메뉴 건너뛰기




Volumn 290, Issue 47, 2015, Pages 28374-28387

Characterization of the Pseudomonas aeruginosa glycoside hydrolase PslG reveals that its levels are critical for Psl polysaccharide biosynthesis and biofilm formation

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; BIOCHEMISTRY; BIOFILMS; BIOSYNTHESIS; ENZYMES; GLUCOSE; PLANTS (BOTANY); SUGARS;

EID: 84947769276     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.674929     Document Type: Article
Times cited : (70)

References (82)
  • 1
    • 79551521160 scopus 로고    scopus 로고
    • The pel polysaccharide can serve a structural and protective role in the biofilm matrix of Pseudomonas aeruginosa
    • Colvin, K. M., Gordon, V. D., Murakami, K., Borlee, B. R., Wozniak, D. J., Wong, G. C., and Parsek, M. R. (2011) The pel polysaccharide can serve a structural and protective role in the biofilm matrix of Pseudomonas aeruginosa. PLoS Pathog. 7, e1001264
    • (2011) PLoS Pathog. , vol.7 , pp. e1001264
    • Colvin, K.M.1    Gordon, V.D.2    Murakami, K.3    Borlee, B.R.4    Wozniak, D.J.5    Wong, G.C.6    Parsek, M.R.7
  • 2
    • 84883435047 scopus 로고    scopus 로고
    • The extracellular matrix component Psl provides fast-acting antibiotic defense in Pseudomonas aeruginosa biofilms
    • Billings, N., Millan, M., Caldara, M., Rusconi, R., Tarasova, Y., Stocker, R., and Ribbeck, K. (2013) The extracellular matrix component Psl provides fast-acting antibiotic defense in Pseudomonas aeruginosa biofilms. PLoS Pathog. 9, e1003526
    • (2013) PLoS Pathog. , vol.9 , pp. e1003526
    • Billings, N.1    Millan, M.2    Caldara, M.3    Rusconi, R.4    Tarasova, Y.5    Stocker, R.6    Ribbeck, K.7
  • 3
    • 83655163672 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa Psl polysaccharide reduces neutrophil phagocytosis and the oxidative response by limiting complement-mediated opsonization
    • Mishra, M., Byrd, M. S., Sergeant, S., Azad, A. K., Parsek, M. R., McPhail, L., Schlesinger, L. S., and Wozniak, D. J. (2012) Pseudomonas aeruginosa Psl polysaccharide reduces neutrophil phagocytosis and the oxidative response by limiting complement-mediated opsonization. Cell. Microbiol. 14, 95-106
    • (2012) Cell. Microbiol. , vol.14 , pp. 95-106
    • Mishra, M.1    Byrd, M.S.2    Sergeant, S.3    Azad, A.K.4    Parsek, M.R.5    McPhail, L.6    Schlesinger, L.S.7    Wozniak, D.J.8
  • 4
    • 84860188732 scopus 로고    scopus 로고
    • Biosynthesis of the Pseudomonas aeruginosa extracellular polysaccharides, alginate, Pel, and Psl
    • Franklin, M. J., Nivens, D. E., Weadge, J. T., and Howell, P. L. (2011) Biosynthesis of the Pseudomonas aeruginosa extracellular polysaccharides, alginate, Pel, and Psl. Front. Microbiol. 2, 167
    • (2011) Front. Microbiol. , vol.2 , pp. 167
    • Franklin, M.J.1    Nivens, D.E.2    Weadge, J.T.3    Howell, P.L.4
  • 5
    • 36549026048 scopus 로고    scopus 로고
    • Role of polysaccharides in Pseudomonas aeruginosa biofilm development
    • Ryder, C., Byrd, M., and Wozniak, D. J. (2007) Role of polysaccharides in Pseudomonas aeruginosa biofilm development. Curr. Opin. Microbiol. 10, 644-648
    • (2007) Curr. Opin. Microbiol. , vol.10 , pp. 644-648
    • Ryder, C.1    Byrd, M.2    Wozniak, D.J.3
  • 6
    • 84862777354 scopus 로고    scopus 로고
    • The roles of biofilm matrix polysaccharide Psl in mucoid Pseudomonas aeruginosa biofilms
    • Ma, L., Wang, S., Wang, D., Parsek, M. R., and Wozniak, D. J. (2012) The roles of biofilm matrix polysaccharide Psl in mucoid Pseudomonas aeruginosa biofilms. FEMS Immunol. Med. Microbiol. 65, 377-380
    • (2012) FEMS Immunol. Med. Microbiol. , vol.65 , pp. 377-380
    • Ma, L.1    Wang, S.2    Wang, D.3    Parsek, M.R.4    Wozniak, D.J.5
