Skip Navigation


Glycobiology Advance Access originally published online on December 15, 2004
Glycobiology 2005 15(5):463-474; doi:10.1093/glycob/cwi028
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
15/5/463    most recent
cwi028v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (28)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Paschinger, K.
Right arrow Articles by Wilson, I. B. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Paschinger, K.
Right arrow Articles by Wilson, I. B. H.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Glycobiology vol. 15 no. 5 © Oxford University Press 2004; all rights reserved.

Fucosyltransferase substrate specificity and the order of fucosylation in invertebrates

Katharina Paschinger, Erika Staudacher, Ute Stemmer, Gustáv Fabini1 and Iain B. H. Wilson2

Department für Chemie der Universität für Bodenkultur, Muthgasse 18, 1190 Wien, Austria

1 Present address: Octapharma Pharmazeutika Produktionsges. m.b.H., A-1100 Wien

2 To whom correspondence should be addressed: e-mail: iain.wilson{at}boku.ac.at

Received on July 7, 2004; revised on November 2, 2004; accepted on December 10, 2004

Core {alpha}1,6-fucosylation is a conserved feature of animal N-linked oligosaccharides being present in both invertebrates and vertebrates. To prove that the enzymatic basis for this modification is also evolutionarily conserved, cDNAs encoding the catalytic regions of the predicted Caenorhabditis elegans and Drosophila melanogaster homologs of vertebrate {alpha}1,6-fucosyltransferases (E.C. 2.4.1.68) were engineered for expression in the yeast Pichia pastoris. Recombinant forms of both enzymes were found to display core fucosyltransferase activity as shown by a variety of methods. Unsubstituted nonreducing terminal GlcNAc residues appeared to be an obligatory feature of the substrate for the recombinant Caenorhabditis and Drosophila {alpha}1,6-fucosyltransferases, as well as for native Caenorhabditis and Schistosoma mansoni core {alpha}1,6-fucosyltransferases. On the other hand, these {alpha}1,6-fucosyltransferases could not act on N-glycopeptides already carrying core {alpha}1,3-fucose residues, whereas recombinant Drosophila and native Schistosoma core {alpha}1,3-fucosyltransferases were able to use core {alpha}1,6-fucosylated glycans as substrates. Lewis-type fucosylation was observed with native Schistosoma extracts and could take place after core {alpha}1,3-fucosylation, whereas prior Lewis-type fucosylation precluded the action of the Schistosoma core {alpha}1,3-fucosyltransferase. Overall, we conclude that the strict order of fucosylation events, previously determined for fucosyltransferases in crude extracts from insect cell lines (core {alpha}1,6 before core {alpha}1,3), also applies for recombinant Drosophila core {alpha}1,3- and {alpha}1,6-fucosyltransferases as well as for core fucosyltransferases in schistosomal egg extracts.

