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Volumn 268, Issue 3, 2002, Pages 344-351

Streptomyces olivaceoviridis possesses a phosphotransferase system that mediates specific, phosphoenolpyruvate-dependent uptake of N-acetylglucosamine

Author keywords

N acetylglucosamine; Phosphoenolpyruvate dependent phosphotransferase; Streptomycetes; Sugar uptake; Xylose

Indexed keywords

N ACETYLGLUCOSAMINE; PHOSPHOENOLPYRUVATE; PHOSPHOTRANSFERASE;

EID: 0036434284     PISSN: 16174615     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00438-002-0749-3     Document Type: Article
Times cited : (31)

References (34)
  • 1
    • 0037046560 scopus 로고    scopus 로고
    • Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)
    • Bentley SD, et al (2002) Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2). Nature 417:141-147
    • (2002) Nature , vol.417 , pp. 141-147
    • Bentley, S.D.1
  • 2
    • 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
  • 3
    • 0028925347 scopus 로고
    • Binding and substrate specificities of a Streptomyces olivaceoviridis chitinase in comparison with its proteolytically processed form
    • Blaak H, Schrempf H (1995) Binding and substrate specificities of a Streptomyces olivaceoviridis chitinase in comparison with its proteolytically processed form. Eur J Biochem 229:132-139
    • (1995) Eur J Biochem , vol.229 , pp. 132-139
    • Blaak, H.1    Schrempf, H.2
  • 4
    • 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
  • 5
    • 0030463224 scopus 로고    scopus 로고
    • Sugar transport by the marine chitinolytic bacterium Vibrio furnissii. Molecular cloning and analysis of the glucose and N-acetylglucosamine permeases
    • Bouma CL, Roseman S (1996) Sugar transport by the marine chitinolytic bacterium Vibrio furnissii. Molecular cloning and analysis of the glucose and N-acetylglucosamine permeases. J Biol Chem 271:33457-33467
    • (1996) J Biol Chem , vol.271 , pp. 33457-33467
    • Bouma, C.L.1    Roseman, S.2
  • 7
    • 0032838288 scopus 로고    scopus 로고
    • Transport of D-xylose in Lactobacillus pentosus, Lactobacillus casei, and Lactobacillus plantarum: Evidence for a mechanism of facilitated diffusion via the phosphoenolpyruvate:mannose phosphotransferase system
    • Chaillou S, Pouwels PH, Postma PW (1999) Transport of D-xylose in Lactobacillus pentosus, Lactobacillus casei, and Lactobacillus plantarum: Evidence for a mechanism of facilitated diffusion via the phosphoenolpyruvate:mannose phosphotransferase system. J Bacteriol 181:4768-4773
    • (1999) J Bacteriol , vol.181 , pp. 4768-4773
    • Chaillou, S.1    Pouwels, P.H.2    Postma, P.W.3
  • 8
    • 0029942806 scopus 로고    scopus 로고
    • Cloning and sequencing of two genes from Staphylococcus carnosus coding for glucose-specific PTS and their expression in Escherichia coli K-12
    • Christiansen I, Hengstenberg W (1996) Cloning and sequencing of two genes from Staphylococcus carnosus coding for glucose-specific PTS and their expression in Escherichia coli K-12. Mol Gen Genet 250:375-379
    • (1996) Mol Gen Genet , vol.250 , pp. 375-379
    • Christiansen, I.1    Hengstenberg, W.2
  • 9
    • 0022902510 scopus 로고
    • Glucose-permease of the bacterial phosphotransferase system. Gene cloning, overproduction, and amino acid sequence of enzyme IIGlc
    • Erni B, Zanolari B (1986) Glucose-permease of the bacterial phosphotransferase system. Gene cloning, overproduction, and amino acid sequence of enzyme IIGlc. J Biol Chem 261:16398-16403
    • (1986) J Biol Chem , vol.261 , pp. 16398-16403
    • Erni, B.1    Zanolari, B.2
  • 10
    • 0000207681 scopus 로고
    • TMbase - A database of membrane spanning protein segments
    • Hoffman K, Stoffel W (1993) TMbase - A database of membrane spanning protein segments. Biol Chem 347:166
    • (1993) Biol Chem , vol.347 , pp. 166
    • Hoffman, K.1    Stoffel, W.2
  • 12
    • 0034693218 scopus 로고    scopus 로고
    • The chitin disaccharide, N, N'-diacetylchitobiose, is catabolized by Escherichia coli and is transported/phosphorylated by the phosphoenolpyruvate:glycose phosphotransferase system
    • Keyhani NO, Wang LX, Lee YC, Roseman S (2000) The chitin disaccharide, N, N'-diacetylchitobiose, is catabolized by Escherichia coli and is transported/phosphorylated by the phos-phoenolpyruvate:glycose phosphotransferase system. J Biol Chem 275:33084-33090