  • 9
    • 33751579323 scopus 로고    scopus 로고
    • Analysis of Pseudomonas aeruginosa conditional psl variants reveals roles for the psl polysaccharide in adhesion and maintaining biofilm structure postattachment
    • Ma, L., Jackson, K. D., Landry, R. M., Parsek, M. R., and Wozniak, D. J. (2006) Analysis of Pseudomonas aeruginosa conditional psl variants reveals roles for the psl polysaccharide in adhesion and maintaining biofilm structure postattachment. J. Bacteriol. 188, 8213-8221
    • (2006) J. Bacteriol. , vol.188 , pp. 8213-8221
    • Ma, L.1    Jackson, K.D.2    Landry, R.M.3    Parsek, M.R.4    Wozniak, D.J.5
  • 10
    • 63449113742 scopus 로고    scopus 로고
    • Assembly and development of the Pseudomonas aeruginosa biofilm matrix
    • Ma, L., Conover, M., Lu, H., Parsek, M. R., Bayles, K., and Wozniak, D. J. (2009) Assembly and development of the Pseudomonas aeruginosa biofilm matrix. PLoS Pathog. 5, e1000354
    • (2009) PLoS Pathog. , vol.5 , pp. e1000354
    • Ma, L.1    Conover, M.2    Lu, H.3    Parsek, M.R.4    Bayles, K.5    Wozniak, D.J.6
  • 12
    • 84873107819 scopus 로고    scopus 로고
    • Synthase-dependent exopolysaccharide secretion in Gram-negative bacteria
    • Whitney, J. C., and Howell, P. L. (2013) Synthase-dependent exopolysaccharide secretion in Gram-negative bacteria. Trends Microbiol. 21, 63-72
    • (2013) Trends Microbiol. , vol.21 , pp. 63-72
    • Whitney, J.C.1    Howell, P.L.2
  • 13
    • 3042856626 scopus 로고    scopus 로고
    • Identification of psl, a locus encoding a potential exopolysaccharide that is essential for Pseudomonas aeruginosa PAO1 biofilm formation
    • Jackson, K. D., Starkey, M., Kremer, S., Parsek, M. R., and Wozniak, D. J. (2004) Identification of psl, a locus encoding a potential exopolysaccharide that is essential for Pseudomonas aeruginosa PAO1 biofilm formation. J. Bacteriol. 186, 4466-4475
    • (2004) J. Bacteriol. , vol.186 , pp. 4466-4475
    • Jackson, K.D.1    Starkey, M.2    Kremer, S.3    Parsek, M.R.4    Wozniak, D.J.5
  • 14
    • 1242297814 scopus 로고    scopus 로고
    • Genes involved in matrix formation in Pseudomonas aeruginosa PA14 biofilms
    • Friedman, L., and Kolter, R. (2004) Genes involved in matrix formation in Pseudomonas aeruginosa PA14 biofilms. Mol. Microbiol. 51, 675-690
    • (2004) Mol. Microbiol. , vol.51 , pp. 675-690
    • Friedman, L.1    Kolter, R.2
  • 15
    • 3042735895 scopus 로고    scopus 로고
    • Two genetic loci produce distinct carbohydrate-rich structural components of the Pseudomonas aeruginosa biofilm matrix
    • Friedman, L., and Kolter, R. (2004) Two genetic loci produce distinct carbohydrate-rich structural components of the Pseudomonas aeruginosa biofilm matrix. J. Bacteriol. 186, 4457-4465
    • (2004) J. Bacteriol. , vol.186 , pp. 4457-4465
    • Friedman, L.1    Kolter, R.2
  • 16
    • 79955969731 scopus 로고    scopus 로고
    • Apo- and cellopentaose-bound structures of the bacterial cellulose synthase subunit BcsZ
    • Mazur, O., and Zimmer, J. (2011) Apo- and cellopentaose-bound structures of the bacterial cellulose synthase subunit BcsZ. J. Biol. Chem. 286, 17601-17606
    • (2011) J. Biol. Chem. , vol.286 , pp. 17601-17606
    • Mazur, O.1    Zimmer, J.2
  • 17
    • 0141484352 scopus 로고    scopus 로고
    • Biofilm formation at the air-liquid interface by the Pseudomonas fluorescens SBW25 wrinkly spreader requires an acetylated form of cellulose
    • Spiers, A. J., Bohannon, J., Gehrig, S. M., and Rainey, P. B. (2003) Biofilm formation at the air-liquid interface by the Pseudomonas fluorescens SBW25 wrinkly spreader requires an acetylated form of cellulose. Mol. Microbiol. 50, 15-27
    • (2003) Mol. Microbiol. , vol.50 , pp. 15-27
