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Volumn 4, Issue 4-5, 2004, Pages 417-425

Yeast cells harboring human α-1,3-fucosyltransferase at the cell surface engineered using Pir, a cell wall-anchored protein

Author keywords

Fucosyltransferase; Intact cell enzyme; Oligosaccharide synthesis; Pir; Saccharomyces cerevisiae

Indexed keywords

ALPHA 1,3 FUCOSYLTRANSFERASE; CELL MEMBRANE PROTEIN; FUNGAL PROTEIN; GLYCOSYLTRANSFERASE; HYBRID PROTEIN; OLIGOSACCHARIDE; PROTEIN PIR; UNCLASSIFIED DRUG;

EID: 0742321954     PISSN: 15671356     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1567-1356(03)00193-4     Document Type: Article
Times cited : (22)

References (31)
  • 1
    • 0026655074 scopus 로고
    • Enzyme-catalyzed oligosaccharide synthesis
    • Ichikawa Y., Look G., Wong C.-H. Enzyme-catalyzed oligosaccharide synthesis. Anal. Biochem. 202:1992;215-238.
    • (1992) Anal. Biochem. , vol.202 , pp. 215-238
    • Ichikawa, Y.1    Look, G.2    Wong, C.-H.3
  • 3
    • 0032530914 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of a selectin ligand using recombinant yeast cells
    • Lubineau A., Narvor C., Auge C., Gallet P., Petit J., Julien R. Chemoenzymatic synthesis of a selectin ligand using recombinant yeast cells. J. Mol. Catal. 5:1998;229-234.
    • (1998) J. Mol. Catal. , vol.5 , pp. 229-234
    • Lubineau, A.1    Narvor, C.2    Auge, C.3    Gallet, P.4    Petit, J.5    Julien, R.6
  • 4
    • 0034614594 scopus 로고    scopus 로고
    • Expression of functional soluble forms of human β-1,4- galactosyltransferase I, α-2,6-sialyltransferase, and α-1,3- fucosyltransferase VI in the methylotrophic yeast Pichia pastoris
    • Malissard M., Zeng S., Berger E.G. Expression of functional soluble forms of human β-1,4-galactosyltransferase I, α-2,6- sialyltransferase, and α-1,3-fucosyltransferase VI in the methylotrophic yeast Pichia pastoris. Biochem. Biophys. Res. Commun. 267:2000;169-173.
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 169-173
    • Malissard, M.1    Zeng, S.2    Berger, E.G.3
  • 5
    • 0032861961 scopus 로고    scopus 로고
    • The yeast expression system for recombinant glycosyltransferases
    • Malissard M., Zeng S., Berger E.G. The yeast expression system for recombinant glycosyltransferases. Glycoconj. J. 16:1999;125-139.
    • (1999) Glycoconj. J. , vol.16 , pp. 125-139
    • Malissard, M.1    Zeng, S.2    Berger, E.G.3
  • 6
    • 0028964058 scopus 로고
    • Use of transformed whole yeast cells expressing β-1,4- galactosyltransferase for the synthesis of N-acetyllactosamine
    • Herrmann G.F., Lothar E., Krezdorn C.H., Ralf K., Berger E.G., Christian W. Use of transformed whole yeast cells expressing β-1,4- galactosyltransferase for the synthesis of N-acetyllactosamine. Bioorg. Med. Chem. Lett. 5:1995;673-676.
    • (1995) Bioorg. Med. Chem. Lett. , vol.5 , pp. 673-676
    • Herrmann, G.F.1    Lothar, E.2    Krezdorn, C.H.3    Ralf, K.4    Berger, E.G.5    Christian, W.6
  • 7
    • 0037322147 scopus 로고    scopus 로고
    • In vitro oligosaccharide synthesis using intact yeast cells that display glycosyltransferases at the cell surface through cell wall-anchored protein Pir
    • Abe H., Shimma Y., Jigami Y. In vitro oligosaccharide synthesis using intact yeast cells that display glycosyltransferases at the cell surface through cell wall-anchored protein Pir. Glycobiology. 13:2003;87-95.
    • (2003) Glycobiology , vol.13 , pp. 87-95
    • Abe, H.1    Shimma, Y.2    Jigami, Y.3
  • 8
    • 0027208062 scopus 로고
    • Three yeast genes, PIR1, PIR2 and PIR3, containing internal tandem repeats, are related to each other, and PIR1 and PIR2 are required for tolerance to heat shock
