Characterization of sialyltransferase mutants using surface plasmon resonance

Glycobiology

Volumn 11, Issue 3, 2001, Pages 175-182

  Laroy, Wouter ^a   Ameloot, Paul ^a   Contreras, Roland ^a,b  

^a DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^b Department of Molecular Biology ^*  (Belgium)

Author keywords

CMP NeuAc; Glycoconjugate; Sialyltransferase; ST6GalI; Surface plasmon resonance

Indexed keywords

ACYLNEURAMINATE CYTIDYLYLTRANSFERASE; ASIALOFETUIN; GLYCOCONJUGATE; GLYCOSYLTRANSFERASE; MUTANT PROTEIN; SIALYLTRANSFERASE; SODIUM CHLORIDE;

AFFINITY CHROMATOGRAPHY; ANIMAL CELL; ARTICLE; BINDING AFFINITY; BINDING SITE; CATALYSIS; CHEMICAL INTERACTION; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; MODEL; MONKEY; MUTANT; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; SIALYLATION; SURFACE PLASMON RESONANCE;

ANIMALIA;

EID: 0035018012     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/11.3.175     Document Type: Article

References (34)

1. Birnboim, H.C. and Doly, J. (1979) A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res., 7, 1513-1523.
2. Chen, C. and Okayama, H. (1987) High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol., 7, 2745-2752.
3. Colley, K.J., Lee, E.U., Adler, B., Browne, J.K., and Paulson, J.C. (1989) Conversion of a Golgi apparatus sialyltransferase to a secretory protein by replacement of the NH2-terminal signal anchor with a signal peptide. J. Biol. Chem., 264, 17619-17622.
4. Datta, A.K. and Paulson, J.C. (1995) The sialyltransferase "sialylmotif" participates in binding the donor substrate CMP-NeuAc. J. Biol. Chem., 270, 1497-1500.
5. Datta, A.K. and Paulson, J.C. (1997) Sialylmotifs of sialyltransferases. Indian J. Biochem. Bio., 34, 157-165.
6. Datta, A.K., Sinha, A., and Paulson, J.C. (1998) Mutation of the sialyltransferase S-sialylmotif alters the kinetics of the donor and acceptor substrates. J. Biol. Chem., 273, 9608-9614.
7. Fagerstam, L., Ivarsson, B., Johnsson, B., Karlsson, R., Lofas, S., Lundh, K., Malmquist, M., Ostlin, H., Persson, B., Ronnberg, I., and others. (1991) Real-time biospecific interaction analysis using surface plasmon resonance and a sensor chip technology. Biotechniques, 11, 620-627.
8. Field, M.C. and Wainwright, L.J. (1995) Molecular cloning of eukaryotic glycoprotein and glycolipid glycosyltransferases: A survey. Glycobiology, 5, 463-472.
9. Gastinel, L.N., Cambillau, C., and Bourne, Y. (1999) Crystal structures of the bovine β4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose. Embo J., 18, 3546-3557.
10. Giordanengo, V., Bannwarth, S., Laffont, C., VanMiegem, V., Harduin-Lepers, A., Delannoy, P., and Lefebvre, J.C. (1997) Cloning and expression of cDNA for a human Gal(beta 1-3)GalNAc alpha 2,3-sialyltransferase from the CEM T-cell line. Eur. J. Biochem., 247, 558-566.
11. Grundmann, U., Nerlich, C., Rein, T., and Zettlmeissl, G. (1990) Complete cDNA sequence encoding human β-galactoside α-2,6-sialyltransferase. Nucleic Acids Res., 18, 667.
12. Harduin-Lepers, A., Recchi, M.A., and Delannoy, P. (1995) 1994, the year of sialyltransferases. Glycobiology, 5, 741-758.
13. Hutchinson, A.M. (1994) Characterization of glycoprotein oligosaccharides using surface plasmon resonance. Anal. Biochem., 220, 303-307.
14. Johnsson, B., Lofas, S., and Lindquist, G. (1991) Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in the surface plasmon resonance sensors. Anal. Biochem., 198, 268-277.
15. Kitazume-Kawaguchi, S., Dohmae, N., Takio, K., Tsuji, S., and Colley, K.J. (1999) The relationship between ST6GalI Golgi retention and its cleavage-secretion. Glycobiology, 9, 1397-1406.