Key words: Caenorhabditis / Drosophila / fucosyltransferase / Schistosoma


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
A. Titz, A. Butschi, B. Henrissat, Y.-Y. Fan, T. Hennet, E. Razzazi-Fazeli, M. O. Hengartner, I. B. H. Wilson, M. Kunzler, and M. Aebi
Molecular Basis for Galactosylation of Core Fucose Residues in Invertebrates: IDENTIFICATION OF CAENORHABDITIS ELEGANS N-GLYCAN CORE {alpha}1,6-FUCOSIDE {beta}1,4-GALACTOSYLTRANSFERASE GALT-1 AS A MEMBER OF A NOVEL GLYCOSYLTRANSFERASE FAMILY
J. Biol. Chem., December 25, 2009; 284(52): 36223 - 36233.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. Mollicone, S. E. H. Moore, N. Bovin, M. Garcia-Rosasco, J.-J. Candelier, I. Martinez-Duncker, and R. Oriol
Activity, Splice Variants, Conserved Peptide Motifs, and Phylogeny of Two New {alpha}1,3-Fucosyltransferase Families (FUT10 and FUT11)
J. Biol. Chem., February 13, 2009; 284(7): 4723 - 4738.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
T. Takeuchi, K. Hayama, J. Hirabayashi, and K.-i. Kasai
Caenorhabditis elegans N-glycans containing a Gal-Fuc disaccharide unit linked to the innermost GlcNAc residue are recognized by C. elegans galectin LEC-6
Glycobiology, November 1, 2008; 18(11): 882 - 890.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
Q. Zheng, I. Van Die, and R. D Cummings
A novel {alpha}1,2-fucosyltransferase (CE2FT-2) in Caenorhabditis elegans generates H-type 3 glycan structures
Glycobiology, April 1, 2008; 18(4): 290 - 302.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Gutternigg, D. Kretschmer-Lubich, K. Paschinger, D. Rendic, J. Hader, P. Geier, R. Ranftl, V. Jantsch, G. Lochnit, and I. B. H. Wilson
Biosynthesis of Truncated N-Linked Oligosaccharides Results from Non-orthologous Hexosaminidase-mediated Mechanisms in Nematodes, Plants, and Insects
J. Biol. Chem., September 21, 2007; 282(38): 27825 - 27840.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
K. Nguyen, I. van Die, K. M Grundahl, Z. S Kawar, and R. D Cummings
Molecular cloning and characterization of the Caenorhabditis elegans {alpha}1,3-fucosyltransferase family
Glycobiology, June 1, 2007; 17(6): 586 - 599.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
H. Ihara, Y. Ikeda, S. Toma, X. Wang, T. Suzuki, J. Gu, E. Miyoshi, T. Tsukihara, K. Honke, A. Matsumoto, et al.
Crystal structure of mammalian {alpha}1,6-fucosyltransferase, FUT8
Glycobiology, May 1, 2007; 17(5): 455 - 466.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
B. Ma, J. L. Simala-Grant, and D. E. Taylor
Fucosylation in prokaryotes and eukaryotes
Glycobiology, December 1, 2006; 16(12): 158R - 184R.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Paschinger, M. Hackl, M. Gutternigg, D. Kretschmer-Lubich, U. Stemmer, V. Jantsch, G. Lochnit, and I. B. H. Wilson
A Deletion in the Golgi {alpha}-Mannosidase II Gene of Caenorhabditis elegans Results in Unexpected Non-wild-type N-Glycan Structures
J. Biol. Chem., September 22, 2006; 281(38): 28265 - 28277.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
M. S. Duffy, H. R. Morris, A. Dell, J. A. Appleton, and S. M. Haslam
Protein glycosylation in Parelaphostrongylus tenuis--first description of the Gal{alpha}1-3Gal sequence in a nematode
Glycobiology, September 1, 2006; 16(9): 854 - 862.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
A. J. Hanneman, J. C. Rosa, D. Ashline, and V. N. Reinhold
Isomer and glycomer complexities of core GlcNAcs in Caenorhabditis elegans
Glycobiology, September 1, 2006; 16(9): 874 - 890.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
M. Crispin, D. J. Harvey, V. T. Chang, C. Yu, A. R. Aricescu, E. Y. Jones, S. J. Davis, R. A. Dwek, and P. M. Rudd
Inhibition of hybrid- and complex-type glycosylation reveals the presence of the GlcNAc transferase I-independent fucosylation pathway
Glycobiology, August 1, 2006; 16(8): 748 - 756.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Sarkar, P. A. Leventis, C. I. Silvescu, V. N. Reinhold, H. Schachter, and G. L. Boulianne
Null Mutations in Drosophila N-Acetylglucosaminyltransferase I Produce Defects in Locomotion and a Reduced Life Span
J. Biol. Chem., May 5, 2006; 281(18): 12776 - 12785.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. Leonard, D. Rendic, C. Rabouille, I. B. H. Wilson, T. Preat, and F. Altmann
The Drosophila fused lobes Gene Encodes an N-Acetylglucosaminidase Involved in N-Glycan Processing
J. Biol. Chem., February 24, 2006; 281(8): 4867 - 4875.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. Rendic, A. Linder, K. Paschinger, N. Borth, I. B. H. Wilson, and G. Fabini
Modulation of Neural Carbohydrate Epitope Expression in Drosophila melanogaster Cells
J. Biol. Chem., February 10, 2006; 281(6): 3343 - 3353.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.