    • Toh-e A., Yasunaga S., Nisogi H., Tanaka K., Oguchi T., Matsui Y. Three yeast genes, PIR1, PIR2 and PIR3, containing internal tandem repeats, are related to each other, and PIR1 and PIR2 are required for tolerance to heat shock. Yeast. 9:1993;481-494.
    • (1993) Yeast , vol.9 , pp. 481-494
    • Toh-E, A.1    Yasunaga, S.2    Nisogi, H.3    Tanaka, K.4    Oguchi, T.5    Matsui, Y.6
  • 9
    • 0032816832 scopus 로고    scopus 로고
    • Identification of two mannoproteins released from cell walls of a Saccharomyces cerevisiae mnn1 mnn9 double mutant by reducing agents
    • Moukadiri I., Jaafar L., Zueco J. Identification of two mannoproteins released from cell walls of a Saccharomyces cerevisiae mnn1 mnn9 double mutant by reducing agents. J. Bacteriol. 181:1999;4741-4745.
    • (1999) J. Bacteriol. , vol.181 , pp. 4741-4745
    • Moukadiri, I.1    Jaafar, L.2    Zueco, J.3
  • 10
    • 0030883927 scopus 로고    scopus 로고
    • Specific labelling of cell wall proteins by biotinylation. Identification of four covalently linked O-mannosylated proteins of Saccharomyces cerevisiae
    • Mrsa V., Seidl T., Gentzsch M., Tanner W. Specific labelling of cell wall proteins by biotinylation. Identification of four covalently linked O-mannosylated proteins of Saccharomyces cerevisiae. Yeast. 13:1997;1145-1154.
    • (1997) Yeast , vol.13 , pp. 1145-1154
    • Mrsa, V.1    Seidl, T.2    Gentzsch, M.3    Tanner, W.4
  • 12
    • 0025076540 scopus 로고
    • A cloned human cDNA determines expression of a mouse stage-specific embryonic antigen and the Lewis blood group α(1,3/1,4)fucosyltransferase
    • Kukowska-Latallo J.F., Larsen R.D., Nair R.P., Lowe J.B. A cloned human cDNA determines expression of a mouse stage-specific embryonic antigen and the Lewis blood group α(1,3/1,4)fucosyltransferase. Genes Dev. 4:1990;1288-1303.
    • (1990) Genes Dev. , vol.4 , pp. 1288-1303
    • Kukowska-Latallo, J.F.1    Larsen, R.D.2    Nair, R.P.3    Lowe, J.B.4
  • 13
    • 0026672572 scopus 로고
    • The cloning and expression of a human α-1,3 fucosyltransferase capable of forming the E-selectin ligand
    • Koszdin K.L., Bowen B.R. The cloning and expression of a human α-1,3 fucosyltransferase capable of forming the E-selectin ligand. Biochem. Biophys. Res. Commun. 187:1992;152-157.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 152-157
    • Koszdin, K.L.1    Bowen, B.R.2
  • 14
    • 0026759584 scopus 로고
    • Isolation of a novel human α(1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group α(1,3/1,4) fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities
    • Weston B.W., Nair R.P., Larsen R.D., Lowe J.B. Isolation of a novel human α(1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group α(1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities. J. Biol. Chem. 267:1992;4152-4160.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4152-4160
    • Weston, B.W.1    Nair, R.P.2    Larsen, R.D.3    Lowe, J.B.4
  • 15
    • 0028275940 scopus 로고
    • Expression cloning of a novel α1,3-fucosyltransferase that is involved in biosynthesis of the sialyl Lewis x carbohydrate determinants in leukocytes
    • Sasaki K., Kurata K., Funayama K., Nagata M., Watanabe E., Ohta S., Hanai N., Nishi T. Expression cloning of a novel α1,3-fucosyltransferase that is involved in biosynthesis of the sialyl Lewis x carbohydrate determinants in leukocytes. J. Biol. Chem. 269:1994;14730-14737.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14730-14737
    • Sasaki, K.1    Kurata, K.2    Funayama, K.3    Nagata, M.4    Watanabe, E.5    Ohta, S.6    Hanai, N.7    Nishi, T.8
  • 16
    • 0028292790 scopus 로고
    • Molecular cloning of a cDNA encoding a novel human leukocyte α-1,3-fucosyltransferase capable of synthesizing the sialyl Lewis x determinant