    • Spiers, A.J.1    Bohannon, J.2    Gehrig, S.M.3    Rainey, P.B.4
  • 18
    • 0027185230 scopus 로고
    • Characterization of the Pseudomonas aeruginosa alginate lyase gene (algL): Cloning, sequencing, and expression in Escherichia coli
    • Schiller, N. L., Monday, S. R., Boyd, C. M., Keen, N. T., and Ohman, D. E. (1993) Characterization of the Pseudomonas aeruginosa alginate lyase gene (algL): cloning, sequencing, and expression in Escherichia coli. J. Bacteriol. 175, 4780-4789
    • (1993) J. Bacteriol. , vol.175 , pp. 4780-4789
    • Schiller, N.L.1    Monday, S.R.2    Boyd, C.M.3    Keen, N.T.4    Ohman, D.E.5
  • 19
    • 84929282872 scopus 로고    scopus 로고
    • Listeria monocytogenes exopolysaccharide: Origin, structure, biosynthetic machinery and c-di-GMP-dependent regulation
    • Köseoʇlu, V. K., Heiss, C., Azadi, P., Topchiy, E., Guvener, Z. T., Lehmann, T. E., Miller, K. W., and Gomelsky, M. (2015) Listeria monocytogenes exopolysaccharide: origin, structure, biosynthetic machinery and c-di-GMP-dependent regulation. Mol. Microbiol. 96, 728-743
    • (2015) Mol. Microbiol. , vol.96 , pp. 728-743
    • Köseoʇlu, V.K.1    Heiss, C.2    Azadi, P.3    Topchiy, E.4    Guvener, Z.T.5    Lehmann, T.E.6    Miller, K.W.7    Gomelsky, M.8
  • 20
    • 84877994854 scopus 로고    scopus 로고
    • PelA deacetylase activity is required for Pel polysaccharide synthesis in Pseudomonas aeruginosa
    • Colvin, K. M., Alnabelseya, N., Baker, P., Whitney, J. C., Howell, P. L., and Parsek, M. R. (2013) PelA deacetylase activity is required for Pel polysaccharide synthesis in Pseudomonas aeruginosa. J. Bacteriol. 195, 2329-2339
    • (2013) J. Bacteriol. , vol.195 , pp. 2329-2339
    • Colvin, K.M.1    Alnabelseya, N.2    Baker, P.3    Whitney, J.C.4    Howell, P.L.5    Parsek, M.R.6
  • 21
    • 1942443593 scopus 로고    scopus 로고
    • The pgaABCD locus of Escherichia coli promotes the synthesis of a polysaccharide adhesin required for biofilm formation
    • Wang, X., Preston, J. F., 3rd, and Romeo, T. (2004) The pgaABCD locus of Escherichia coli promotes the synthesis of a polysaccharide adhesin required for biofilm formation. J. Bacteriol. 186, 2724-2734
    • (2004) J. Bacteriol. , vol.186 , pp. 2724-2734
    • Wang, X.1    Preston, J.F.2    Romeo, T.3
  • 22
    • 0036214650 scopus 로고    scopus 로고
    • Molecular biology of cellulose production in bacteria
    • Römling, U. (2002) Molecular biology of cellulose production in bacteria. Res. Microbiol. 153, 205-212
    • (2002) Res. Microbiol. , vol.153 , pp. 205-212
    • Römling, U.1
  • 23
    • 0036263285 scopus 로고    scopus 로고
    • Adaptive divergence in experimental populations of Pseudomonas fluorescens. I. Genetic and phenotypic bases of wrinkly spreader fitness
    • Spiers, A. J., Kahn, S. G., Bohannon, J., Travisano, M., and Rainey, P. B. (2002) Adaptive divergence in experimental populations of Pseudomonas fluorescens. I. Genetic and phenotypic bases of wrinkly spreader fitness. Genetics 161, 33-46
    • (2002) Genetics , vol.161 , pp. 33-46
    • Spiers, A.J.1    Kahn, S.G.2    Bohannon, J.3    Travisano, M.4    Rainey, P.B.5
  • 24
    • 28844451839 scopus 로고    scopus 로고
    • Role of the Pseudomonas fluorescens alginate lyase (AlgL) in clearing the periplasm of alginates not exported to the extracellular environment
    • Bakkevig, K., Sletta, H., Gimmestad, M., Aune, R., Ertesvåg, H., Degnes, K., Christensen, B. E., Ellingsen, T. E., and Valla, S. (2005) Role of the Pseudomonas fluorescens alginate lyase (AlgL) in clearing the periplasm of alginates not exported to the extracellular environment. J. Bacteriol. 187, 8375-8384
    • (2005) J. Bacteriol. , vol.187 , pp. 8375-8384
