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Volumn 70, Issue 4, 2006, Pages 798-807

Cloning and comparison of third β-glucoside utilization (bglEFIA) operon with two operons of Pectobacterium carotovorum subsp. carotovorum LY34

Author keywords

6 phospho glucosidase; bgl operon; Pectobacterium carotovorum subsp. carotovorum LY34; PTS system

Indexed keywords

CLONING; ENZYMES; GENES; MOLECULAR WEIGHT;

EID: 33646148043     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70.798     Document Type: Article
Times cited : (9)

References (40)
  • 1
    • 0025168749 scopus 로고
    • Molecular biology of cellulose degradation
    • Beguin, P., Molecular biology of cellulose degradation. Annu. Rev. Microbiol., 44, 219-248 (1990).
    • (1990) Annu. Rev. Microbiol. , vol.44 , pp. 219-248
    • Beguin, P.1
  • 2
    • 0035098812 scopus 로고    scopus 로고
    • Cloning and biochemical characterization of BglC, a β-glucosidase from the cellulolytic actinomycete Thermobifida fusca
    • Spiridonov, N. A., and Wilson, D. B., Cloning and biochemical characterization of BglC, a β-glucosidase from the cellulolytic actinomycete Thermobifida fusca. Curr. Microbiol., 42, 295-301 (2001).
    • (2001) Curr. Microbiol. , vol.42 , pp. 295-301
    • Spiridonov, N.A.1    Wilson, D.B.2
  • 3
    • 0028915108 scopus 로고
    • Cleavage of trehalose-phosphate in Bacillus subtilis is catalyzed by a phospho-α-(1,1)-glucosidase encoded by the treA gene
    • Helfert, C., Gotsche, S., and Dahl, M. K., Cleavage of trehalose-phosphate in Bacillus subtilis is catalyzed by a phospho-α-(1,1)-glucosidase encoded by the treA gene. Mol. Microbiol., 16, 111-120 (1995).
    • (1995) Mol. Microbiol. , vol.16 , pp. 111-120
    • Helfert, C.1    Gotsche, S.2    Dahl, M.K.3
  • 5
    • 0038771945 scopus 로고    scopus 로고
    • The β-glucoside genes of Klebsiella aerogenes: Conservation and divergence in relation to the cryptic bgl genes of Escherichia coli
    • Raghunand, T. R., and Mahadevan, S., The β-glucoside genes of Klebsiella aerogenes: conservation and divergence in relation to the cryptic bgl genes of Escherichia coli. FEMS Microbiol. Lett., 223, 267-274 (2003).
    • (2003) FEMS Microbiol. Lett. , vol.223 , pp. 267-274
    • Raghunand, T.R.1    Mahadevan, S.2
  • 6
    • 0032545669 scopus 로고    scopus 로고
    • The cloning, expression and characterization of a cellobiase gene encoding a secretary enzyme from Cellulomonas biazotea
    • Wong, W. K. R., Ali, A., Chan, W. K., Ho, V., and Lee, N. T. K., The cloning, expression and characterization of a cellobiase gene encoding a secretary enzyme from Cellulomonas biazotea. Gene, 207, 79-86 (1998).
    • (1998) Gene , vol.207 , pp. 79-86
    • Wong, W.K.R.1    Ali, A.2    Chan, W.K.3    Ho, V.4    Lee, N.T.K.5
  • 7
    • 0036032981 scopus 로고    scopus 로고
    • Domain analysis of transcriptional regulators bearing PTS regulatory domains
    • Greenberg, D. B., Stulke, J., and Saier, M. H. Jr., Domain analysis of transcriptional regulators bearing PTS regulatory domains. Res. Microbiol., 153, 519-526 (2002).
    • (2002) Res. Microbiol. , vol.153 , pp. 519-526
    • Greenberg, D.B.1    Stulke, J.2    Saier Jr., M.H.3
  • 8
    • 0036034303 scopus 로고    scopus 로고
    • Phylogeny of phosphoryl transfer proteins of the phosphoenolpyruvate-dependent sugar-transporting phosphotransferase system
    • Hu, K. Y., and Saier, M. H. Jr., Phylogeny of phosphoryl transfer proteins of the phosphoenolpyruvate-dependent sugar-transporting phosphotransferase system. Res. Microbiol., 153, 405-415 (2002).