    • Natsuka S., Gersten K.M., Zenita K., Kannagi R., Lowe J.B. Molecular cloning of a cDNA encoding a novel human leukocyte α-1,3- fucosyltransferase capable of synthesizing the sialyl Lewis x determinant. J. Biol. Chem. 269:1994;16789-16794.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16789-16794
    • Natsuka, S.1    Gersten, K.M.2    Zenita, K.3    Kannagi, R.4    Lowe, J.B.5
  • 17
    • 0032586973 scopus 로고    scopus 로고
    • α 1,3-fucosyltransferase IX (Fuc-TIX) is very highly conserved between human and mouse; Molecular cloning, characterization and tissue distribution of human Fuc-TIX
    • Kaneko M., Kudo T., Iwasaki H., Ikehara Y., Nishihara S., Nakagawa S., Sasaki K., Shiina T., Inoko H., Saitou N., Narimatsu H. α 1,3-fucosyltransferase IX (Fuc-TIX) is very highly conserved between human and mouse; molecular cloning, characterization and tissue distribution of human Fuc-TIX. FEBS Lett. 452:1999;237-242.
    • (1999) FEBS Lett. , vol.452 , pp. 237-242
    • Kaneko, M.1    Kudo, T.2    Iwasaki, H.3    Ikehara, Y.4    Nishihara, S.5    Nakagawa, S.6    Sasaki, K.7    Shiina, T.8    Inoko, H.9    Saitou, N.10    Narimatsu, H.11
  • 18
    • 0023657264 scopus 로고
    • The GDP-fucose:N-acetylglucosaminide 3-α-L-fucosyltransferases of LEC11 and LEC12 Chinese hamster ovary mutants exhibit novel specificities for glycolipid substrates
    • Howard D.R., Fukuda M., Fukuda M.N., Stanley P. The GDP-fucose:N- acetylglucosaminide 3-α-L-fucosyltransferases of LEC11 and LEC12 Chinese hamster ovary mutants exhibit novel specificities for glycolipid substrates. J. Biol. Chem. 262:1987;16830-16837.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16830-16837
    • Howard, D.R.1    Fukuda, M.2    Fukuda, M.N.3    Stanley, P.4
  • 20
    • 0025018353 scopus 로고
    • ELAM-1-dependent cell adhesion to vascular endothelium determined by a transfected human fucosyltransferase cDNA
    • Lowe J.B., Stoolman L.M., Nair R.P., Larsen R.D., Berhend T.L., Marks R.M. ELAM-1-dependent cell adhesion to vascular endothelium determined by a transfected human fucosyltransferase cDNA. Cell. 63:1990;475-484.
    • (1990) Cell , vol.63 , pp. 475-484
    • Lowe, J.B.1    Stoolman, L.M.2    Nair, R.P.3    Larsen, R.D.4    Berhend, T.L.5    Marks, R.M.6
  • 21
    • 0026724918 scopus 로고
    • Comparison of L-selectin and E-selectin ligand specificities: The L-selectin can bind the E-selectin ligands sialyl Le(x) and sialyl Le(a)
    • Berg E.L., Magnani J., Warnock R.A., Robinson M.K., Butcher E.C. Comparison of L-selectin and E-selectin ligand specificities: the L-selectin can bind the E-selectin ligands sialyl Le(x) and sialyl Le(a). Biochem. Biophys. Res. Commun. 184:1992;1048-1055.
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 1048-1055
    • Berg, E.L.1    Magnani, J.2    Warnock, R.A.3    Robinson, M.K.4    Butcher, E.C.5
  • 22
    • 0026763332 scopus 로고
    • The three members of the selectin receptor family recognize a common carbohydrate epitope, the sialyl Lewis(x) oligosaccharide
    • Foxall C., Watson S.R., Dowbenko D., Fennie C., Lasky L.A., Kiso M., Hasegawa A., Asa D., Brandley B.K. The three members of the selectin receptor family recognize a common carbohydrate epitope, the sialyl Lewis(x) oligosaccharide. J. Cell. Biol. 117:1992;895-902.
    • (1992) J. Cell. Biol. , vol.117 , pp. 895-902
    • Foxall, C.1    Watson, S.R.2    Dowbenko, D.3    Fennie, C.4    Lasky, L.A.5    Kiso, M.6    Hasegawa, A.7    Asa, D.8    Brandley, B.K.9
  • 23
    • 0032553325 scopus 로고    scopus 로고
    • x motifs on complex-type N-glycans. Coexpression studies from BHK-21 cells together with human β-trace protein