    • Bakkevig, K.1    Sletta, H.2    Gimmestad, M.3    Aune, R.4    Ertesvåg, H.5    Degnes, K.6    Christensen, B.E.7    Ellingsen, T.E.8    Valla, S.9
  • 25
    • 47049129510 scopus 로고    scopus 로고
    • Roles of pgaABCD genes in synthesis, modification, and export of the Escherichia coli biofilm adhesin poly-β-1,6-N-acetyl-D-glucosamine
    • Itoh, Y., Rice, J. D., Goller, C., Pannuri, A., Taylor, J., Meisner, J., Beveridge, T. J., Preston, J. F., 3rd, and Romeo, T. (2008) Roles of pgaABCD genes in synthesis, modification, and export of the Escherichia coli biofilm adhesin poly-β-1,6-N-acetyl-D-glucosamine. J. Bacteriol. 190, 3670-3680
    • (2008) J. Bacteriol. , vol.190 , pp. 3670-3680
    • Itoh, Y.1    Rice, J.D.2    Goller, C.3    Pannuri, A.4    Taylor, J.5    Meisner, J.6    Beveridge, T.J.7    Preston, J.F.8    Romeo, T.9
  • 26
    • 63849263023 scopus 로고    scopus 로고
    • Pivotal roles of the outer membrane polysaccharide export and polysaccharide copolymerase protein families in export of extracellular polysaccharides in Gram-negative bacteria
    • Cuthbertson, L., Mainprize, I. L., Naismith, J. H., and Whitfield, C. (2009) Pivotal roles of the outer membrane polysaccharide export and polysaccharide copolymerase protein families in export of extracellular polysaccharides in Gram-negative bacteria. Microbiol. Mol. Biol. Rev. 73, 155-177
    • (2009) Microbiol. Mol. Biol. Rev. , vol.73 , pp. 155-177
    • Cuthbertson, L.1    Mainprize, I.L.2    Naismith, J.H.3    Whitfield, C.4
  • 27
    • 33746356503 scopus 로고    scopus 로고
    • Biosynthesis and assembly of capsular polysaccharides in Escherichia coli
    • Whitfield, C. (2006) Biosynthesis and assembly of capsular polysaccharides in Escherichia coli. Annu. Rev. Biochem. 75, 39-68
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 39-68
    • Whitfield, C.1
  • 30
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., Larsson, B., von Heijne, G., and Sonnhammer, E. L. (2001) Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305, 567-580
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 31
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • Petersen, T. N., Brunak, S., von Heijne, G., and Nielsen, H. (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat. Methods 8, 785-786
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 32
    • 23044461889 scopus 로고    scopus 로고
    • An improved method for rapid generation of unmarked Pseudomonas aeruginosa deletion mutants
    • Choi, K. H., and Schweizer, H. P. (2005) An improved method for rapid generation of unmarked Pseudomonas aeruginosa deletion mutants. BMC Microbiol. 5, 30
    • (2005) BMC Microbiol. , vol.5 , pp. 30
    • Choi, K.H.1    Schweizer, H.P.2
  • 33
    • 0032575051 scopus 로고    scopus 로고
    • A broad-host-range Flp-FRT recombination system for sitespecific excision of chromosomally-located DNA sequences: Application for isolation of unmarked Pseudomonas aeruginosa mutants
    • Hoang, T. T., Karkhoff-Schweizer, R. R., Kutchma, A. J., and Schweizer, H. P. (1998) A broad-host-range Flp-FRT recombination system for sitespecific excision of chromosomally-located DNA sequences: application for isolation of unmarked Pseudomonas aeruginosa mutants. Gene 212, 77-86
    • (1998) Gene , vol.212 , pp. 77-86
    • Hoang, T.T.1    Karkhoff-Schweizer, R.R.2    Kutchma, A.J.3    Schweizer, H.P.4
  • 34
    • 0028358260 scopus 로고
    • Analysis and construction of stable phenotypes in gram-negative bacteria with Tn5- and Tn10-derived minitransposons
    • de Lorenzo, V., and Timmis, K. N. (1994) Analysis and construction of stable phenotypes in gram-negative bacteria with Tn5- and Tn10-derived minitransposons. Methods Enzymol. 235, 386-405
    • (1994) Methods Enzymol. , vol.235 , pp. 386-405
