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J. Biol. Chem., Vol. 277, Issue 42, 39823-39832, October 18, 2002
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From the Here we report the discovery of a unique
fucosyltransferase (FT) in Caenorhabditis elegans. In
studying the activities of FTs in extracts of adult C. elegans, we detected activity toward the unusual disaccharide
acceptors Gal
Molecular Cloning and Characterization of a Novel
1,2-Fucosyltransferase (CE2FT-1) from Caenorhabditis
elegans*
§,§
Department of Biochemistry and Molecular
Biology and the § Oklahoma Center for Medical Glycobiology,
University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma
73104 and the ¶ Department of Molecular Cell Biology, VU
University Medical Center, Van der Boechorststraat 7, 1081 BT Amsterdam, The Netherlands
1-4Xyl-R and Gal1-6GlcNAc-R to generate products
with the general structure Fuc
1-2Gal1-R. We identified a gene
encoding a unique 1,2FT (designated CE2FT-1), which
contains an open reading frame encoding a predicted protein of 355 amino acids with the type 2 topology and domain structure typical of
other glycosyltransferases. The predicted cDNA for CE2FT-1 has very
low identity (5-10%) at the amino acid level to 1,2FT sequences in
humans, rabbits, and mice. Recombinant CE2FT-1 expressed in human 293T
cells has high 1,2FT activity toward the simple acceptor
Gal-O-phenyl acceptor to generate Fuc1-2Gal-R,
which in this respect resembles mammalian 1,2FTs. However, CE2FT-1
is otherwise completely different from known 1,2FTs in its acceptor
specificity, since it is unable to fucosylate either Gal1-4Glc-R
or free lactose and prefers the unusual acceptors Gal1-4Xyl-R
and Gal1-6GlcNAc-R. Promoter analysis of the CE2FT-1 gene using green fluorescent protein reporter constructs demonstrates that CE2FT-1 is expressed in single cells of early stage embryos and
exclusively in the 20 intestinal cells of
L1-L4 and adult worms. These and other results
suggest that multiple fucosyltransferase genes in C. elegans may encode enzymes with unique activities, expression,
and developmental roles.
*
This work was supported by National Institutes of Health
Grant RO1 HD037549 (to R. D. C.).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of
Biochemistry and Molecular Biology, University of Oklahoma Health
Sciences Center, 975 N.E. 10th St., BRC417, Oklahoma City, OK 73104. Tel.: 405-271-2481; Fax: 405-271-3910; E-mail:
richard-cummings@ouhsc.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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