus 로고    scopus 로고
    • Crystal structures of Urtica dioica agglutinin and its complex with tri- N -acetylchitotriose
    • Harata K, Muraki M (2000) Crystal structures of Urtica dioica agglutinin and its complex with tri- N -acetylchitotriose. J Mol Biol 297:673-681
    • (2000) J Mol Biol , vol.297 , pp. 673-681
    • Harata, K.1    Muraki, M.2
  • 13
    • 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, Xavier KB, Santos H, DiRuggiero J, Kossmann M, Boos W (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
  • 14
    • 0027459427 scopus 로고
    • Derivatives of pUC18 that have Bgl II sites flanking a modified multiple cloning site and that retain the ability to identify recombinant clones by visual screening of Escherichia coli colonies
    • Janssen GR, Bibb MJ (1993) Derivatives of pUC18 that have Bgl II sites flanking a modified multiple cloning site and that retain the ability to identify recombinant clones by visual screening of Escherichia coli colonies. Gene 124:133-134
    • (1993) Gene , vol.124 , pp. 133-134
    • Janssen, G.R.1    Bibb, M.J.2
  • 15
    • 0036091602 scopus 로고    scopus 로고
    • Redundancy in periplasmic binding protein-dependent transport systems for trehalose, sucrose, and maltose in Sinorhizobium meliloti
    • Jensen JB, Peters NK, Bhuvaneswari TV (2002) Redundancy in periplasmic binding protein-dependent transport systems for trehalose, sucrose, and maltose in Sinorhizobium meliloti. J Bacteriol 184:2978-2986
    • (2002) J Bacteriol , vol.184 , pp. 2978-2986
    • Jensen, J.B.1    Peters, N.K.2    Bhuvaneswari, T.V.3
  • 16
    • 0034885332 scopus 로고    scopus 로고
    • Cellobiose uptake in the hyperthermophilic archaeon Pyrococcus furiosus is mediated by an inducible, high-affinity ABC transporter
    • Koning SM, Elferink MG, Konings WN, Driessen AJ (2001) Cellobiose uptake in the hyperthermophilic archaeon Pyrococcus furiosus is mediated by an inducible, high-affinity ABC transporter. J Bacteriol 183:4979-4984
    • (2001) J Bacteriol , vol.183 , pp. 4979-4984
    • Koning, S.M.1    Elferink, M.G.2    Konings, W.N.3    Driessen, A.J.4
  • 18
    • 0025314134 scopus 로고
    • Genetic approach to the role of tryptophan residues in the activities and fluorescence of a bacterial periplasmic maltose-binding protein
    • Martineau P, Szmelcman S, Spurlino JC, Quiocho FA, Hofnung M (1990) Genetic approach to the role of tryptophan residues in the activities and fluorescence of a bacterial periplasmic maltose-binding protein. J Mol Biol 214:337-352
    • (1990) J Mol Biol , vol.214 , pp. 337-352
    • Martineau, P.1    Szmelcman, S.2    Spurlino, J.C.3    Quiocho, F.A.4    Hofnung, M.5
  • 20
    • 0028337332 scopus 로고
    • Maltose transport system of Escherichia coli: An ABC-type transporter
    • Nikaido H (1994) Maltose transport system of Escherichia coli: an ABC-type transporter. FEBS Lett 346:55-58
    • (1994) FEBS Lett , vol.346 , pp. 55-58
    • Nikaido, H.1
  • 21
    • 0031571605 scopus 로고    scopus 로고
    • Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor
    • Quiocho FA, Spurlino JC, Rodseth LE (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
    • Quiocho, F.A.1    Spurlino, J.C.2    Rodseth, L.E.3
  • 22
  • 23
    • 0021101390 scopus 로고
    • Study of binding protein-ligand interaction by ammonium sulfate-assisted adsorption on cellulose esters filters
    • Richarme G, Kepes A (1983) Study of binding protein-ligand interaction by ammonium sulfate-assisted adsorption on cellulose esters filters. Biochim Biophys Acta 742:16-24
    • (1983) Biochim Biophys Acta , vol.742 , pp. 16-24
    • Richarme, G.1    Kepes, A.2
  • 24
    • 0026687972 scopus 로고
    • A binding protein-dependent transport system in Streptococcus mutans responsible for multiple sugar metabolism
    • Russell RRB, Aduse-Opoku J, Sutcliffe IC, Tao L, Ferretti JJ (1992) A binding protein-dependent transport system in Streptococcus mutans responsible for multiple sugar metabolism. J Biol Chem 267:4631-4637
    • (1992) J Biol Chem , vol.267 , pp. 4631-4637
    • Russell, R.R.B.1    Aduse-Opoku, J.2    Sutcliffe, I.C.3    Tao, L.4    Ferretti, J.J.5