    • (2000) J Biol Chem , vol.275 , pp. 33084-33090
    • Keyhani, N.O.1    Wang, L.X.2    Lee, Y.C.3    Roseman, S.4
  • 13
    • 0031780384 scopus 로고    scopus 로고
    • The Streptomyces reticuli α-chitin-binding protein CHB2 and its gene
    • Kolbe S, Fischer S, Becirevic A, Hinz P, Schrempf H (1998) The Streptomyces reticuli α-chitin-binding protein CHB2 and its gene. Microbiology 144:1291-1297
    • (1998) Microbiology , vol.144 , pp. 1291-1297
    • Kolbe, S.1    Fischer, S.2    Becirevic, A.3    Hinz, P.4    Schrempf, H.5
  • 14
    • 0032524676 scopus 로고    scopus 로고
    • The glucose transporter of the Escherichia coli phosphotransferase system. Mutant analysis of the invariant arginines, histidines, and domain linker
    • Lanz R, Erni B (1998) The glucose transporter of the Escherichia coli phosphotransferase system. Mutant analysis of the invariant arginines, histidines, and domain linker. J Biol Chem 273:12239-12243
    • (1998) J Biol Chem , vol.273 , pp. 12239-12243
    • Lanz, R.1    Erni, B.2
  • 15
    • 0031764298 scopus 로고    scopus 로고
    • The conjugative plasmid pSG5 from Streptomyces ghanaensis DSM 2932 differs in its transfer functions from other Streptomyces rolling-circle-type plasmids
    • Maas RM, Gotz J, Wohlleben W, Muth G (1998) The conjugative plasmid pSG5 from Streptomyces ghanaensis DSM 2932 differs in its transfer functions from other Streptomyces rolling-circle-type plasmids. Microbiology 144:2809-2817
    • (1998) Microbiology , vol.144 , pp. 2809-2817
    • Maas, R.M.1    Gotz, J.2    Wohlleben, W.3    Muth, G.4
  • 16
    • 0033553420 scopus 로고    scopus 로고
    • A mutated PtsG, the glucose transporter, allows uptake of D-ribose
    • Oh H, Park Y, Park C (1999) A mutated PtsG, the glucose transporter, allows uptake of D-ribose. J Biol Chem 274:14006-14011
    • (1999) J Biol Chem , vol.274 , pp. 14006-14011
    • Oh, H.1    Park, Y.2    Park, C.3
  • 17
    • 0346690417 scopus 로고    scopus 로고
    • The phosphotransferase system (PTS) of Streptomyces coelicolor: Identification and biochemical analysis of a histidine phosphocarrier protein HPr encoded by the gene ptsH
    • Parche S, Schmid R, Titgemeyer F (1999) The phosphotransferase system (PTS) of Streptomyces coelicolor: Identification and biochemical analysis of a histidine phosphocarrier protein HPr encoded by the gene ptsH. Eur J Biochem 265:308-317
    • (1999) Eur J Biochem , vol.265 , pp. 308-317
    • Parche, S.1    Schmid, R.2    Titgemeyer, F.3
  • 18
    • 0034451137 scopus 로고    scopus 로고
    • Sugar uptake and utilisation in Streptomyces coelicolor: A PTS view to the genome
    • Parche S, Nothaft H, Kamionka A, Titgemeyer F (2000) Sugar uptake and utilisation in Streptomyces coelicolor: A PTS view to the genome. Antonie van Leeuwenhoek 78:243-251
    • (2000) Antonie van Leeuwenhoek , vol.78 , pp. 243-251
    • Parche, S.1    Nothaft, H.2    Kamionka, A.3    Titgemeyer, F.4
  • 19
    • 0023989064 scopus 로고
    • Improved tools for biology sequence comparison
    • Pearson WR, Lipman DJ (1988) Improved tools for biology sequence comparison. Proc Natl Acad Sci USA 85:2444-2448
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 20
    • 0001014412 scopus 로고    scopus 로고
    • Phosphoenolpyruvate:carbohydrate phosphotransferase systems
    • Neidhardt FC, Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (eds). American Society for Microbiology, Washington, D.C
    • Postma PW, Lengeler JW, Jacobson GR (1996) Phosphoenolpyruvate:carbohydrate phosphotransferase systems. In: Neidhardt FC, Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (eds) Escherichia coli and Salmonella: Cellular and molecular biology. American Society for Microbiology, Washington, D.C., pp 1149-1174
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology , pp. 1149-1174
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 21
    • 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, Boos W (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
  • 22
    • 0030064491 scopus 로고    scopus 로고
    • Novel phosphotransferase genes revealed by bacterial genome sequencing: A gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in Escherichia coli
    • Reizer J, Ramseier TM, Reizer A, Charbit A, Saier MHJ (1996) Novel phosphotransferase genes revealed by bacterial genome sequencing: A gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in Escherichia coli. Microbiology 142:231-250