    • (2002) Res. Microbiol. , vol.153 , pp. 405-415
    • Hu, K.Y.1    Saier Jr., M.H.2
  • 9
    • 0037804190 scopus 로고    scopus 로고
    • A single V317A or V317M substitution in enzyme II of a newly identified β-glucoside phosphotransferase and utilization system of Corynebacterium glutamicum R extends its specificity towards cellobiose
    • Kotrba, P., Inui, M., and Yukawa, H., A single V317A or V317M substitution in enzyme II of a newly identified β-glucoside phosphotransferase and utilization system of Corynebacterium glutamicum R extends its specificity towards cellobiose. Microbiology, 149, 1569-1580 (2003).
    • (2003) Microbiology , vol.149 , pp. 1569-1580
    • Kotrba, P.1    Inui, M.2    Yukawa, H.3
  • 10
    • 0038191150 scopus 로고    scopus 로고
    • The LicT protein acts as both a positive and a negative regulator of loci within the bgl regulon of Streptococcus mutans
    • Cote, C. K., and Honeyman, A. L., The LicT protein acts as both a positive and a negative regulator of loci within the bgl regulon of Streptococcus mutans. Microbiology, 149, 1333-1340 (2003).
    • (2003) Microbiology , vol.149 , pp. 1333-1340
    • Cote, C.K.1    Honeyman, A.L.2
  • 11
    • 0344564161 scopus 로고    scopus 로고
    • Regulation of the lic operon of Bacillus subtilis and characterization of potential phosphorylation sites of the LicR regulator protein by site-directed mutagenesis
    • Tobisch, S., Stulke, J., and Hecker, M., Regulation of the lic operon of Bacillus subtilis and characterization of potential phosphorylation sites of the LicR regulator protein by site-directed mutagenesis. J. Bacteriol., 181, 4995-5003 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 4995-5003
    • Tobisch, S.1    Stulke, J.2    Hecker, M.3
  • 12
    • 0037470987 scopus 로고    scopus 로고
    • A Crh-specific function in carbon catabolite repression in Bacilus subtilis
    • Warner, J. B., and Lolkema, J. S., A Crh-specific function in carbon catabolite repression in Bacilus subtilis. FEMS Microbiol. Lett., 220, 277-280 (2003).
    • (2003) FEMS Microbiol. Lett. , vol.220 , pp. 277-280
    • Warner, J.B.1    Lolkema, J.S.2
  • 13
    • 0033977101 scopus 로고    scopus 로고
    • Families of transmembrane sugar transport proteins
    • Saier, M. H. Jr., Families of transmembrane sugar transport proteins. Mol. Microbiol., 35, 699-710 (2000).
    • (2000) Mol. Microbiol. , vol.35 , pp. 699-710
    • Saier Jr., M.H.1
  • 14
    • 0026546539 scopus 로고
    • Proposed uniform nomenclature for the proteins and the protein domains of the bacterial phosphoenolpyruvate: Sugar phosphotransferase system
    • Saier, M. H. Jr., and Reizer, J., Proposed uniform nomenclature for the proteins and the protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. J. Bacteriol., 174, 1433-1438 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 1433-1438
    • Saier Jr., M.H.1    Reizer, J.2
  • 15
    • 0032580862 scopus 로고    scopus 로고
    • Cloning and characterization of a CMCase gene, celB, of Erwinia carotovra subsp. carotovora LY34 and its comparison to celA
    • Park, Y. W., Lim, S. T., and Yun, H. D., Cloning and characterization of a CMCase gene, celB, of Erwinia carotovra subsp. carotovora LY34 and its comparison to celA. Mol. Cells, 8, 280-285 (1998).
    • (1998) Mol. Cells , vol.8 , pp. 280-285
    • Park, Y.W.1    Lim, S.T.2    Yun, H.D.3
  • 17
    • 20044370442 scopus 로고    scopus 로고
    • Structural and biochemical analysis of the asc operon encoding 6-phospho-β-glucosidase in Pectobacterium carotovorum subsp. carotovorum LY34
    • An, C. L., Lim, W. J., Hong, S. Y., Shin, E. C., Kim, M. K., Lee, J. Y., Park, S. R., Woo, J. G., Lim, Y. P., and Yun, H. D., Structural and biochemical analysis of the asc operon encoding 6-phospho-β-glucosidase in Pectobacterium carotovorum subsp. carotovorum LY34. Res. Microbiol., 156, 145-153 (2005).