  • 25
    • 0033977101 scopus 로고    scopus 로고
    • Families of transmembrane sugar transport proteins
    • Saier MH Jr (2000) Families of transmembrane sugar transport proteins. Mol Microbiol 35:699-710
    • (2000) Mol Microbiol , vol.35 , pp. 699-710
    • Saier Jr., M.H.1
  • 30
    • 0029828076 scopus 로고    scopus 로고
    • A lipid-anchored binding protein is a component of an ATP-dependent cellobiose/-triose transport system from the cellulose degrader Streptomyces reticuli
    • Schlösser A, Schrempf H (1996) A lipid-anchored binding protein is a component of an ATP-dependent cellobiose/-triose transport system from the cellulose degrader Streptomyces reticuli. Eur J Biochem 242:332-338
    • (1996) Eur J Biochem , vol.242 , pp. 332-338
    • Schlösser, A.1    Schrempf, H.2
  • 31
    • 0035282418 scopus 로고    scopus 로고
    • Synthesis of the Streptomyces lividans maltodextrin ABC transporter depends on the presence of the regulator MaIR
    • Schlösser A, Weber A, Schrempf H (2001) Synthesis of the Streptomyces lividans maltodextrin ABC transporter depends on the presence of the regulator MaIR. FEMS Microbiol Lett 196:77-83
    • (2001) FEMS Microbiol Lett , vol.196 , pp. 77-83
    • Schlösser, A.1    Weber, A.2    Schrempf, H.3
  • 32
    • 0035010435 scopus 로고    scopus 로고
    • ABC transporter catalyzing carbohydrate uptake
    • Schneider E (2001) ABC transporter catalyzing carbohydrate uptake. Res Microbiol 152:303-310
    • (2001) Res Microbiol , vol.152 , pp. 303-310
    • Schneider, E.1
  • 34
    • 0028956297 scopus 로고
    • Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein
    • Sharff AJ, Rodseth LE, Szmelcman S, Hofnung M, Quiocho FA (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
  • 35
    • 0024419124 scopus 로고
    • Cloning of genes governing the deoxysugar portion of the erythromycin biosynthesis pathway in Saccharopolyspora erythraea (Streptomyces erythreus)
    • Vara J, Lewandowska-Skarbek M, Wang YG, Donadio S, Hutchinson CR (1989) Cloning of genes governing the deoxysugar portion of the erythromycin biosynthesis pathway in Saccharopolyspora erythraea (Streptomyces erythreus). J Bacteriol 171:5872-5881
    • (1989) J Bacteriol , vol.171 , pp. 5872-5881
    • Vara, J.1    Lewandowska-Skarbek, M.2    Wang, Y.G.3    Donadio, S.4    Hutchinson, C.R.5
  • 36
    • 0036434284 scopus 로고    scopus 로고
    • Streptomyces olivaceoviridis possesses a phosphotransferase system that mediates specific, phosphoenolpyruvate-dependent uptake of N-acetylglucosamine
    • Wang F, Xiao X, Saito A, Schrempf H (2002) Streptomyces olivaceoviridis possesses a phosphotransferase system that mediates specific, phosphoenolpyruvate-dependent uptake of N-acetylglucosamine. Mol Genet Genomics 268:344-351
    • (2002) Mol Genet Genomics , vol.268 , pp. 344-351
    • Wang, F.1    Xiao, X.2    Saito, A.3    Schrempf, H.4
  • 37
    • 0021755746 scopus 로고
    • Structural comparison of the two distinct sugar binding sites in wheat germ agglutinin isolectin II
    • Wright CS (1984) Structural comparison of the two distinct sugar binding sites in wheat germ agglutinin isolectin II. J Mol Biol 178:91-104
    • (1984) J Mol Biol , vol.178 , pp. 91-104
    • Wright, C.S.1
  • 38
    • 0029779716 scopus 로고    scopus 로고
    • High-affinity maltose/trehalose transport system in the hyperthermophilic archaeon Thermococcus litoralis
    • Xavier KB, Martins LO, Peist R, Kossmann M, Boos W, Santos H (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
  • 39
    • 0036089944 scopus 로고    scopus 로고
    • The novel Streptomyces olivaceoviridis ABC transporter Ngc mediates uptake of N -acetylglucosamine and N, N′-diacetylchitobiose
    • Xiao X, Wang F, Saito A, Majka J, Schlösser A, Schrempf H (2002) The novel Streptomyces olivaceoviridis ABC transporter Ngc mediates uptake of N -acetylglucosamine and N, N′-diacetylchitobiose. Mol Gen Genomics 267:429-439
    • (2002) Mol Gen Genomics , vol.267 , pp. 429-439
    • Xiao, X.1    Wang, F.2    Saito, A.3    Majka, J.4    Schlösser, A.5    Schrempf, H.6


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