    • De Lorenzo, V.1    Timmis, K.N.2
  • 35
    • 0028271237 scopus 로고
    • Subcellular localization of Clostridium thermocellum ORF3p, a protein carrying a receptor for the docking sequence borne by the catalytic components of the cellulosome
    • Salamitou, S., Lemaire, M., Fujino, T., Ohayon, H., Gounon, P., Béguin, P., and Aubert, J. P. (1994) Subcellular localization of Clostridium thermocellum ORF3p, a protein carrying a receptor for the docking sequence borne by the catalytic components of the cellulosome. J. Bacteriol. 176, 2828-2834
    • (1994) J. Bacteriol. , vol.176 , pp. 2828-2834
    • Salamitou, S.1    Lemaire, M.2    Fujino, T.3    Ohayon, H.4    Gounon, P.5    Béguin, P.6    Aubert, J.P.7
  • 36
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
  • 41
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter, J., and Merritt, E. A. (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr. D Biol. Crystallogr. 62, 439-450
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 42
    • 33645158291 scopus 로고    scopus 로고
    • TLSMD web server for the generation of multi-group TLS models
    • Painter, J., and Merritt, E. A. (2006) TLSMD web server for the generation of multi-group TLS models. J. Appl. Crystallogr. 39, 109-111
    • (2006) J. Appl. Crystallogr. , vol.39 , pp. 109-111
    • Painter, J.1    Merritt, E.A.2
  • 43
    • 34547559704 scopus 로고    scopus 로고
    • PDB2PQR: Expanding and upgrading automated preparation of biomolecular structures for molecular simulations
    • Dolinsky, T. J., Czodrowski, P., Li, H., Nielsen, J. E., Jensen, J. H., Klebe, G., and Baker, N. A. (2007) PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations. Nucleic Acids Res. 35, W522-W525
    • (2007) Nucleic Acids Res. , vol.35 , pp. W522-W525
    • Dolinsky, T.J.1    Czodrowski, P.2    Li, H.3    Nielsen, J.E.4    Jensen, J.H.5    Klebe, G.6    Baker, N.A.7
  • 44
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • Dolinsky, T. J., Nielsen, J. E., McCammon, J. A., and Baker, N. A. (2004) PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res. 32, W665-W667
    • (2004) Nucleic Acids Res. , vol.32 , pp. W665-W667
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 46
    • 77954257799 scopus 로고    scopus 로고
    • Con-Surf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy, H., Erez, E., Martz, E., Pupko, T., and Ben-Tal, N. (2010) Con-Surf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res. 38, W529-W533
    • (2010) Nucleic Acids Res. , vol.38 , pp. W529-W533
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 49
    • 0037096082 scopus 로고    scopus 로고
    • Determination of reducing sugars with 3-methyl-2-benzothiazolinonehydrazone
    • Anthon, G. E., and Barrett, D. M. (2002) Determination of reducing sugars with 3-methyl-2-benzothiazolinonehydrazone. Anal. Biochem. 305, 287-289
    • (2002) Anal. Biochem. , vol.305 , pp. 287-289
    • Anthon, G.E.1    Barrett, D.M.2
  • 50
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B., and Bairoch, A. (1993) New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293, 781-788
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 52
    • 70350141013 scopus 로고    scopus 로고
    • PilM/N/O/P proteins form an inner membrane complex that affects the stability of the Pseudomonas aeruginosa type IV pilus secretin
    • Ayers, M., Sampaleanu, L. M., Tammam, S., Koo, J., Harvey, H., Howell, P. L., and Burrows, L. L. (2009) PilM/N/O/P proteins form an inner membrane complex that affects the stability of the Pseudomonas aeruginosa type IV pilus secretin. J. Mol. Biol. 394, 128-142
    • (2009) J. Mol. Biol. , vol.394 , pp. 128-142
    • Ayers, M.1    Sampaleanu, L.M.2    Tammam, S.3    Koo, J.4    Harvey, H.5    Howell, P.L.6    Burrows, L.L.7