    • (1996) Microbiology , vol.142 , pp. 231-250
    • Reizer, J.1    Ramseier, T.M.2    Reizer, A.3    Charbit, A.4    Saier, M.H.J.5
  • 23
    • 0026517235 scopus 로고
    • Cloning and high-level expression of chitinase-encoding gene of Streptomyces plicatus
    • Robbins PW, Overbye K, Albright C, Benfield B, Pero J (1992) Cloning and high-level expression of chitinase-encoding gene of Streptomyces plicatus. Gene 111:69-76
    • (1992) Gene , vol.111 , pp. 69-76
    • Robbins, P.W.1    Overbye, K.2    Albright, C.3    Benfield, B.4    Pero, J.5
  • 24
    • 0023848581 scopus 로고
    • Nucleotide sequences of the Escherichia coli nagE and nagB genes: The structural genes for the N-acetylglucosamine transport protein of the bacterial phosphoenolpyruvate: Sugar phosphotransferase system and for glucosamine-6-phosphate deaminase
    • Rogers MJ, Ohgi T, Plumbridge J, Soll D (1988) Nucleotide sequences of the Escherichia coli nagE and nagB genes: The structural genes for the N-acetylglucosamine transport protein of the bacterial phosphoenolpyruvate: Sugar phosphotransferase system and for glucosamine-6-phosphate deaminase. Gene 62:197-207
    • (1988) Gene , vol.62 , pp. 197-207
    • Rogers, M.J.1    Ohgi, T.2    Plumbridge, J.3    Soll, D.4
  • 26
    • 0035290928 scopus 로고    scopus 로고
    • Characteristics of a Streptomyces coelicolor A3(2) extracellular protein targeting chitin and chitosan
    • Saito A, Miyashita K, Biukovic G, Schrempf H (2001) Characteristics of a Streptomyces coelicolor A3(2) extracellular protein targeting chitin and chitosan. Appl Environ Microbiol 67:1268-1273
    • (2001) Appl Environ Microbiol , vol.67 , pp. 1268-1273
    • Saito, A.1    Miyashita, K.2    Biukovic, G.3    Schrempf, H.4
  • 28
    • 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
  • 29
    • 0028070108 scopus 로고
    • The novel lectin-like protein CHB1 is encoded by a chitin-inducible Streptomyces olivaceoviridis gene and binds specifically to crystalline α-chitin of fungi and other organisms
    • Schnellmann J, Zeltins A, Blaak H, Schrempf H (1994) The novel lectin-like protein CHB1 is encoded by a chitin-inducible Streptomyces olivaceoviridis gene and binds specifically to crystalline α-chitin of fungi and other organisms. Mol Microbiol 13:807-819
    • (1994) Mol Microbiol , vol.13 , pp. 807-819
    • Schnellmann, J.1    Zeltins, A.2    Blaak, H.3    Schrempf, H.4
  • 30
    • 0020442864 scopus 로고
    • The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers
    • Vieira J, Messing J (1982) The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene 19:259-268
    • (1982) Gene , vol.19 , pp. 259-268
    • Vieira, J.1    Messing, J.2
  • 31
    • 0024471892 scopus 로고
    • Analysis of the nag regulon from Escherichia coli K12 and Klebsiella pneumoniae and of its regulation
    • Vogler AP, Lengeler JW (1989) Analysis of the nag regulon from Escherichia coli K12 and Klebsiella pneumoniae and of its regulation. Mol Gen Genet 219:97-105
    • (1989) Mol Gen Genet , vol.219 , pp. 97-105
    • Vogler, A.P.1    Lengeler, J.W.2
  • 32
    • 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 Genet Genomics 267:429-439
    • (2002) Mol Genet Genomics , vol.267 , pp. 429-439
    • Xiao, X.1    Wang, F.2    Saito, A.3    Majka, J.4    Schlösser, A.5    Schrempf, H.6
  • 33
    • 0031203083 scopus 로고    scopus 로고
    • Cloning and sequencing of the genes for N-acetylglucosamine use that construct divergent operons (nagE-nagAC) from Vibrio cholerae non-O1
    • Yamano N, Oura N, Wang J, Fujishima S (1997) Cloning and sequencing of the genes for N-acetylglucosamine use that construct divergent operons (nagE-nagAC) from Vibrio cholerae non-O1. Biosci Biotechnol Biochem 61:1349-1353
    • (1997) Biosci Biotechnol Biochem , vol.61 , pp. 1349-1353
    • Yamano, N.1    Oura, N.2    Wang, J.3    Fujishima, S.4
  • 34
    • 0026709566 scopus 로고
    • Cloning and nucleotide sequence of the ptsG gene of Bacillus subtilis
    • Zagorec M, Postma PW (1992) Cloning and nucleotide sequence of the ptsG gene of Bacillus subtilis. Mol Gen Genet 234:325-328
    • (1992) Mol Gen Genet , vol.234 , pp. 325-328
    • Zagorec, M.1    Postma, P.W.2


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