    • x motifs on complex-type N-glycans. Coexpression studies from BHK-21 cells together with human β-trace protein. J. Biol. Chem. 273:1998;30985-30994.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30985-30994
    • Grabenhorst, E.1    Nimtz, M.2    Costa, J.3    Conradt, H.S.4
  • 24
    • 0031559578 scopus 로고    scopus 로고
    • Distinct substrate specificities of five human α-1,3- fucosyltransferases for in vivo synthesis of the sialyl Lewis x and Lewis x epitope
    • Kimura H., Shinya N., Nishihara S., Kaneko M., Irimura T., Narimatsu H. Distinct substrate specificities of five human α-1,3-fucosyltransferases for in vivo synthesis of the sialyl Lewis x and Lewis x epitope. Biochem. Biophys. Res. Commun. 237:1997;131-137.
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 131-137
    • Kimura, H.1    Shinya, N.2    Nishihara, S.3    Kaneko, M.4    Irimura, T.5    Narimatsu, H.6
  • 25
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman F. Getting started with yeast. Methods Enzymol. 194:1991;3-21.
    • (1991) Methods Enzymol. , vol.194 , pp. 3-21
    • Sherman, F.1
  • 26
    • 0021071824 scopus 로고
    • A general method for polyethylene-glycol-induced genetic transformation of bacteria and yeast
    • Klebe R.J., Harriss J.V., Sharp Z.D., Douglas M.G. A general method for polyethylene-glycol-induced genetic transformation of bacteria and yeast. Gene. 25:1983;333-341.
    • (1983) Gene , vol.25 , pp. 333-341
    • Klebe, R.J.1    Harriss, J.V.2    Sharp, Z.D.3    Douglas, M.G.4
  • 27
    • 0023392267 scopus 로고
    • A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains
    • Alani E., Cao L., Kleckner N. A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains. Genetics. 116:1987;541-545.
    • (1987) Genetics , vol.116 , pp. 541-545
    • Alani, E.1    Cao, L.2    Kleckner, N.3
  • 28
    • 0034682464 scopus 로고    scopus 로고
    • Localization of α1,3-fucosyltransferase VI in Weibel-Palade bodies of human endothelial cells
    • Schnyder-Candrian S., Borsig L., Moser R., Berger E. Localization of α1,3-fucosyltransferase VI in Weibel-Palade bodies of human endothelial cells. Proc. Natl. Acad. Sci. USA. 97:2000;8369-8374.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8369-8374
    • Schnyder-Candrian, S.1    Borsig, L.2    Moser, R.3    Berger, E.4
  • 29
    • 0345621646 scopus 로고    scopus 로고
    • Role of NaOH-extractable cell wall proteins Ccw5p, Ccw6p, Ccw7p and Ccw8p (members of the Pir protein family) in stability of the Saccharomyces cerevisiae cell wall
    • Mrsa V., Tanner W. Role of NaOH-extractable cell wall proteins Ccw5p, Ccw6p, Ccw7p and Ccw8p (members of the Pir protein family) in stability of the Saccharomyces cerevisiae cell wall. Yeast. 15:1999;813-820.
    • (1999) Yeast , vol.15 , pp. 813-820
    • Mrsa, V.1    Tanner, W.2
  • 30
    • 0033038844 scopus 로고    scopus 로고
    • The contribution of the O-glycosylated protein Pir2p/Hsp150 to the construction of the yeast cell wall in wild-type cells and β1,6-glucan- deficient mutants
    • Kapteyn J.C., Van Egmond P., Sievi E., Van Den Ende H., Makarow M., Klis F.M. The contribution of the O-glycosylated protein Pir2p/Hsp150 to the construction of the yeast cell wall in wild-type cells and β1,6-glucan- deficient mutants. Mol. Microbiol. 31:1999;1835-1844.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1835-1844
    • Kapteyn, J.C.1    Van Egmond, P.2    Sievi, E.3    Van Den Ende, H.4    Makarow, M.5    Klis, F.M.6
  • 31
    • 0024977417 scopus 로고
    • Elevated recombination rates in transcriptionally active DNA
    • Thomas B.J., Rothstein R. Elevated recombination rates in transcriptionally active DNA. Cell. 56:1989;619-630.
    • (1989) Cell , vol.56 , pp. 619-630
    • Thomas, B.J.1    Rothstein, R.2


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