  • 53
    • 0037031264 scopus 로고    scopus 로고
    • A case for reverse protonation: Identification of Glu160 as an acid/base catalyst in Thermoanaerobacterium saccharolyticum β-xylosidase and detailed kinetic analysis of a site-directed mutant
    • Vocadlo, D. J., Wicki, J., Rupitz, K., and Withers, S. G. (2002) A case for reverse protonation: identification of Glu160 as an acid/base catalyst in Thermoanaerobacterium saccharolyticum β-xylosidase and detailed kinetic analysis of a site-directed mutant. Biochemistry 41, 9736-9746
    • (2002) Biochemistry , vol.41 , pp. 9736-9746
    • Vocadlo, D.J.1    Wicki, J.2    Rupitz, K.3    Withers, S.G.4
  • 56
    • 26844535502 scopus 로고    scopus 로고
    • Enzyme-substrate complex structures of a GH39β-xylosidase from Geobacillus stearothermophilus
    • Czjzek, M., Ben David, A., Bravman, T., Shoham, G., Henrissat, B., and Shoham, Y. (2005) Enzyme-substrate complex structures of a GH39β-xylosidase from Geobacillus stearothermophilus. J. Mol. Biol. 353, 838-846
    • (2005) J. Mol. Biol. , vol.353 , pp. 838-846
    • Czjzek, M.1    Ben David, A.2    Bravman, T.3    Shoham, G.4    Henrissat, B.5    Shoham, Y.6
  • 57
    • 0037709362 scopus 로고    scopus 로고
    • Family 39 α-L-iduronidases and β-D-xylosidases react through similar glycosyl-enzyme intermediates: Identification of the human iduronidase nucleophile
    • Nieman, C. E., Wong, A. W., He, S., Clarke, L., Hopwood, J. J., and Withers, S. G. (2003) Family 39 α-L-iduronidases and β-D-xylosidases react through similar glycosyl-enzyme intermediates: identification of the human iduronidase nucleophile. Biochemistry 42, 8054-8065
    • (2003) Biochemistry , vol.42 , pp. 8054-8065
    • Nieman, C.E.1    Wong, A.W.2    He, S.3    Clarke, L.4    Hopwood, J.J.5    Withers, S.G.6
  • 58
    • 0032532593 scopus 로고    scopus 로고
    • Identification of Glu-277 as the catalytic nucleophile of Thermoanaerobacterium saccharolyticum β-xylosidase using electrospray MS
    • Vocadlo, D. J., MacKenzie, L. F., He, S., Zeikus, G. J., and Withers, S. G. (1998) Identification of Glu-277 as the catalytic nucleophile of Thermoanaerobacterium saccharolyticum β-xylosidase using electrospray MS. Biochem. J. 335, 449-455
    • (1998) Biochem. J. , vol.335 , pp. 449-455
    • Vocadlo, D.J.1    MacKenzie, L.F.2    He, S.3    Zeikus, G.J.4    Withers, S.G.5
  • 60
    • 84866668560 scopus 로고    scopus 로고
    • The accessory domain changes the accessibility and molecular topography of the catalytic interface in monomeric GH39 β-xylosidases
    • Santos, C. R., Polo, C. C., Corrêa, J. M., Simão Rde, C., Seixas, F. A., and Murakami, M. T. (2012) The accessory domain changes the accessibility and molecular topography of the catalytic interface in monomeric GH39 β-xylosidases. Acta Crystallogr. D Biol. Crystallogr. 68, 1339-1345
    • (2012) Acta Crystallogr. D Biol. Crystallogr. , vol.68 , pp. 1339-1345
    • Santos, C.R.1    Polo, C.C.2    Corrêa, J.M.3    Simão-Rde, C.4    Seixas, F.A.5    Murakami, M.T.6
  • 61
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • Dundas, J., Ouyang, Z., Tseng, J., Binkowski, A., Turpaz, Y., and Liang, J. (2006) CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acids Res. 34, W116-W118
    • (2006) Nucleic Acids Res. , vol.34 , pp. W116-W118
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 62
    • 0041989751 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins
    • Binkowski, T. A., Naghibzadeh, S., and Liang, J. (2003) CASTp: computed atlas of surface topography of proteins. Nucleic Acids Res. 31, 3352-3355
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3352-3355
    • Binkowski, T.A.1    Naghibzadeh, S.2    Liang, J.3