16. Kleene, R. and Berger, E.G. (1993) The molecular and cell biology of glycosyltransferases. Biochim. Biophys. Acta, 1154, 283-325.
17. Laroy, W., Maras, M., Fiers, W., and Contreras, R. (1997) A radioactive assay for sialyltransferase activity using 96-well multiscreen filtration plates. Anal. Biochem., 249, 108-111.
18. Leung, D.W., Chen, E., and Goeddel, D.V. (1989) Error prone PCR. Technique, 1, 11-15.
19. Ma, J., Qian, R., Rausa, F.M., and Colley, K.J. (1997) Two naturally occurring 2,6-sialyltransferase forms with a single amino acid change in the catalytic domain. J. Biol. Chem., 272, 672-679.
20. Mattox, S., Walrath, K., Ceiler, D., Smith, D.F., and Cummings, R.D. (1992) A solid-phase assay for the activity of CMPNeuAc:Gal β1-4GlcNAc-R α-2,6-sialyltransferase. Anal. Biochem., 206, 430-436.
21. Niwa, H., Yamamura, K., and Miyazaki, J. (1991) Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene, 108, 193-199.
22. Paulson, J.C. and Colley, K.J. (1989) Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation. J. Biol. Chem., 264, 17615-17618.
23. Paulson, J.C., Beranek, W.E., and Hill, R.L. (1977) purification of a sialyltransferase from colostrums by chromatography on CDP-agarose. J. Biol. Chem., 252, 2356-2362.
24. Samyn-Petit, B., Krzewinski-Recchi, M.A., Steelant, W.F.A., Delannoy, P., and Harduin-Lepers, A. (2000) Molecular cloning and functional expression of human ST6GalNAcII. Molecular expression in various human cultured cells. Biochim. Biophys. Acta, 1474, 201-211.
25. Sanger, F., Nicklen, S., and Coulson, A.R. (1977) DNA sequencing with chain-terminating inhibitors. Proc. Natl Acad. Sci. USA, 74, 5463-5467.
26. Takasaki, S. and Kobata, A. (1986) Asparagine-linked sugar chains of fetuin: Occurrence of tetrasialyl triantennary sugar chains containing the Galβ1-3GlcNAc sequence. Biochemistry, 25, 5709-5715.
27. Tsuji, S. (1996) Molecular cloning and functional analysis of sialyltransferases. J. Biochem. (Tokyo), 120, 1-13.
28. Tsuji, S. (1999l Molecular cloning and characterization of mouse sialyltransferases. In Inoue, Y., Lee, Y.C., and Troy II, F.A. (eds), Sialobiology and Other Novel Forms of Glycosylation, Gakushin Publishing Company, Osaka, pp. 145-154.
29. Varki, A. (1993) Biological roles of oligosaccharides: All of the theories are correct. Glycobiology, 3, 97-130.
30. Wang, X., O'Hanlon, T.P., Young, R.F., and Lau, J.T. (1990) Rat β-galactoside α2,6-sialyltransferase genomic organization: Alternate promoters direct the synthesis of liver and kidney transcripts. Glycobiology, 1, 25-31.
31. Wang, X., Vertino, A., Eddy, R.L., Byers, M.G., Jani-Sait, S.N., Shows, T.B., and Lau, J.T. (1993) Chromosome mapping and organization of the human β-galactosicle α2,6-sialyltransferase gene. Differential and cell-type specific usage of upstream exon sequences in B-lymphoblastoid cells. J. Biol. Chem., 268, 4355-4361.
32. Weinstein, J., de Souza-e-Silva, U., and Paulson, J.C. (1982a) Purification of a Galβ1-4GlcNAc α-2-6 sialyltransferase and a Galβ1-3(4)GlcNAc α2-3 sialyltransferase to homogeneity from rat liver. J. Biol. Chem., 257, 13835-13844.
33. Weinstein, J., de Souza-e-Silva, U. and Paulson, J.C. (1982b) Sialylation of glycoprotein oligosaccharides N-linked to asparagines. Enzymatic characterization of a Galβ1-3(4)GlcNAc α2-3 sialyltransferase and a Galβ1-4GlcNAc α2-6 sialyltransferase from rat liver. J. Biol. Chem., 257, 13845-13853.
34. Wen, D.X., Livingston, B.D., Medzihradszky, K.F., Kelm, S., Burlingame, A.L., and Paulson, J.C. (1992) Primary structure of Gal-b-1,3(4)GlcNAc a-2,3 sialyltransferase determined by mass-spectrometry sequence-analysis and molecular-cloning. Evidence for a protein motif in the sialyltransferase gene family. J. Biol. Chem., 267, 21011-21019.