    • (2005) Res. Microbiol. , vol.156 , pp. 145-153
    • An, C.L.1    Lim, W.J.2    Hong, S.Y.3    Shin, E.C.4    Kim, M.K.5    Lee, J.Y.6    Park, S.R.7    Woo, J.G.8    Lim, Y.P.9    Yun, H.D.10
  • 19
    • 11144339455 scopus 로고    scopus 로고
    • International symposium on molecular biology of bacterial plasmids
    • Wild, J., Hradecna, Z., and Szybalski, W., International symposium on molecular biology of bacterial plasmids. Plasmid, 45, 142 (2001).
    • (2001) Plasmid , vol.45 , pp. 142
    • Wild, J.1    Hradecna, Z.2    Szybalski, W.3
  • 20
    • 0032176017 scopus 로고    scopus 로고
    • Purification and characterization of extracellular and cell wall bound β-glucosidases from Aspergillus kawachii
    • Iwashita, K., Todoroki, K., Himura, H., Shimoi, H., and Ito, K., Purification and characterization of extracellular and cell wall bound β-glucosidases from Aspergillus kawachii. Biosci. Biotechnol. Biochem., 62, 1938-1946 (1998).
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 1938-1946
    • Iwashita, K.1    Todoroki, K.2    Himura, H.3    Shimoi, H.4    Ito, K.5
  • 21
    • 15244348772 scopus 로고    scopus 로고
    • Preparation and properties of gelatin-immobilized β-glucosidase from Pyrococcus furiosus
    • Nagatomo, H., Matsushita, Y., Sugamoto, K., and Matsui, T., Preparation and properties of gelatin-immobilized β-glucosidase from Pyrococcus furiosus. Biosci. Biotechnol. Biochem., 69, 128-136 (2005).
    • (2005) Biosci. Biotechnol. Biochem. , vol.69 , pp. 128-136
    • Nagatomo, H.1    Matsushita, Y.2    Sugamoto, K.3    Matsui, T.4
  • 22
    • 0038151854 scopus 로고    scopus 로고
    • Production and characterization of recombinant Phanerochaete chrysosporium β-glucosidase in the methylotropic yeast Pichia pastoris
    • Kawai, R., Yoshida, M., Tani, T., Igarashi, K., Ohira, T., Nagasawa, H., and Samejima, M., Production and characterization of recombinant Phanerochaete chrysosporium β-glucosidase in the methylotropic yeast Pichia pastoris. Biosci. Biotechnol. Biochem., 67, 1-7 (2003).
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 1-7
    • Kawai, R.1    Yoshida, M.2    Tani, T.3    Igarashi, K.4    Ohira, T.5    Nagasawa, H.6    Samejima, M.7
  • 23
    • 0030942244 scopus 로고    scopus 로고
    • Glycoside hydrolase production by an anaerobic rumen fungus Caecomyces communis
    • Bata, J., and Gerbi, C., Glycoside hydrolase production by an anaerobic rumen fungus Caecomyces communis. Res. Microbiol., 148, 263-269 (1997).
    • (1997) Res. Microbiol. , vol.148 , pp. 263-269
    • Bata, J.1    Gerbi, C.2
  • 24
    • 0037902560 scopus 로고    scopus 로고
    • Transglucosylation of tertiary alcohols using cassava β-glucosidase
    • Svasti, J., Phongsak, T., and Sarnthima, R., Transglucosylation of tertiary alcohols using cassava β-glucosidase. Biochem. Biophys. Res. Commun., 305, 470-475 (2003).
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 470-475
    • Svasti, J.1    Phongsak, T.2    Sarnthima, R.3
  • 25
    • 0031780571 scopus 로고    scopus 로고
    • Expression of the bglH gene of Lactobasillus plantarum is controlled by carbon catabolite repression
    • Marasco, R., Muscariello, L., Varcamonti, M., De Felice, M., and Sacco, M., Expression of the bglH gene of Lactobasillus plantarum is controlled by carbon catabolite repression. J. Bacteriol., 180, 3400-3404 (1998).