  • 65
    • 84866334862 scopus 로고    scopus 로고
    • Synthesis of long-chain chitooligosaccharides by a hypertransglycosylating processive endochitinase of Serratia proteamaculans 568
    • Purushotham, P., and Podile, A. R. (2012) Synthesis of long-chain chitooligosaccharides by a hypertransglycosylating processive endochitinase of Serratia proteamaculans 568. J. Bacteriol. 194, 4260-4271
    • (2012) J. Bacteriol. , vol.194 , pp. 4260-4271
    • Purushotham, P.1    Podile, A.R.2
  • 66
    • 0032574722 scopus 로고    scopus 로고
    • The Rhizobium meliloti ExoK and ExsH glycanases specifically depolymerize nascent succinoglycan chains
    • York, G. M., and Walker, G. C. (1998) The Rhizobium meliloti ExoK and ExsH glycanases specifically depolymerize nascent succinoglycan chains. Proc. Natl. Acad. Sci. U.S.A. 95, 4912-4917
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 4912-4917
    • York, G.M.1    Walker, G.C.2
  • 67
    • 84887086438 scopus 로고    scopus 로고
    • BcsA and BcsB form the catalytically active core of bacterial cellulose synthase sufficient for in vitro cellulose synthesis
    • Omadjela, O., Narahari, A., Strumillo, J., Mélida, H., Mazur, O., Bulone, V., and Zimmer, J. (2013) BcsA and BcsB form the catalytically active core of bacterial cellulose synthase sufficient for in vitro cellulose synthesis. Proc. Natl. Acad. Sci. U.S.A. 110, 17856-17861
    • (2013) Proc. Natl. Acad. Sci. U.S.A , vol.110 , pp. 17856-17861
    • Omadjela, O.1    Narahari, A.2    Strumillo, J.3    Mélida, H.4    Mazur, O.5    Bulone, V.6    Zimmer, J.7
  • 68
    • 84867338465 scopus 로고    scopus 로고
    • Identification of key peptidoglycan hydrolases for morphogenesis, autolysis, and peptidoglycan composition of Lactobacillus plantarum WCFS1
    • Rolain, T., Bernard, E., Courtin, P., Bron, P. A., Kleerebezem, M., Chapot-Chartier, M. P., and Hols, P. (2012) Identification of key peptidoglycan hydrolases for morphogenesis, autolysis, and peptidoglycan composition of Lactobacillus plantarum WCFS1. Microb. Cell Fact. 11, 137
    • (2012) Microb. Cell Fact. , vol.11 , pp. 137
    • Rolain, T.1    Bernard, E.2    Courtin, P.3    Bron, P.A.4    Kleerebezem, M.5    Chapot-Chartier, M.P.6    Hols, P.7
  • 69
    • 84455162073 scopus 로고    scopus 로고
    • Peptidoglycan hydrolases of Escherichia coli
    • van Heijenoort, J. (2011) Peptidoglycan hydrolases of Escherichia coli. Microbiol. Mol. Biol. Rev. 75, 636-663
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , pp. 636-663
    • Van Heijenoort, J.1
  • 70
    • 84886648533 scopus 로고    scopus 로고
    • Afamily 3 glycosyl hydrolase of Dickeya dadantii 3937 is involved in the cleavage of aromatic glucosides
    • Charaoui-Boukerzaza, S., and Hugouvieux-Cotte-Pattat, N. (2013) Afamily 3 glycosyl hydrolase of Dickeya dadantii 3937 is involved in the cleavage of aromatic glucosides. Microbiology 159, 2395-2404
    • (2013) Microbiology , vol.159 , pp. 2395-2404
    • Charaoui-Boukerzaza, S.1    Hugouvieux-Cotte-Pattat, N.2
  • 71
    • 79960855994 scopus 로고    scopus 로고
    • Structural diversity of the core oligosaccharide domain of Pseudomonas aeruginosa lipopolysaccharide
    • Kocíncová, D., and Lam, J. S. (2011) Structural diversity of the core oligosaccharide domain of Pseudomonas aeruginosa lipopolysaccharide. Biochemistry 76, 755-760
    • (2011) Biochemistry , vol.76 , pp. 755-760
    • Kocíncová, D.1    Lam, J.S.2
  • 72
    • 34547531757 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa lipopolysaccharide: A major virulence factor, initiator of inflammation and target for effective immunity
    • Pier, G. B. (2007) Pseudomonas aeruginosa lipopolysaccharide: a major virulence factor, initiator of inflammation and target for effective immunity. Int. J. Med. Microbiol. 297, 277-295