    • (1998) J. Bacteriol. , vol.180 , pp. 3400-3404
    • Marasco, R.1    Muscariello, L.2    Varcamonti, M.3    De Felice, M.4    Sacco, M.5
  • 26
    • 0014036299 scopus 로고
    • Inducible system for the utilization of β-glucosides in Escherichia coli. I. Active transport and utilization of β-glucosides
    • Schaefler, S., Inducible system for the utilization of β-glucosides in Escherichia coli. I. Active transport and utilization of β-glucosides. J. Bacteriol., 93, 254-263 (1967).
    • (1967) J. Bacteriol. , vol.93 , pp. 254-263
    • Schaefler, S.1
  • 27
    • 0037444765 scopus 로고    scopus 로고
    • Sphingomonas paucimobilis beta-glucosidase Bgl1: A member of a new bacterial subfamily in glycoside hydrolase family 1
    • Marques, A. R., Coutinho, P. M., Videira, P., Fialho, A. M., and Sa-Correia, I., Sphingomonas paucimobilis beta-glucosidase Bgl1: a member of a new bacterial subfamily in glycoside hydrolase family 1. Biochem. J., 370, 793-804 (2003).
    • (2003) Biochem. J. , vol.370 , pp. 793-804
    • Marques, A.R.1    Coutinho, P.M.2    Videira, P.3    Fialho, A.M.4    Sa-Correia, I.5
  • 28
    • 0031038989 scopus 로고    scopus 로고
    • Phospho-β-glucosidase from Fusobacterium mortiferum: Purification, cloning, and inactivation by 6-phosphoglucono-δ-lactone
    • Thompson, J., Robrish, S. A., Bouma, C. L., Freedberg, D. I., and Folk, J. E., Phospho-β-glucosidase from Fusobacterium mortiferum: purification, cloning, and inactivation by 6-phosphoglucono-δ-lactone. J. Bacteriol., 179, 1636-1645 (1997).
    • (1997) J. Bacteriol. , vol.179 , pp. 1636-1645
    • Thompson, J.1    Robrish, S.A.2    Bouma, C.L.3    Freedberg, D.I.4    Folk, J.E.5
  • 29
    • 0016285069 scopus 로고
    • The β-glucoside system of Escherichia coli. IV. Purification and properties of phospho-β-glucosidases A and B
    • Wilson, G., and Fox, C. F., The β-glucoside system of Escherichia coli. IV. Purification and properties of phospho-β-glucosidases A and B. J. Biol. Chem., 249, 5586-5598 (1974).
    • (1974) J. Biol. Chem. , vol.249 , pp. 5586-5598
    • Wilson, G.1    Fox, C.F.2
  • 30
    • 10744220908 scopus 로고    scopus 로고
    • Cloning and characterization of a thermostable intracellular α-amylase gene from the hyperthermophilic bacterium Thermotoga maritima MSB8
    • Lim, W. J., Park, S. R., An, C. L., Lee, J. Y., Hong, S. Y., Shin, E. C., Kim, E. J., Kim, J. O., Kim, H., and Yun, H. D., Cloning and characterization of a thermostable intracellular α-amylase gene from the hyperthermophilic bacterium Thermotoga maritima MSB8. Res. Microbiol., 154, 681-687 (2003).
    • (2003) Res. Microbiol. , vol.154 , pp. 681-687
    • Lim, W.J.1    Park, S.R.2    An, C.L.3    Lee, J.Y.4    Hong, S.Y.5    Shin, E.C.6    Kim, E.J.7    Kim, J.O.8    Kim, H.9    Yun, H.D.10
  • 31
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 32
    • 0030897083 scopus 로고    scopus 로고
    • Cloning of cellobiose phosphoenolpyruvate-dependent phosphotransferase genes: Functional expression in recombinant Escherichia coli and identification of a putative binding region for disaccharides
    • Lai, X., Davis, F. C., Hespell, R. B., and Ingram, L. O., Cloning of cellobiose phosphoenolpyruvate-dependent phosphotransferase genes: functional expression in recombinant Escherichia coli and identification of a putative binding region for disaccharides. Appl. Environ. Microbiol., 63, 355-363 (1997).