    • (2007) Int. J. Med. Microbiol. , vol.297 , pp. 277-295
    • Pier, G.B.1
  • 73
    • 0032831499 scopus 로고    scopus 로고
    • Genetics of O-antigen biosynthesis in Pseudomonas aeruginosa
    • Rocchetta, H. L., Burrows, L. L., and Lam, J. S. (1999) Genetics of O-antigen biosynthesis in Pseudomonas aeruginosa. Microbiol. Mol. Biol. Rev. 63, 523-553
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 523-553
    • Rocchetta, H.L.1    Burrows, L.L.2    Lam, J.S.3
  • 74
    • 0028215039 scopus 로고
    • Detailed structural characterization of succinoglycan, the major exopolysaccharide of Rhizobium meliloti Rm1021
    • Reinhold, B. B., Chan, S. Y., Reuber, T. L., Marra, A., Walker, G. C., and Reinhold, V. N. (1994) Detailed structural characterization of succinoglycan, the major exopolysaccharide of Rhizobium meliloti Rm1021. J. Bacteriol. 176, 1997-2002
    • (1994) J. Bacteriol. , vol.176 , pp. 1997-2002
    • Reinhold, B.B.1    Chan, S.Y.2    Reuber, T.L.3    Marra, A.4    Walker, G.C.5    Reinhold, V.N.6
  • 75
    • 84883145511 scopus 로고    scopus 로고
    • The succinoglycan endoglycanase encoded by exoK is required for efficient symbiosis of Sinorhizobium meliloti 1021 with the host plants Medicago truncatula and Medicago sativa (Alfalfa)
    • Mendis, H. C., Queiroux, C., Brewer, T. E., Davis, O. M., Washburn, B. K., and Jones, K. M. (2013) The succinoglycan endoglycanase encoded by exoK is required for efficient symbiosis of Sinorhizobium meliloti 1021 with the host plants Medicago truncatula and Medicago sativa (Alfalfa). Mol. Plant Microbe Interact. 26, 1089-1105
    • (2013) Mol. Plant Microbe Interact. , vol.26 , pp. 1089-1105
    • Mendis, H.C.1    Queiroux, C.2    Brewer, T.E.3    Davis, O.M.4    Washburn, B.K.5    Jones, K.M.6
  • 76
    • 0032721976 scopus 로고    scopus 로고
    • Structural characterization of the symbiotically important low-molecular-weight succinoglycan of Sinorhizobium meliloti
    • Wang, L. X., Wang, Y., Pellock, B., and Walker, G. C. (1999) Structural characterization of the symbiotically important low-molecular-weight succinoglycan of Sinorhizobium meliloti. J. Bacteriol. 181, 6788-6796
    • (1999) J. Bacteriol. , vol.181 , pp. 6788-6796
    • Wang, L.X.1    Wang, Y.2    Pellock, B.3    Walker, G.C.4
  • 78
    • 84876342824 scopus 로고    scopus 로고
    • Insights into the role of extracellular polysaccharides in Burkholderia adaptation to different environments
    • Ferreira, A. S., Silva, I. N., Oliveira, V. H., Cunha, R., and Moreira, L. M. (2011) Insights into the role of extracellular polysaccharides in Burkholderia adaptation to different environments. Front. Cell. Infect. Microbiol. 1, 16
    • (2011) Front. Cell. Infect. Microbiol. , vol.1 , pp. 16
    • Ferreira, A.S.1    Silva, I.N.2    Oliveira, V.H.3    Cunha, R.4    Moreira, L.M.5
  • 79
    • 0000271704 scopus 로고
    • Genetic recombination in Pseudomonas aeruginosa
    • Holloway, B. W. (1955) Genetic recombination in Pseudomonas aeruginosa. J. Gen. Microbiol. 13, 572-581
    • (1955) J. Gen. Microbiol. , vol.13 , pp. 572-581
    • Holloway, B.W.1
  • 80
    • 20344403312 scopus 로고    scopus 로고
    • ExsE, a secreted regulator of type III secretion genes in Pseudomonas aeruginosa
    • Rietsch, A., Vallet-Gely, I., Dove, S. L., and Mekalanos, J. J. (2005) ExsE, a secreted regulator of type III secretion genes in Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. U.S.A. 102, 8006-8011
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 8006-8011
    • Rietsch, A.1    Vallet-Gely, I.2    Dove, S.L.3    Mekalanos, J.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.