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 355-363
    • Lai, X.1    Davis, F.C.2    Hespell, R.B.3    Ingram, L.O.4
  • 34
    • 0024043616 scopus 로고
    • A fourth Escherichia coli gene system with the potential to evolve β-glucoside utilization
    • Parker, L. L., and Hall, B. G., A fourth Escherichia coli gene system with the potential to evolve β-glucoside utilization. Genetics, 119, 485-490 (1988).
    • (1988) Genetics , vol.119 , pp. 485-490
    • Parker, L.L.1    Hall, B.G.2
  • 35
    • 0001463551 scopus 로고
    • Unequivocal demonstration of the involvement of a glutamate residue as a nucleophile in the mechanism of a "retaining" glucosidase
    • Withers, S. G., Warren, R. A. J., Street, I. P., Rupitz, K., Kempton, J. B., and Aebersold, R., Unequivocal demonstration of the involvement of a glutamate residue as a nucleophile in the mechanism of a "retaining" glucosidase. J. Am. Chem. Soc., 112, 5887-5889 (1990).
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 5887-5889
    • Withers, S.G.1    Warren, R.A.J.2    Street, I.P.3    Rupitz, K.4    Kempton, J.B.5    Aebersold, R.6
  • 36
    • 0028848613 scopus 로고
    • Identification of the acid/base catalyst in Agrobacterium faecalis β-glucosidase by kinetic analysis of mutants
    • Wang, Q., Trimbur, D., Graham, R., Warren, R. A. J., and Withers, S. G., Identification of the acid/base catalyst in Agrobacterium faecalis β-glucosidase by kinetic analysis of mutants. Biochemistry, 34, 14554-14562 (1995).
    • (1995) Biochemistry , vol.34 , pp. 14554-14562
    • Wang, Q.1    Trimbur, D.2    Graham, R.3    Warren, R.A.J.4    Withers, S.G.5
  • 37
    • 0001014412 scopus 로고    scopus 로고
    • Phosphoenolpyruvate: Carbohydrate phosphotransferase systems
    • eds. Neidhardt, F. C., Curtiss III, R., Ingraham, J. L., Lin, E. C. C., Low, K. B., Magasanik, B., Rezniko., W. S., Riley, M., Schaechter, M., and Umbarger, H. E., ASM Press, Washington, DC
    • Postma, P. W., Lengeler, J. W., and Jacobson, G. R., Phosphoenolpyruvate: carbohydrate phosphotransferase systems. In "Escherichia coli and Salmonella: Cellular and Molecular Biology," eds. Neidhardt, F. C., Curtiss III, R., Ingraham, J. L., Lin, E. C. C., Low, K. B., Magasanik, B., Rezniko., W. S., Riley, M., Schaechter, M., and Umbarger, H. E., ASM Press, Washington, DC, pp. 1149-1174 (1996).
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 1149-1174
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 38
    • 0034604396 scopus 로고    scopus 로고
    • Microbial genome analyses: Comparative transport capabilities in eighteen prokaryotes
    • Paulsen, I. T., Nguyen, L., Sliwinski, M. K., Rabus, R., and Saier, M. H. Jr., Microbial genome analyses: comparative transport capabilities in eighteen prokaryotes. J. Mol. Biol., 301, 75-100 (2000).
    • (2000) J. Mol. Biol. , vol.301 , pp. 75-100
    • Paulsen, I.T.1    Nguyen, L.2    Sliwinski, M.K.3    Rabus, R.4    Saier Jr., M.H.5
  • 39
    • 0035702148 scopus 로고    scopus 로고
    • Bacterial phosphotransferase system (PTS) in carbohydrate uptake and control of carbon metabolism
    • Kotrba, P., Inui, M., and Yukawa, H., Bacterial phosphotransferase system (PTS) in carbohydrate uptake and control of carbon metabolism. J. Biosci. Bioeng., 92, 502-517 (2001).
    • (2001) J. Biosci. Bioeng. , vol.92 , pp. 502-517
    • Kotrba, P.1    Inui, M.2    Yukawa, H.3
  • 40
    • 0021847027 scopus 로고
    • The detection and classification of membrane spanning proteins
    • Klein, P., Kanehisa, M., and Delisi, C., The detection and classification of membrane spanning proteins. Biochim. Blophys. Acta, 815, 468-476 (1985).
    • (1985) Biochim. Blophys. Acta , vol.815 , pp. 468-476
    • Klein, P.1    Kanehisa, M.2    Delisi, C.3


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